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Journal articles on the topic 'Proteine allergeniche'
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1
Toomer, Ondulla, Andrew Do, Marion Pereira, and Kristina Williams. "The effect of simulated gastric and intestinal digestion on temporal stability and immunoreactivity of peanut, almond and pine nut protein allergens (P6206)." Journal of Immunology 190, no. 1_Supplement (May 1, 2013): 62.2. http://dx.doi.org/10.4049/jimmunol.190.supp.62.2.
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Abstract Current models of digestibility utilize pepsin stability to assess the safety of allergenic versus non-allergenic food proteins. Dietary protein digestion in vivo, however, requires acid denaturation and protease cleavage by pepsin, trypsin, and/or chymotrypsin. The ability of this approach to identify food protein stability in the mammalian gut may be limited. We determined the temporal stability and immunoreactivity of almond, pine nut, and peanut allergenic proteins using simulated physiologic gastric and intestinal digestive conditions in vitro. Gel electrophoresis and immunoblot analyses were used to determine protein stability and immunoreactivity, respectively. Peanut, almond, and pine nut proteins were pepsin- and pancreatin-stable, and immunoreactive for up to 1 h after initiating digestion. Moreover, successive acid denaturation, and pepsin and pancreatin cleavage were necessary to hydrolyze these allergenic proteins and reduce their IgG and IgE-binding capacity, which suggests that digestibility models must be improved for more accurate safety assessment of food allergens.
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Boukil, Abir, Véronique Perreault, Julien Chamberland, Samir Mezdour, Yves Pouliot, and Alain Doyen. "High Hydrostatic Pressure-Assisted Enzymatic Hydrolysis Affect Mealworm Allergenic Proteins." Molecules 25, no. 11 (June 9, 2020): 2685. http://dx.doi.org/10.3390/molecules25112685.
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Edible insects have garnered increased interest as alternative protein sources due to the world’s growing population. However, the allergenicity of specific insect proteins is a major concern for both industry and consumers. This preliminary study investigated the capacity of high hydrostatic pressure (HHP) coupled to enzymatic hydrolysis by Alcalase® or pepsin in order to improve the in vitro digestion of mealworm proteins, specifically allergenic proteins. Pressurization was applied as pretreatment before in vitro digestion or, simultaneously, during hydrolysis. The degree of hydrolysis was compared between the different treatments and a mass spectrometry-based proteomic method was used to determine the efficiency of allergenic protein hydrolysis. Only the Alcalase® hydrolysis under pressure improved the degree of hydrolysis of mealworm proteins. Moreover, the in vitro digestion of the main allergenic proteins was increased by pressurization conditions that were specifically coupled to pepsin hydrolysis. Consequently, HHP-assisted enzymatic hydrolysis represents an alternative strategy to conventional hydrolysis for generating a large amount of peptide originating from allergenic mealworm proteins, and for lowering their immunoreactivity, for food, nutraceutical, and pharmaceutical applications.
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Gangur, Venu, Sitaram Parvataneni, Babu Gonipeta, and Rob Tempelman. "Immune response and clinical reaction to food proteins with high vs. low/non allergenic potential in an adjuvant-free mouse model (79.17)." Journal of Immunology 182, no. 1_Supplement (April 1, 2009): 79.17. http://dx.doi.org/10.4049/jimmunol.182.supp.79.17.
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Abstract Predicting allergenic potential of novel proteins present in foods such as genetically modified foods is a major challenge facing regulatory agencies and biotech industries. Here we tested the hypothesis that the adjuvant-free mouse model that we have previously reported (Birmingham et al Int Arch Allergy Immunol 2007;144(3):203-10) will be useful to distinguish human food proteins with high vs. low/non allergenic potential. Three readouts were used for testing food allergenicity: 1) systemic specific IgE antibody response to transdermal food protein exposure; 2) clinical symptoms of systemic anaphylaxis to oral food protein challenge; and 3) drop in rectal temperature (hypothermia) to oral food protein challenge. The following food proteins were tested for allergenicity: food proteins with high allergenic potential (cashew nut, milk), food proteins with low/non allergenic potential (kidney bean, Pinto bean); and a food protein with unknown history of allergenicity (Amaranth seed protein). We found that whereas, both cashew nut and milk tested positive for all three readouts of allergenicity, Pinto bean and kidney bean although induced specific IgE antibodies, did not cause systemic anaphylaxis and hypothermia. Interestingly, Amaranth seed protein induced not only a robust IgE response but also elicited clinical symptoms of systemic anaphylaxis as well as hypothermia. These data demonstrate that: 1) further testing with additional food proteins is necessary to evaluate the predictive utility of this mouse model for allergenicity testing; and 2) further studies are needed to evaluate the relationship between circulating food specific IgE antibodies and clinical sensitization for oral food induced systemic anaphylaxis. Funding: US EPA STAR Grant#R833133
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TIVSIZ, Delal, Ibrahim Halil KILIC, and Isik Didem KARAGOZ. "Allergenic Proteins of Tilia Cordata." Eurasia Proceedings of Science Technology Engineering and Mathematics 12 (December 31, 2021): 62–66. http://dx.doi.org/10.55549/epstem.103837000000.
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Pollen forms large amount of aeroallergens in the atmosphere that spread through winds and insects. Allergenic pollen grains are water-soluble glycoprotein or protein bioparticles and its weight is approximately 5-80 kDa. There are many factors that cause allergies and considering the recently changing climatic conditions and their ability to spread over a wide geographical areas, pollens are among the major factors causing allergies. In this study, it was aimed to detect potential allergen pollen proteins of Tilia cordata which is a potent allergen. The pollen samples belonging to T. cordata were dried and then they were separated with sieve. Acetone washing and dialysis processes were applied to purificate pollen. Afterwards, the amount of protein in the pollens of T. cordata was determined by the bicinchoninic acid (BCA) method. In order to detect allergen proteins, gel runing was performed by SDS-PAGE. Silver staining method was applied to make visible the bands of T. cordata pollen proteins obtained from the gel. Five different allergenic pollen proteins, weights 10, 23, 40, 50 and 80 kDa, were detected as a result of SDS-PAGE. This is the second study in the literature related with the identification of T. cordata allergenic proteins and we showed two different protein bands compared with the former study result. Besides, our study is original in this perspective. We think that this study contributes to the literature on allergenic proteins of T. cordata and should be supported by future studies.
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TIVSIZ, Delal, Ibrahim Halil KILIC, and Isik Didem KARAGOZ. "Allergenic Proteins of Tilia Cordata." Eurasia Proceedings of Science Technology Engineering and Mathematics 12 (December 31, 2021): 62–66. http://dx.doi.org/10.55549/epstem.1038370.
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Pollen forms large amount of aeroallergens in the atmosphere that spread through winds and insects. Allergenic pollen grains are water-soluble glycoprotein or protein bioparticles and its weight is approximately 5-80 kDa. There are many factors that cause allergies and considering the recently changing climatic conditions and their ability to spread over a wide geographical areas, pollens are among the major factors causing allergies. In this study, it was aimed to detect potential allergen pollen proteins of Tilia cordata which is a potent allergen. The pollen samples belonging to T. cordata were dried and then they were separated with sieve. Acetone washing and dialysis processes were applied to purificate pollen. Afterwards, the amount of protein in the pollens of T. cordata was determined by the bicinchoninic acid (BCA) method. In order to detect allergen proteins, gel runing was performed by SDS-PAGE. Silver staining method was applied to make visible the bands of T. cordata pollen proteins obtained from the gel. Five different allergenic pollen proteins, weights 10, 23, 40, 50 and 80 kDa, were detected as a result of SDS-PAGE. This is the second study in the literature related with the identification of T. cordata allergenic proteins and we showed two different protein bands compared with the former study result. Besides, our study is original in this perspective. We think that this study contributes to the literature on allergenic proteins of T. cordata and should be supported by future studies.
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Naneva, L., M. Nedyalkova, S. Madurga, F. Mas, and V. Simeonov. "Applying Discriminant and Cluster Analyses to Separate Allergenic from Non-allergenic Proteins." Open Chemistry 17, no. 1 (June 3, 2019): 401–7. http://dx.doi.org/10.1515/chem-2019-0045.
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AbstractAs a result of increased healthcare requirements and the introduction of genetically modified foods, the problem of allergies is becoming a growing health problem. The concept of allergies has prompted the use of new methods such as genomics and proteomics to uncover the nature of allergies. In the present study, a selection of 1400 food proteins was analysed by PLS-DA (Partial Least Square-based Discriminant Analysis) after suitable transformation of structural parameters into uniform vectors. Then, the resulting strings of different length were converted into vectors with equal length by Auto and Cross-Covariance (ACC) analysis. Hierarchical and non-hierarchical (K-means) Cluster Analysis (CA) was also performed in order to reach a certain level of separation within a small training set of plant proteins (16 allergenic and 16 non-allergenic) using a new three-dimensional descriptor based on surface protein properties in combination with amino acid hydrophobicity scales. The novelty of the approach in protein differentiation into allergenic and non-allergenic classes is described in the article.The general goal of the present study was to show the effectiveness of a traditional chemometric method for classification (PLS–DA) and the options of Cluster Analysis (CA) to separate by multivariate statistical methods allergenic from non-allergenic proteins.
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Calinoiu, Lavinia Florina, Dan Cristian Vodnar, and Carmen Socaciu. "The Reactivity and Allergenic Potential of Hazelnut Peptides." Bulletin of University of Agricultural Sciences and Veterinary Medicine Cluj-Napoca. Food Science and Technology 70, no. 1 (November 13, 2013): 25. http://dx.doi.org/10.15835/buasvmcn-fst:9506.
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The aim of this paper was to focus on proteins present in some food products, like hazelnuts and to investigate their allergenic potential. Several techniques were used to characterize these extracted proteins, with respect to their composition, degradability by digestive proteolytic enzymes and their reactivity with specific antibodies. It was important to analyse which proteins were present in the hazelnuts, to see if there were proteins present to trigger an allergic reaction and if the digestion enzymes trypsin and pepsin influence the presence of the (allergic) protein compounds. Allergies to tree nuts and seeds can cause life-threatening and sometimes fatal reactions. To examine the properties of Hazelnut protein it was important to solubilize it by extraction. After extraction, it was investigated how hazelnut protein can be modified by proteases and what the effect was on the immune reaction. The Bradford method is a fast and sensitive method to determine the concentration of soluble protein. When the Bradford reagent (Coomassie Brilliant Blue) binds to the protein, the colour changes from red to purple and the absorption maximum changes from 495 to 595 nm. The value obtained as the final concentration of proteins was 7.3495. SDS-PAGE is a method to separate mixtures of proteins by electrophoresis. Protein molecules are negatively charged by binding of SDS molecules; subsequently they are separated in an electric field. Their differences in size (molecular weight) leads to separation. In this case the method is used to follow proteolytic degradation of hazelnut proteins (allergens) by intestinal proteases (trypsin, pepsin). A different, more specific and sensitive method is immunoblotting (Western Blot) in which the SDS-PAGE separated proteins are transferred from the gel to a membrane and specific antibodies are used in a series of reactions to visualize specific allergens on this membrane. The remarked spots represented a positive identification of allergenic proteins. This means that peptide fragments of various size, produced during the digestion of a protein can still be immunological active. As it was shown there was still reactivity between proteins and specific antibodies. The Dot Blot is a simple immunoblotting technique used to detected specific proteins in a mixture of different proteins and/or other molecules. No separation technique prior to the actual immuno-detection is necessary. Also, Dot Blot confirmed the presence of allergenic proteins made visible through the light spots on the membrane.
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Sakai, Shinobu, Ryosuke Nakamaura, Rika Nakamaura, Reiko Adachi, and Reiko Teshima. "Food allergenic proteins in lactose as the pharmaceutical excipient (P6222)." Journal of Immunology 190, no. 1_Supplement (May 1, 2013): 62.10. http://dx.doi.org/10.4049/jimmunol.190.supp.62.10.
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Abstract Most drugs contain pharmaceutical excipients which are pharmacologically inactive substances used as vehicles to deliver the active ingredients of a medication. Some of these pharmaceutical excipients are produced from foods containing allergenic proteins (e.g., milk, egg, peanut, soybean, and sesame) and removing these completely from the excipients is difficult. Therefore, if individuals with food allergies consume drugs containing allergenic food-derived excipients, they are at risk for developing specific allergic symptoms. We determined the levels of total protein in lactose found in pharmaceutical excipients and ethical drugs known to contain lactose by spectrophotometric analyses. The level of total protein in lactose was approximately 1 mg/g. We also determined the levels of allergenic proteins in lactose using commercial enzyme-linked immunosorbent assay systems. The milk proteins in lactose were detected in the range of 1.4-13.1 μg/g. Furthermore, we performed a luciferase-based in vitro elicitation test (EXiLE test) in addition to western-blot analysis using the sera from patients with milk allergies in order to examine the allergenicity of protein residues in lactose. The result of the EXiLE test indicated that the protein residues in lactose have the ability to crosslink human FcϵRI on mast cells.
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Dearman, Rebecca J., and Ian Kimber. "Characterisation of immune responses to food allergens in mice." Proceedings of the Nutrition Society 64, no. 4 (November 2005): 426–33. http://dx.doi.org/10.1079/pns2005456.
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There is considerable interest in the development and evaluation of approaches for the safety assessment of novel foods, and in particular in methods for characterisation of allergenic potential. One strategy that has found favour is a tiered approach in which the potential of novel proteins to induce allergic sensitisation is assessed based on considerations of stability of the protein in a simulated gastric juice and homology with, or structural similarity to, known allergens. Linked to such an approach may be evaluation of serological identity with proteins known to cause allergic disease. With the aim of supplementing such approaches with a more direct measurement of potential allergenic activity, attempts have been made to characterise the quality of immune responses elicited in BALB/c strain mice. Such evaluations comprise measurement of IgG and IgE antibody production and (to a lesser extent) of induced cytokine expression patterns. Investigations to date suggest that in mice proteins provoke variable immune responses, those with the potential to cause allergic sensitisation stimulating IgE (and IgG) antibody production. In contrast, non-allergenic, but nevertheless immunogenic, proteins are associated with IgG antibody responses in the absence of marked IgE production. Consistent with the selective activation of selective type 2 T lymphocyte responses, exposure of mice to allergenic protein is associated with preferential expression of IL-4, -5, -10 and -13. Collectively these data suggest that characterisation of the nature of immune response induced in mice by proteins may provide a useful adjunct or alternative to current strategies for the assessment of allergenic potential.
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Pantoja-Uceda, D., M. Bruix, J. Santoro, M. Rico, R. Monsalve, and M. Villalba. "Solution structure of allergenic 2 S albumins." Biochemical Society Transactions 30, no. 6 (November 1, 2002): 919–24. http://dx.doi.org/10.1042/bst0300919.
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The NMR solution structures at different levels of refinement of three different 2 S albumin seed proteins, the recombinant pronapin precursor from Brassica napus, the recombinant RicC3 from Ricinus communis and the methionine-rich protein from sunflower (Helianthus annuus), are described. The resulting common structure consists of a bundle of five α-helices, folded in a right-handed superhelix. The structure is very similar to that of other plant proteins: the hydrophobic protein from soybean, non-specific lipid transfer proteins and amylase/trypsin inhibitors. Analogies and differences in the structures of these families, as well as their possible relationship to allergenicity, are discussed.
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Ewart, Fiona A. "Making Milk Less Allergenic." STEM Fellowship Journal 4, no. 1 (April 1, 2018): 27–32. http://dx.doi.org/10.17975/sfj-2018-008.
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The formation of stable aggregates by food proteins is associated with allergenicity. In particular, amyloid formation by the fish allergen parvalbumin was recently shown to favor IgE binding and subsequent allergic recognition. Therefore, reducing amyloid content in an allergenic food might offer a direct way to make that food less likely to trigger an allergy. In this project, protein aggregation and amyloid formation were studied in milk using gel electrophoresis and fluorescence-based assays. The results suggested that ordinary pasteurized milk from the grocery store contained protein aggregates and specifically amyloid. Processing the milk as normally done during food preparation did not appreciably affect general aggregation or amyloid formation. However, the addition of some polyphenol-containing food products to the milk appeared to result in reduced amyloid levels. Moreover, cranberry juice also appeared to reduce amyloid formation by the milk protein casein. These results suggest that the addition of cranberry or other polyphenol-rich foods to milk products for young children may reduce the risk of milk allergy development by diminishing protein aggregation.
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Wolff, N., U. Cogan, H. Zuckerman, N. Karin, Y. Levy, Y. E Krasik, J. Felsteiner, R. Reifen, and S. Yannai. "Decrease of the allergenic activity of foods by shock waves." Czech Journal of Food Sciences 22, SI - Chem. Reactions in Foods V (January 1, 2004): S36—S39. http://dx.doi.org/10.17221/10607-cjfs.
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Food allergy significantly affects the life-quality for many people worldwide and is life-threatening in extreme cases. In recent years the incidence of this disease shows a gradual increase in many countries. It is a well-established fact that common food-processing operations involving heat treatments fail to significantly decrease the allergenic reactivity of foods. Furthermore, allergenic proteins are remarkably resistant to proteolysis by digestive enzymes and often remain intact after passing through the gastrointestinal tract. The tested materials were protein extracts from sesame seeds, milk and peanuts, or isolated proteins from the same sources. Treatments investigated included application of 6 to 10 pulses of high-frequency acoustic shock waves, lasting a few microseconds. The treated samples were tested in vitro by Western blotting with sera from humans diagnosed to be allergic to the food in question, and in vivo by measuring the IgE levels produced in young Brown Norway rats exposed to the tested proteins by sensitisation through i.p. injection, or by feeding for up to 6 weeks, using direct and indirect ELISA. The treatments markedly decreased or completely eliminated the allergenic reactivity of the foods, as evidenced by the assays used.
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Vicente, Fatima, Africa Sanchiz, Rosa Rodríguez-Pérez, Maria Pedrosa, Santiago Quirce, Joseph Haddad, Colette Besombes, Rosario Linacero, Karim Allaf, and Carmen Cuadrado. "Influence of Instant Controlled Pressure Drop (DIC) on Allergenic Potential of Tree Nuts." Molecules 25, no. 7 (April 10, 2020): 1742. http://dx.doi.org/10.3390/molecules25071742.
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Pistachio and cashew contain allergenic proteins, which causes them to be removed from the diet of allergic people. Previous studies have demonstrated that food processing (thermal and non-thermal) can produce structural and/or conformational changes in proteins by altering their allergenic capacity. In this study, the influence of instant controlled pressure drop (DIC) on pistachio and cashew allergenic capacity has been studied. Western blot was carried out using IgG anti-11S and anti-2S and IgE antibodies from sera of patients sensitized to pistachio and cashew. DIC processing causes changes in the electrophoretic pattern, reducing the number and intensity of protein bands, as the pressure and temperature treatment increment, which results in a remarkable decrease in detection of potentially allergenic proteins. The harshest conditions of DIC (7 bar, 120 s) markedly reduce the immunodetection of allergenic proteins, not only by using IgG (anti 11S and anti 2S) but also when IgE sera from sensitized patients were used for Western blots. Such immunodetection is more affected in pistachio than in cashew nuts, but is not completely removed. Therefore, cashew proteins are possibly more resistant than pistachio proteins. According these findings, instant controlled pressure drop (DIC) can be considered a suitable technique in order to obtain hypoallergenic tree nut flour to be used in the food industry.
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Shamsbiranvand, Mohammad-Hosein, Ali Khodadadi, Mohammad-Ali Assarehzadegan, Seyed Hamid Borsi, and Akram Amini. "Immunochemical Characterization of Acacia Pollen Allergens and Evaluation of Cross-Reactivity Pattern with the Common Allergenic Pollens." Journal of Allergy 2014 (May 18, 2014): 1–7. http://dx.doi.org/10.1155/2014/409056.
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Pollen from the Acacia has been reported as an important source of pollinosis in tropical and subtropical regions of the world. The aim of this study was to characterize the IgE binding protein of Acacia farnesiana pollen extract and evaluate cross-reactivity with the most allergenic pollens. In this study, pollen extract was fractionated by SDS-PAGE and the allergenic profile was determined by IgE-immunoblotting and specific ELISA using forty-two Acacia allergic patients. Potential cross-reactivity among Acacia and selected allergenic plants was evaluated with ELISA and immunoblotting inhibition experiments. There were several resolved protein fractions on SDS-PAGE which ranged from 12 to 85 kDa. Several allergenic protein bands with molecular weights approximately between 12 and 85 kDa were recognized by IgE-specific antibodies from Acacia allergic patients in the immunoblot assay. The inhibition by the Prosopis juliflora pollen extract was more than those by other pollen extracts. Moreover, the wheal diameters generated by the Acacia pollen extract were highly correlated with those of P. juliflora pollen extracts. The findings suggest that several proteins such as 15, 23, 45, and 50 kDa proteins could be used as diagnostic and therapeutic reagents for patients allergic to A. farnesiana and P. juliflora.
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Scheib, Holger, K. Anne-Isola Nekaris, Johanna Rode-Margono, Lotten Ragnarsson, Kate Baumann, James S. Dobson, Wirdateti Wirdateti, et al. "The Toxicological Intersection between Allergen and Toxin: A Structural Comparison of the Cat Dander Allergenic Protein Fel d1 and the Slow Loris Brachial Gland Secretion Protein." Toxins 12, no. 2 (January 28, 2020): 86. http://dx.doi.org/10.3390/toxins12020086.
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Slow lorises are enigmatic animal that represent the only venomous primate lineage. Their defensive secretions have received little attention. In this study we determined the full length sequence of the protein secreted by their unique brachial glands. The full length sequences displayed homology to the main allergenic protein present in cat dander. We thus compared the molecular features of the slow loris brachial gland protein and the cat dander allergen protein, showing remarkable similarities between them. Thus we postulate that allergenic proteins play a role in the slow loris defensive arsenal. These results shed light on these neglected, novel animals.
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Mohamad Yadzir, Zailatul Hani, Rosmilah Misnan, Faizal Bakhtiar, Noormalin Abdullah, and Shahnaz Murad. "Tropomyosin and Actin Identified as Major Allergens of the Carpet Clam (Paphia textile) and the Effect of Cooking on Their Allergenicity." BioMed Research International 2015 (2015): 1–6. http://dx.doi.org/10.1155/2015/254152.
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Objectives. To identify the major allergenic proteins of clam (Paphia textile) and to investigate the effect of different cooking methods on the allergenicity of these identified proteins.Methods. Clam protein extracts were separated by denaturing polyacrylamide gel electrophoresis. IgE reactive proteins were then analyzed by immunoblotting with sera from patients with positive skin prick tests (SPT) to the raw clam extract. Mass spectrometry was used to identify the major allergenic proteins of this clam.Results. Raw extract showed 12 protein bands (18–150 kDa). In contrast, fewer protein bands were seen in the boiled extract; those ranging from 40 to 150 kDa were denatured. The protein profiles were similarly altered by frying or roasting. The immunoblots of raw and boiled extracts yielded 10 and 2 IgE-binding proteins, respectively. The fried and roasted extracts showed only a single IgE-binding protein at 37 kDa. Mass spectrometry analysis of the 37 and 42 kDa major allergens indicated that these spots were tropomyosin and actin, respectively.Conclusion. The two major allergens ofPaphia textilewere identified as the thermostable tropomyosin and a new thermolabile allergen actin.
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Gervazieva, V. B., P. V. Samoylikov, V. M. Berzhets, L. A. Pishchulina, S. A. Mazurina, and A. A. Dudorova. "Allergenic extracts from natural and genetically modified soybean." Russian Journal of Allergy 15, no. 5 (December 15, 2018): 41–46. http://dx.doi.org/10.36691/rja125.
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Background. The wide spread of soybeans both natural and genetically modified (GM) in agriculture and food industry arises a question about the safety of its use, as soy is the most common food allergen among leguminous plants. Meanwhile, there are no registered domestic diagnostic allergens from soybeans in Russia. Objective. The aim of this study was to obtain allergenic extracts from natural and GM soybeans resistant to the herbicide «Roundup» and evaluate their biochemical and allergenic properties. Methods. Soybean extracts were obtained by the Evans-Kok method. The amount of protein nitrogen was determined by the Nessler method. The protein composition of the soybean was determined by the SDSPAGE. Specific activity was assessed in the reaction of NDTK. Allergenic activity was assessed in ELISA according to the sIgE levels to soy in the sera of patients with food allergy. Results. The protein fractions corresponding to known allergens weare revealed by SDS-PAGE in the samples of extracts: natural soybeans - Gly m 3, Gly m 5, and Gly m 6, while GM soybeans - Gly m Bd 30k. In addition to those proteins, in both extracts the 20 kD protein was clearly detected, which can correspond to the inhibitor of trypsin Kunitsa (Hor v 1, CMb, BDR). Allergenic soybean extracts bind sIgE and sIgG in the sera of patients with allergies. Conclusion. The obtained data confirm the high allergenic potential of extracts from natural soybeans, whereas the allergenic activity of GM soybeans extracts is reduced.
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Maurer-Stroh, Sebastian, Nora L. Krutz, Petra S. Kern, Vithiagaran Gunalan, Minh N. Nguyen, Vachiranee Limviphuvadh, Frank Eisenhaber, and G. Frank Gerberick. "AllerCatPro—prediction of protein allergenicity potential from the protein sequence." Bioinformatics 35, no. 17 (January 18, 2019): 3020–27. http://dx.doi.org/10.1093/bioinformatics/btz029.
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Abstract Motivation Due to the risk of inducing an immediate Type I (IgE-mediated) allergic response, proteins intended for use in consumer products must be investigated for their allergenic potential before introduction into the marketplace. The FAO/WHO guidelines for computational assessment of allergenic potential of proteins based on short peptide hits and linear sequence window identity thresholds misclassify many proteins as allergens. Results We developed AllerCatPro which predicts the allergenic potential of proteins based on similarity of their 3D protein structure as well as their amino acid sequence compared with a data set of known protein allergens comprising of 4180 unique allergenic protein sequences derived from the union of the major databases Food Allergy Research and Resource Program, Comprehensive Protein Allergen Resource, WHO/International Union of Immunological Societies, UniProtKB and Allergome. We extended the hexamer hit rule by removing peptides with high probability of random occurrence measured by sequence entropy as well as requiring 3 or more hexamer hits consistent with natural linear epitope patterns in known allergens. This is complemented with a Gluten-like repeat pattern detection. We also switched from a linear sequence window similarity to a B-cell epitope-like 3D surface similarity window which became possible through extensive 3D structure modeling covering the majority (74%) of allergens. In case no structure similarity is found, the decision workflow reverts to the old linear sequence window rule. The overall accuracy of AllerCatPro is 84% compared with other current methods which range from 51 to 73%. Both the FAO/WHO rules and AllerCatPro achieve highest sensitivity but AllerCatPro provides a 37-fold increase in specificity. Availability and implementation https://allercatpro.bii.a-star.edu.sg/ Supplementary information Supplementary data are available at Bioinformatics online.
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Uasuf, Carina Gabriela, Elisabetta De Angelis, Rocco Guagnano, Rosa Pilolli, Claudia D’Anna, Danilo Villalta, Ignazio Brusca, and Linda Monaci. "Emerging Allergens in Goji Berry Superfruit: The Identification of New IgE Binding Proteins towards Allergic Patients’ Sera." Biomolecules 10, no. 5 (April 29, 2020): 689. http://dx.doi.org/10.3390/biom10050689.
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The goji berry (Lycium barbarum L.) (GB) is gaining increasing attention with high consumption worldwide due to its exceptional nutritional value and medicinal benefits displayed in humans. Beyond their beneficial properties, GBs contain renowned allergenic proteins, and therefore deserve inclusion among the allergenic foods capable of inducing allergic reactions in sensitive consumers. GB allergy has been frequently linked to the panallergen lipid transfer protein (LTP), especially across the population of the Mediterranean area. Methods: In this study, we investigated the protein profile of GBs focusing on the most reactive proteins against immunoglobulins E (IgE) of allergic patients’ sera, as ascertained by immunoblot experiments. The protein spots displaying a clear reaction were excised, in-gel digested, and analyzed by liquid chromatography-tandem mass spectrometry (LC-MS/MS) followed by data searching against a restricted database for a reliable protein identification. Results: According to our data, three main spots were identified in GB extract as IgE binding proteins after immunoblot analysis. Some major proteins were identified and the three proteins that provided the highest reactivity were putatively attributed to vicilin and legumin proteins followed by a protein matching with 11S globulin belonging to the cupin superfamily. Finally, the whole GB protein extract was also submitted to bottom-up proteomics followed by a software-based database (DB) screening and a more exhaustive list of GB proteins was compiled.
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Aquino, Adriano, and Carlos Adam Conte-Junior. "A Systematic Review of Food Allergy: Nanobiosensor and Food Allergen Detection." Biosensors 10, no. 12 (November 29, 2020): 194. http://dx.doi.org/10.3390/bios10120194.
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Several individuals will experience accidental exposure to an allergen. In this sense, the industry has invested in the processes of removing allergenic compounds in food. However, accidental exposure to allergenic proteins can result from allergenic substances not specified on labels. Analysis of allergenic foods is involved in methods based on immunological, genetic, and mass spectrometry. The traditional methods have some limitations, such as high cost. In recent years, biosensor and nanoparticles combined have emerged as sensitive, selective, low-cost, and time-consuming techniques that can replace classic techniques. Nevertheless, each nanomaterial has shown a different potential to specific allergens or classes. This review used Preferred Reporting Items for Systematic Reviews and the Meta-Analysis guidelines (PRISMA) to approach these issues. A total of 104 articles were retrieved from a standardized search on three databases (PubMed, Scopus and Web of Science). The systematic review article is organized by the category of allergen detection and nanoparticle detection. This review addresses the relevant biosensors and nanoparticles as gold, carbon, graphene, quantum dots to allergen protein detection. Among the selected articles it was possible to notice a greater potential application on the allergic proteins Ah, in peanuts and gold nanoparticle-base as a biosensor. We envision that in our review, the association between biosensor and nanoparticles has shown promise in the analysis of allergenic proteins present in different food samples.
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Burzyńska, Marta, and Dorota Piasecka-Kwiatkowska. "A Review of Honeybee Venom Allergens and Allergenicity." International Journal of Molecular Sciences 22, no. 16 (August 4, 2021): 8371. http://dx.doi.org/10.3390/ijms22168371.
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Honeybee venom is a source of proteins with allergenic properties which can result in in various symptoms, ranging from local reactions through to systematic life-threatening anaphylaxis, or even death. According to the World Allergy Organization (WAO), honeybee venom allergy is one of the most common causes of anaphylaxis. Among the proteins present in honeybee venom, 12 protein fractions were registered by the World Health Organization’s Allergen Nomenclature Sub-Committee (WHO/IUIS) as allergenic. Most of them are highly immunogenic glycoproteins that cross-react with IgE and, as a consequence, may give false positive results in allergy diagnosis. Allergenic fractions are different in terms of molecular weight and biological activity. Eight of these allergenic fractions have also been identified in honey. This explains frequent adverse reactions after consuming honey in people allergic to venom and sheds new light on the causes of allergic symptoms in some individuals after honey consumption. At the same time, it also indicates the possibility of using honey as a natural source of allergen in specific immunotherapy.
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Chen, Chen Chi, Tzu Tai Lee, Chin Bin Hsu, Chien Wei Huang, and Bi Yu. "Associations of allergenic soybean proteins with piglet skin allergic reaction and application of polyclonal antibodies." Animal Production Science 51, no. 11 (2011): 1008. http://dx.doi.org/10.1071/an11142.
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A skin prick test was conducted to evaluate the skin allergic reaction of piglets caused by allergenic proteins contained in soybean meal. The data accumulated from subcutaneous piglet skin tissue indicated that allergenic proteins contained in soybean meal crude extracts, even in low dosage levels (7 μg), caused immunological redness and inflammation within 5 min. The dosages above 200 μg of β-conglycinin caused inflammation covering a larger area. The glycinin had less of an influence on skin allergenic reaction dosages than β-conglycinin did. The antibodies used for β-conglycinin and glycinin subunits did not exhibit cross-recognition to other subunits or Leguminosae members, such as green beans, lupins and red beans. The polyclonal antibodies further indicated that some allergenic proteins were present after examining soybean meal fermented products individually by Aspergillus or Lactobacillus. None of the allergenic proteins were detected in soybean meal underwent two-stage fermentation. The skin prick test was found to be a convenient method for evaluating the skin allergic reaction of soy allergenic proteins in piglets. The produced polyclonal antibodies are based on subunits of allergenic proteins and can be used to detect the allergenic proteins present in soya products and soybean meal fermented products.
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Yukalo, V. G., and K. Ye Datsyshyn. "Technology of low allergenic milk with whey proteins hydrolysate." Scientific Messenger of LNU of Veterinary Medicine and Biotechnologies 21, no. 92 (November 8, 2019): 14–18. http://dx.doi.org/10.32718/nvlvet-f9203.
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In recent years, there has been a steady increase in the number of various allergic diseases in children and adults. Clinical manifestations of allergic reactions can be observed almost from infancy, which is often associated with nutrition specificity. It is proved that one of the strongest milk allergens are the main whey fractions β-lactoglobulin and α-lactalbumin. One way to reduce allergies is to remove or completely replace whey proteins. Another way to reduce allergenicity is to use whey protein hydrolysates. In most cases, hydrolysates are obtained using cheap active proteolytic preparations. They usually have wide specificity, and the hydrolysates formed by them include short peptides with low allergenicity. Numerous biologically active peptides which have a positive effect on the organism are either lost or the possibility of their formation is reduced in such cases. A valuable source of such biologically active peptides is whey protein-precursors. Therefore, the purpose of the research is to develop a technology of low-allergenic milk with the preservation of natural biologically active peptides from whey proteins. The concentrate of natural casein was obtained in the result of the «milk-pectin-water» system dividing for creating a low-allergenic product. The fractional composition of the casein complex and milk whey proteins was analyzed by polyacrylamide gel electrophoresis. Whey protein concentrate was used as the substrate to obtain the hydrolysate. Proteolysis was performed with pancreatin at 37 °C and pH 7.9. The composition of the obtained hydrolysate was analyzed by gel filtration on Sephadex G-25. The peptides and polypeptides composition of hydrolysate was characterizated with the help of express electrophoresis. The technology of the proposed dairy product includes addition to a liquid concentrate of natural casein the whey protein hydrolysate obtained in physiological conditions. The results of electrophoretic and chromatographic researches indicate about the absence of main proteins allergens from milk whey in the product. This allows recommending it for the nutrition of people allergic to whey proteins.
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Nugraha, Roni, Thimo Ruethers, Elecia B. Johnston, Jennifer M. Rolland, Robyn E. O’Hehir, Sandip D. Kamath, and Andreas L. Lopata. "Effects of Extraction Buffer on the Solubility and Immunoreactivity of the Pacific Oyster Allergens." Foods 10, no. 2 (February 12, 2021): 409. http://dx.doi.org/10.3390/foods10020409.
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Despite recent technological advances, novel allergenic protein discovery is limited by their low abundance, often due to specific physical characteristics restricting their recovery during the extraction process from various allergen sources. In this study, eight different extraction buffers were compared for their ability to recover proteins from Pacific oyster (Crassostrea gigas). The protein composition was investigated using high resolution mass spectrometry. The antibody IgE-reactivity of each extract was determined using a pool of serum from five shellfish-allergic patients. Most of the investigated buffers showed good capacity to extract proteins from the Pacific oyster. In general, a higher concentration of proteins was recovered using high salt buffers or high pH buffers, subsequently revealing more IgE-reactive bands on immunoblotting. In contrast, low pH buffers resulted in a poor protein recovery and reduced IgE-reactivity. Discovery of additional IgE-reactive proteins in high salt buffers or high pH buffers was associated with an increase in allergen abundance in the extracts. In conclusion, increasing the ionic strength and pH of the buffer improves the solubility of allergenic proteins during the extraction process for oyster tissue. This strategy could also be applied for other difficult-to-extract allergen sources, thereby yielding an improved allergen panel for increased diagnostic efficiency.
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Mine, Y., and P. Rupa. "Fine mapping and structural analysis of immunodominant IgE allergenic epitopes in chicken egg ovalbumin." Protein Engineering Design and Selection 16, no. 10 (October 1, 2003): 747–52. http://dx.doi.org/10.1093/protein/gzg095.
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BIRMINGHAM, NEIL, SIRINART THANESVORAKUL, and VENU GANGUR. "Relative Immunogenicity of Commonly Allergenic Foods versus Rarely Allergenic and Nonallergenic Foods in Mice." Journal of Food Protection 65, no. 12 (December 1, 2002): 1988–91. http://dx.doi.org/10.4315/0362-028x-65.12.1988.
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Food allergies affect 6 to 8% of children and 2% of adults in the United States. For reasons that are not clear, eight types of food account for a vast majority (~90%) of food-induced hypersensitivity reactions. In this study, C57Bl/6 mice were used to test the hypothesis that commonly allergenic foods are intrinsically more immunogenic than rarely allergenic or nonallergenic foods in allergy-susceptible hosts. Groups of mice (n = 4 to 5) were injected intraperitoneally with the protein extracts (plus alum as an adjuvant) from chicken eggs, peanuts, almonds, filberts-hazelnuts, walnuts, soybeans, and wheat (commonly allergenic foods) and coffee, sweet potatoes, carrots, white potatoes, cherries, lettuce, and spinach (rarely allergenic and non-allergenic foods). Primary and secondary immune responses (as measured by specific IgG1 antibody serum levels) were measured by an enzyme-linked immunosorbent assay. Proteins from peanuts, almonds, filberts, sweet potatoes, cherries, and spinach elicited robust primary and/or secondary immune responses. Proteins from eggs, walnuts, and lettuce elicited poor primary responses but significant secondary responses. In contrast, wheat, soybeans, coffee, carrots, and white potatoes elicited barely detectable to poor primary and secondary immune responses. The order of the immunogenicity levels of these foods in mice is as follows: almonds = filberts > spinach (Rubisco) > peanuts ≥ sweet potatoes > cherries > lettuce > walnuts > chicken eggs > carrots ≥ white potatoes > wheat = coffee = soybeans. In summary, these data demonstrate for the first time that: (i) foods vary widely with regard to their relative immunogenicity in allergy-susceptible hosts and (ii) intrinsic immunogenicity in mice does not distinguish commonly allergenic foods from rarely allergenic or nonallergenic foods.
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Cárdenas-Torres, Feliznando Isidro, Cuauhtémoc Reyes-Moreno, Marcela de Jesús Vergara-Jiménez, Edith Oliva Cuevas-Rodríguez, Jorge Milán-Carrillo, Roberto Gutiérrez-Dorado, Jesús Gilberto Arámburo-Gálvez, Noé Ontiveros, and Francisco Cabrera-Chávez. "Assessing the Sensitizing and Allergenic Potential of the Albumin and Globulin Fractions from Amaranth (Amaranthus hypochondriacus) Grains before and after an Extrusion Process." Medicina 55, no. 3 (March 20, 2019): 72. http://dx.doi.org/10.3390/medicina55030072.
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Background: The first cases of food allergy to amaranth grain have recently been published. This pseudocereal is considered hypoallergenic, and there is scarce information about the allergenic potential of amaranth proteins, either before or after food processing. Objective: To evaluate, in a mouse model of food allergy, the sensitizing and allergenic potential of extruded and non-extruded albumin and globulin fractions from amaranth grains. Materials and Methods: Amaranth (Amaranthus hypochondriacus) flour was obtained and the albumin and globulin fractions isolated. These protein fractions were also obtained after flour extrusion. An intraperitoneal 28-day protocol was carried out to evaluate the sensitizing and allergenic potential of the proteins. The common and rarely allergenic proteins ovalbumin and potato acidic phosphatase were utilized as reference. Specific IgE and IgG antibodies were evaluated for all the proteins tested. Mast cell protease-1 (mMCP-1) responses were evaluated in serum samples collected after intragastric challenges with the proteins of interest. All serological evaluations were carried out using ELISA. Results: Mice were sensitized to the non-extruded albumin fraction from amaranth grains and to ovalbumin (p = 0.0045). The extrusion process of amaranth proteins abrogated the IgE responses triggered under non-extruded conditions (p = 0.0147). mMCP-1 responses were significantly detected in the group of mice sensitized to ovalbumin (p = 0.0138), but not in others. Conclusions: The non-extruded albumin fraction from amaranth has the potential to sensitize BALB/c mice, but this sensitizing potential fails to induce detectable serum levels of the mast cell degranulation marker mMCP-1 after intragastric challenges. Furthermore, the extrusion process abolished the sensitization potential of the amaranth albumins.
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Barre, Annick, Carole Pichereaux, Esmeralda Velazquez, Agathe Maudouit, Mathias Simplicien, Lorna Garnier, Françoise Bienvenu, et al. "Insights into the Allergenic Potential of the Edible Yellow Mealworm (Tenebrio molitor)." Foods 8, no. 10 (October 18, 2019): 515. http://dx.doi.org/10.3390/foods8100515.
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The edible yellow mealworm (Tenebrio molitor), contains an extremely diverse panel of soluble proteins, including proteins with structural functions such as muscle proteins, as well as proteins involved in metabolic functions such as enzymes. Most of these proteins display a more or less pronounced allergenic character toward previously sensitized people, especially people allergic to shrimps and other shellfish. A mass spectrometry approach following the separation of a mealworm protein, extracted by sodiumdodecyl sulfate-polyacrylamide gel electrophoresis, allowed us to identify up to 106 distinct protein fractions including molecules with structural and functional functions, susceptible to developing an allergenic potential due to the possibility of immunoglobulin E-binding cross-reactions with their counterparts occurring in shellfish. In this respect, most of the sera from people allergic to shrimps reacted with the mealworm protein extract in Western blot experiments. Moreover, the potential mealworm allergens triggered the in vitro degranulation of rat leukemic basophils transfected with the human high-affinity IgE receptor (FcεRI), upon sensitization by the IgE-containing sera from people allergic to shrimps and other shellfish foods. Owing to the large repertoire of IgE-binding cross-reacting allergens the yellow mealworm shares with other phylogenetically-related groups of arthropods, it would seem prudent to inform the consumers, especially those allergic to shellfish, by appropriate labeling on edible mealworm packages about the potential risk of developing an allergic reaction.
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Herman, Rod A., Jason M. Roper, and John X. Q. Zhang. "Evidence runs contrary to digestive stability predicting protein allergenicity." Transgenic Research 29, no. 1 (November 18, 2019): 105–7. http://dx.doi.org/10.1007/s11248-019-00182-x.
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AbstractA dogma has persisted for over two decades that food allergens are more stable to digestion compared with non-allergenic proteins. This belief has become enshrined in regulations designed to assess the allergenic risk of novel food proteins. While the empirical evidence accumulated over the last 20+ years has largely failed to confirm a correlation between digestive stability and the allergenic status of proteins, even those who accept this finding often assert that this shortfall is the result of faulty assay design rather than lack of causality. Here, we outline why digestive stability may not in fact correlate with allergenic potential.
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Schloman, W. W., V. H. Teetor, and D. T. Ray. "Protein Levels Affect the Cure Efficiency and Allergenic Potential of Polyisoprene Latices." Rubber Chemistry and Technology 79, no. 4 (September 1, 2006): 631–40. http://dx.doi.org/10.5254/1.3547957.
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Abstract Commercial NR latex has a higher total protein content than guayule (GR) latex. Some NR proteins are allergens bound to the rubber particle surface. Washing NR latex with a non-ionic surfactant displaced these particle-bound proteins and reduced allergens by more than 95%. The cost of such deproteination was reduced vulcanization efficiency, as determined by crosslink density. The extent of vulcanization correlated well with both total protein and allergen levels. Compared with films prepared from untreated NR latex, films from both surfactant-treated NR latex and GR latex had lower states of cure. Where particle-bound proteins were still present, as they are in GR latex, crosslink development could be completed by heat aging. In contrast, crosslink development in the film from surfactant-treated NR was complete after dipping and drying. The resulting films yielded high levels of extractable protein allergens.
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Arámburo-Galvez, Jesús, Norberto Sotelo-Cruz, Lilian Flores-Mendoza, Martina Gracia-Valenzuela, Francisco Chiquete-Elizalde, Jesús Espinoza-Alderete, Humberto Trejo-Martínez, Vicente Canizalez-Román, Noé Ontiveros, and Francisco Cabrera-Chávez. "Assessment of the Sensitizing Potential of Proteins in BALB/c Mice: Comparison of Three Protocols of Intraperitoneal Sensitization." Nutrients 10, no. 7 (July 14, 2018): 903. http://dx.doi.org/10.3390/nu10070903.
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Most food allergy cases are associated with a limited group of allergens. This could be attributed to an increased ability of some foods to sensitize and trigger allergic reactions. However, there are no validated animal models to evaluate the sensitizing or allergenic potentials of proteins. Our aim was to evaluate three protocols of adjuvant-free intraperitoneal sensitization that differ in the time points for sample collection (days 14, 28 and 35 from beginning of the sensitization) and also in the number of immunizations (2, 5 and 3, respectively). Ovalbumin (OVA; 0.05 mg), cow milk proteins (CMP; 0.025, 0.05 and 0.25 mg), and potato acid phosphatase (PAP; low allergenic protein; 250.0 mg) were administered intraperitoneally (ip) to BALB/c mice (n = 4–6) and the protein-specific IgE and IgG antibody responses were evaluated using ELISA. Additional serum protein-specific IgE antibodies evaluations were carried out after IgG depletion. Anti-OVA IgE antibodies were detected in mice from all three protocols. The responses were higher in the group of mice that underwent the 28-day protocol than in those that underwent the 14- or 35-day protocols (p < 0.01 and p < 0.05, respectively). Anti-CMP IgE antibodies were detected in both the 14- and 28-day protocols, but the response was higher in the group that underwent the 28-day protocol (p < 0.001). The anti-CMP IgE antibody response detection was improved after serum IgG depletion (p < 0.001). Anti-PAP IgE antibodies were not detected. Mice with undetectable serum levels of protein-specific IgE triggered anti-OVA, -CMP, and -PAP IgG responses. An adjuvant-free 28-day protocol with five ip immunizations seems appropriate for evaluation of the inherent sensitizing or allergenic capacity of the studied proteins. Reproducible results were obtained utilizing the BALB/c mouse strain. Inter-laboratory studies including a larger number of proteins should be carried out to validate this model.
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Skrzypczak, Katarzyna, Katarzyna Michalak, Jakub Wyrostek, Ewa Jabłońska-Ryś, Aneta Sławińska, Wojciech Radzki, and Waldemar Gustaw. "Bacterial Profile and Changes in the Protein–Peptide Fraction in Spontaneously Fermented Lens culinaris Medik." Applied Sciences 12, no. 17 (September 5, 2022): 8916. http://dx.doi.org/10.3390/app12178916.
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Pulses have desirable nutritional properties and a wide range of applications in the food industry as meat-free, casein-free, gluten-free, and functional food products. Unfortunately, the legume raw material contains some anti-nutrients and allergenic agents; nonetheless, fermentation processes may reduce some of these undesirable compounds. Therefore, the objective of the preliminary investigation was to determine the profile of bacteria occurring after spontaneous fermentation of Lens culinaris Medik. and detect changes in the protein–peptide pattern, including potential modifications of Len c3, i.e., a non-specific lipid-transfer protein (nsLTP) recognized as an important allergen. This study involved MALDI TOF/TOF, Illumina next-generation sequencing, and FT-IR spectroscopy analyses. Sixteen different species were identified in the plant-based material after 48-h spontaneous fermentation. The most abundant species were Lactococcus taiwanensis and Pediococcus pentosaceus (54.95% and 25.34%, respectively). The performed initial analysis revealed that after spontaneous fermentation had occurred the degradation of proteins (~10 kDa) and peptides (6–8 kDa), as well as the decomposition of proteins in the mass range that might be attributed to allergenic nsLTP. The preliminary findings encourage further research into the functional and technological properties of the isolated bacteria and in-depth analyses of the possibility of the removal of allergenic compounds from red lentils through fermentation carried out by the isolates.
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Yukalo, V. G., K. Ye Datsyshyn, and M. B. Shkilna. "Low allergenic fermented drink enriched with bioactive peptides of whey proteins." Scientific Messenger of LNU of Veterinary Medicine and Biotechnologies 24, no. 97 (June 28, 2022): 20–26. http://dx.doi.org/10.32718/nvlvet-f9704.
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Whey protein hydrolysates are most often used in the production of hypoallergenic products, as low molecular weight proteolysis products do not cause allergic reactions in consumers. However, it has been found that whey proteins are not only a good source of amino acids, but also a large number of natural biologically active peptides (BAP). They are formed during normal digestion in the gastrointestinal tract. These natural BAP have a positive effect on various functions of the human body regardless of age. When using microbial and plant enzyme preparations, as well as hydrolysis conditions other than physiological, the formation of such biologically active peptides is impossible, and such products lose much of their biological value. The article highlights the results of research on the development of technology of low-allergenic fermented drink enriched with biologically active peptides of whey proteins. To develop the technology of beverage, we proposed to use micellar casein, which is a source of basic milk protein – casein and whey protein hydrolysate, obtained in physiological conditions, as a source of biologically active peptides from whey proteins. Whey protein hydrolysate was added to the product in two ways: to the normalized mixture before and after fermentation. The hydrolysate was added to the product in an amount corresponding to the whey protein content: 0.5 %; 0.7 %; 0.9 %; 1.1 %. It was found that the amount of hydrolysate introduced affects the duration of fermentation of the studied samples. It was noted that until the end of the recommended shelf life, the organoleptic characteristics of samples fermented with hydrolysate remained virtually unchanged, while the consistency of samples in which the hydrolysate was added after fermentation became slightly thinner compared to the day of production. It is also proved that the usage of whey protein hydrolysate helps to reduce the release of whey when filtering a fermented beverage during storage for seven days.
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Packi, Kacper, Joanna Matysiak, Eliza Matuszewska, Anna Bręborowicz, and Jan Matysiak. "Changes in Serum Protein–Peptide Patterns in Atopic Children Allergic to Plant Storage Proteins." International Journal of Molecular Sciences 24, no. 2 (January 16, 2023): 1804. http://dx.doi.org/10.3390/ijms24021804.
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Next to cow’s milk and eggs, plant foods, i.e., legumes, tree nuts and cereal grains, most often sensitise atopic children. Storage proteins constitutes the most relevant protein fraction of plant foods, causing primary sensitisation. They exhibit strong allergenic properties and immunogenicity. Our goal was to analyse sensitisation to 26 plant storage proteins in a group of 76 children aged 0–5 years with chronic symptoms of atopic dermatitis using Allergy Explorer ALEX2 and to discover changes in serum protein–peptide patterns in allergic patients with the use of MALDI-TOF-MS. We reported that 25% of children were allergic to 2S albumins, 19.7% to 7S globulins, 13.2% to 11S globulins and 1.3% to cereal prolamins. The most common allergenic molecules were Ara h 1 (18.4%), Ara h 2 (17.1%), Ara h 6 (15.8%) and Ara h 3 (11.8%) from peanuts, and the mean serum sIgE concentrations in allergic patients were 10.93 kUA/L, 15.353 kUA/L, 15.359 kUA/L and 9.038 kUA/L, respectively. In children allergic to storage proteins compared to the other patients (both allergic and non-allergic), the cell cycle control protein 50A, testis-expressed sequence 13B, DENN domain-containing protein 5A and SKI family transcriptional corepressor 2 were altered. Our results indicate that the IgE-mediated allergy to storage proteins is a huge problem in a group of young, atopic children, and show the potential of proteomic analysis in the prediction of primary sensitisation to plant foods. It is the next crucial step for understanding the molecular consequences of allergy to storage proteins.
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Tomková, K., F. Štumr, P. Dvorská, P. Šafářová, J. Rysová, D. Gabrovská, P. Hanák, and J. Plicka. "Methods for the Determination of Allergenic Substances in Foods." Czech Journal of Food Sciences 27, Special Issue 1 (June 24, 2009): S369—S371. http://dx.doi.org/10.17221/945-cjfs.
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Within the framework of the research project ELISA methods for the quantitative determination of allergenic substances in foodstuff and raw materials were developed. ELISA kits for allergenic proteins of milk (casein, beta-lactoglobulin and BSA) egg white proteins and mustard proteins were validated and collaborative studies were performed to prove the validation of the ELISA methods developed. Various methods of extraction were tested. The parameters as a limit of detection, as a limit of quantification, robustness, repeatability and accuracy were determined. A broad range of zero matrices for allergens were tested as well. The ELISA kits are suitable for the determination of allergens according to EU legislation Directive 2005/26/EC and Directive 2006/142/EC in the laboratories focused on this topic.
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Groth, Sabrina, Christoph Budke, Timo Weber, Susanne Neugart, Sven Brockmann, Martina Holz, Bao Chau Sawadski, Diemo Daum, and Sascha Rohn. "Relationship between Phenolic Compounds, Antioxidant Properties, and the Allergenic Protein Mal d 1 in Different Selenium-Biofortified Apple Cultivars (Malus domestica)." Molecules 26, no. 9 (April 30, 2021): 2647. http://dx.doi.org/10.3390/molecules26092647.
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Notable parts of the population in Europe suffer from allergies towards apples. To address this health problem, the analysis of the interactions of relevant allergens with other substances such as phenolic compounds is of particular importance. The aim of this study was to evaluate the correlations between the total phenolic content (TPC), polyphenol oxidase (PPO) activity, antioxidant activity (AOA), and the phenolic compound profile and the content of the allergenic protein Mal d 1 in six apple cultivars. It was found that the PPO activity and the content of individual phenolic compounds had an influence on the Mal d 1 content. With regard to the important constituents, flavan-3-ols and phenolic acids, it was found that apples with a higher content of chlorogenic acid and a low content of procyanidin trimers and/or epicatechin had a lower allergenic potential. This is probably based on the reaction of phenolic compounds (when oxidized by the endogenous PPO) with proteins, thus being able to change the conformation of the (allergenic) proteins, which further corresponds to a loss of antibody recognition. When apples were additionally biofortified with selenium, the composition of the apples, with regard to TPC, phenolic profile, AOA, and PPO, was significantly affected. Consequently, this innovative agronomic practice seems to be promising for reducing the allergenic potential of apples.
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Freidl, Raphaela, Victoria Garib, Birgit Linhart, Elisabeth M. Haberl, Isabelle Mader, Zsolt Szépfalusi, Klara Schmidthaler, et al. "Extensively Hydrolyzed Hypoallergenic Infant Formula with Retained T Cell Reactivity." Nutrients 15, no. 1 (December 26, 2022): 111. http://dx.doi.org/10.3390/nu15010111.
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Background: Immunoglobulin E (IgE)-mediated cow’s milk allergy (CMA) can be life-threatening and affects up to 3% of children. Hypoallergenic infant formulas based on hydrolyzed cow’s milk protein are increasingly considered for therapy and prevention of cow’s milk allergy. The aim of this study was to investigate the allergenic activity and ability to induce T cell and cytokine responses of an infant formula based on extensively hydrolyzed cow’s milk protein (whey) (eHF, extensively hydrolyzed formula) supplemented with Galactooligosaccharides (GOS) and Limosilactobacillus fermentum CECT5716 (LF) to determine its suitability for treatment and prevention of CMA. Methods: eHF and standard protein formula based on intact cow’s milk proteins (iPF) with or without Galactooligosaccharide (GOS) and Limosilactobacillus fermentum CECT5716 (LF) were investigated with allergen-specific antibodies and tested for IgE reactivity and allergenic activity in basophil degranulation assays with sera from cow’s milk (CM)-allergic infants/children. Their ability to stimulate T cell proliferation and cytokine secretion in cultured peripheral blood mononuclear cells (PBMC) from CM-allergic infants and children was studied with a FACS-based carboxyfluorescein diacetate succinimidyl ester (CFSE) dilution assay and xMAP Luminex fluorescent bead-based technology, respectively. Results: An eHF supplemented with GOS and LF exhibiting almost no IgE reactivity and allergenic activity was identified. This eHF induced significantly lower inflammatory cytokine secretion as compared to an intact protein-based infant formula but retained T cell reactivity. Conclusions: Due to strongly reduced allergenic activity and induction of inflammatory cytokine secretion but retained T cell reactivity, the identified eHF may be used for treatment and prevention of CMA by induction of specific T cell tolerance.
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Kok, Melanie, Astrid Compagner, Ina Panneman, Aline Sprikkelman, and Berber Vlieg-Boerstra. "A Food, a Bite, a Sip: How Much Allergen Is in That?" Nutrients 13, no. 2 (February 10, 2021): 587. http://dx.doi.org/10.3390/nu13020587.
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Detailed information about the amount of allergenic protein ingested by the patient prior to an allergic reaction yields valuable information for the diagnosis, guidance and management of food allergy. However, the exact amount of ingredients is often not declared on the label. In this study the feasibility was studied for estimating the amount of allergenic protein from milk, eggs, peanuts and hazelnuts in frequently consumed composite and non-composite foods and per bite or sip size in different age groups in the Netherlands. Foods containing milk, egg, peanut or hazelnut most frequently consumed were selected for the age groups 2–3, 4–6 and 19–30 years. If the label did not yield clear information, the amount of allergenic protein was estimated based on food labels. Bite or sip sizes were determined in these age groups in 30 different foods. The amount of allergenic protein could be estimated in 47/70 (67%) of composite foods, which was complex. Estimated protein content of milk, egg, peanut and hazelnut was 2–3 g for most foods but varied greatly from 3 to 8610 mg and may be below threshold levels of the patient. In contrast, a single bite or sip can contain a sufficient amount of allergenic protein to elicit an allergic reaction. Bite and sip sizes increased with age. In every day practice it is hard to obtain detailed and reliable information about the amount of allergenic protein incorporated in composite foods. We encourage companies to disclose the amount of common allergenic foods on their labels.
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Spöttel, Jenny, Johannes Brockelt, Svenja Badekow, and Sascha Rohn. "Immunological Analysis of Isothiocyanate-Modified α-Lactalbumin Using High-Performance Thin Layer Chromatography." Molecules 26, no. 7 (March 25, 2021): 1842. http://dx.doi.org/10.3390/molecules26071842.
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Undirected modifications between food proteins and secondary plant metabolites can occur during food processing. The results of covalent interactions can alter the functional and biological properties of the proteins. The present work studied the extent of which covalent conjugation of the bioactive metabolite benzyl isothiocyanate (BITC; a glucosinolate breakdown product) to the whey protein α-lactalbumin affects the protein’s allergenicity. Additional to the immunological analysis of native untreated and BITC-modified α-lactalbumin, the analysis of antigenic properties of proteolytically digested protein derivatives was also performed by high performance thin layer chromatography and immunostaining. As a result of the chemical modifications, structural changes in the protein molecule affected the allergenic properties. In this process, epitopes are destroyed or inactivated, but at the same time, buried epitopes can be exposed or newly formed, so that the net effect was an increase in allergenicity, in this case. Results from the tryptic hydrolysis suggest that BITC conjugation sterically hindered the cleavage sites for the enzyme, resulting in reduced digestibility and allergenicity. Residual antigenicity can be still present as short peptide fragments that provide epitopes. The desire to make food safer for allergy sufferers and to protect sensitized individuals from an allergenic reaction makes it clear that the detection of food antigens is mandatory; especially by considering protein interactions.
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Kumar Shaha, Ranajit, Nitai Roy, and Talukdar G. "Characterization and Sensitivity Test of the Allergenic Pollen Proteins from Litchi Chimensis Plant." Journal of Tropical Resources and Sustainable Science (JTRSS) 1, no. 1 (August 15, 2021): 25–35. http://dx.doi.org/10.47253/jtrss.v1i1.667.
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Pollen of Litchi chinensis (Litchi) is a major aeroallergen of Bangladesh. Pollen of this fruits plant was collected from full bloomed flower growing in different places of Rajshahi in Bangladesh. Pollen protein was extracted and partial purified by means of long-term PBS extraction, salting out, dialysis, gel filtrations and DEAE-Cellulose chromatography and the protein was designated as LFPP (Litchi flowers pollen protein). Gel filtration of the purified pollen protein gives two main peaks. The major peak gives four bands on SDS-PAGE. The enzyme (pectate lyase) proteins after gel filtration again re-purified by Ion exchange chromatography, a single band in the protein profile of LFPP, (M.W. 28kDa) was the major allergenic component of Litchi chinensis (Litchi) flower pollen. The homogeneity and the molecular weight of the protein were estimated by SDS-PAGE, and Gel filtration was 28kDa. The allergenic protein was identified by skin prick tests and showed the pectate lyase (Pel) activity. Skin-prick tests also revealed highest degree of sensitivity to the Nawabgang sample giving positive response in 80% of the patients. Skin reactivity ranged between 1+ and 3+.
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Gasparini, Alessandra, Sofie Buhler, Andrea Faccini, Stefano Sforza, and Tullia Tedeschi. "Thermally-Induced Lactosylation of Whey Proteins: Identification and Synthesis of Lactosylated β-lactoglobulin Epitope." Molecules 25, no. 6 (March 12, 2020): 1294. http://dx.doi.org/10.3390/molecules25061294.
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The high temperatures used in the production of milk may induce modifications in proteins structure. Due to occurrence of the Maillard reaction, lactose binds lysine residues in proteins, affecting the nutritional value. Milk is also an important source of allergenic proteins (i.e., caseins, β-lactoglobulin and α-lactalbumin). Thus, this modification may also affect the allergenicity of these proteins. Focusing on milk whey proteins, a screening on different Ultra High Temperatures (UHT) and pasteurized milk samples was performed to identify lactosylation sites, in particular in protein known epitopes, and to verify the correlation between lactosylation and the harshness of the treatment. Whey proteins were extracted from milk samples after caseins precipitations at pH 4.6 and, after chymotryptic and tryptic in solution digestion, peptides were analysed by UPLC-MS and LTQ-Orbitrap. Results show the presence of lactosylated lysine residues in several known epitopes. Then, a β-lactoglobulin epitope was selected and synthesized by solid phase synthesis followed by in solution lactosylation, obtaining high reaction yields and purities. The synthesis of lactosylated allergenic epitopes, described here for the first time, is a useful tool for further studies on the technological impacts on food allergenicity.
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Seweryn, Ewa, Emilia Królewicz, Kamilla Stach, and Irena Kustrzeba-Wójcicka. "Nutritional and allergenic properties of hen eggs." Postępy Higieny i Medycyny Doświadczalnej 72 (April 6, 2018): 205–14. http://dx.doi.org/10.5604/01.3001.0011.7339.
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Chicken eggs, along with cow milk, are the most important source of proteins and other valuable nutrients that are introduced to a baby`s diet. Certain components of eggs, besides nutritional, also have other biological functions. Both proteins, phospholipids or carotenoids, are bioactive components which affect the physiological processes in the human body. Regular consumption of chicken eggs rich in substances with antibacterial, anti-inflammatory, immunomodulatory and antioxidant properties may contribute to reducing the incidence of certain lifestyle diseases. Ovomucoid, as a glycoprotein which inhibits bacterial protease, is a component of eggs with bactericidal properties. Similarly, the ovotransferrin protein has a bacteriostatic effect on the Escherichia coli strain or Streptococcus mutans. Due to the strong antioxidant properties, phospholipids, vitamin E and folic acid are extremely valuable egg components. It is believed that the high antioxidant potential of these compounds is important in preventing the development of atherosclerosis and other metabolic syndromes. It is also worth mentioning lutein and zeaxanthin, which are dyes that form a protective barrier against the degeneration of the macula of the human eye. An extremely important function for the human immune system is also met by lysozyme, which stimulates the synthesis of interferon, stimulating the immune response. Unfortunately, hypersensitivity to chicken eggs is one of the most common food allergies in children and affects 0.5-9% of the population. The major egg allergens (Gallus spp.): ovomucoid (Gal d 1), ovalbumin (Gal d 2), conalbumin (Gal d 3) and lysozyme (Gal d 4) are present in egg white and most often cause allergic reactions in children. Minor allergens: serum albumin (Gal d 5) and YGP42 protein (Gal d 6) are found in the egg yolk and are more likely to sensitize adults.
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Herman, Rod A., Patricia A. Bauman, Laurie Goodwin, Emir Islamovic, Eric H. Ma, Hector Serrano, Andre Silvanovich, et al. "Mass spectrometric analysis of digesta does not improve the allergenicity assessment of GM crops." Transgenic Research 30, no. 3 (April 16, 2021): 283–88. http://dx.doi.org/10.1007/s11248-021-00254-x.
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AbstractAn investigation of the potential allergenicity of newly expressed proteins in genetically modified (GM) crops comprises part of the assessment of GM crop safety. However, allergenicity is not completely predictable from a definitive assay result or set of protein characteristics, and scientific opinions regarding the data that should be used to assess allergenicity are continuously evolving. Early studies supported a correlation between the stability of a protein exposed to digestive enzymes such as pepsin and the protein’s status as a potential allergen, but over time the conclusions of these earlier studies were not confirmed. Nonetheless, many regulatory authorities, including the European Food Safety Authority (EFSA), continue to require digestibility analyses as a component of GM crop risk assessments. Moreover, EFSA has recently investigated the use of mass spectrometry (MS), to make digestion assays more predictive of allergy risk, because it can detect and identify small undigested peptides. However, the utility of MS is questionable in this context, since known allergenic peptides are unlikely to exist in protein candidates intended for commercial development. These protein candidates are pre-screened by the same bioinformatics processes that are normally used to identify MS targets. Therefore, MS is not a standalone allergen identification method and also cannot be used to predict previously unknown allergenic epitopes. Thus, the suggested application of MS for analysis of digesta does not improve the poor predictive power of digestion assays in identifying allergenic risk.
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Ulfman, Laurien, Angela Tsuang, Aline B. Sprikkelman, Anne Goh, and R. J. Joost van Neerven. "Relevance of Early Introduction of Cow’s Milk Proteins for Prevention of Cow’s Milk Allergy." Nutrients 14, no. 13 (June 27, 2022): 2659. http://dx.doi.org/10.3390/nu14132659.
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Food allergy incidence has increased worldwide over the last 20 years. For prevention of food allergy, current guidelines do not recommend delaying the introduction of allergenic foods. Several groundbreaking studies, such as the Learning Early About Peanut Allergy study, showed that the relatively early introduction of this allergenic food between 4–6 months of age reduces the risk of peanut allergy. However, less is known about the introduction of cow’s milk, as many children already receive cow’s-milk-based formula much earlier in life. This can be regular cow’s milk formula with intact milk proteins or hydrolyzed formulas. Several recent studies have investigated the effects of early introduction of cow’s-milk-based formulas with intact milk proteins on the development of cow’s milk allergy while breastfeeding. These studies suggest that depending on the time of introduction and the duration of administration of cow’s milk, the risk of cow’s milk allergy can be reduced (early introduction) or increased (very early introduction followed by discontinuation). The aim of this narrative review is to summarize these studies and to discuss the impact of early introduction of intact cow’s milk protein—as well as hydrolyzed milk protein formulas—and the development of tolerance versus allergy towards cow’s milk proteins.
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Jędrusek-Golińska, Anna, Dorota Piasecka-Kwiatkowska, Paulina Zielińska, Magdalena Zielińska-Dawidziak, Krystyna Szymandera-Buszka, and Marzanna Hęś. "Soy Preparations Are Potentially Dangerous Factors in the Course of a Food Allergy." Foods 8, no. 12 (December 7, 2019): 655. http://dx.doi.org/10.3390/foods8120655.
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The special properties of soy preparations make them common additives for food production and can be dangerous for sensitive individuals. Our aim was to check consumers’ awareness of potential risks of soy preparations added to numerous food products, depending on respondents’ education, and to evaluate immunoreactive properties of chosen soy preparations. A personal questionnaire was used. Respondents (n = 251) were aged 23–28 years old, lived in Poland, and were graduates or students in their last year of food technology, medicine, and university of technology. The slot blot and Western blotting methods were used to mark immunoreactivity of soy preparations. It was shown that most respondents often or usually read labels of food products they buy. The surveyed indicated protein is the allergenic component in soy. Almost half of them were of the opinion that hydrolysis removes the allergenic properties of soy. Most of the medical students surveyed thought that people allergic to soy may consume products that contain soy preparations. The analytical results indicated that soy preparation contained protein fractions that were immunoreactive with sera of allergenic patients. It was proven that preparations, even hydrolysates, contain immunoreactive proteins that may be the source of hidden allergens, even though they are not recognized as dangerous by well-educated respondents.
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Basu, Anamika. "In Silico Epitope-Based Vaccine Prediction against Fungal Infection Aspergillosis." Challenges 13, no. 2 (July 6, 2022): 29. http://dx.doi.org/10.3390/challe13020029.
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Aspergillus fumigatus is a pathogenic microorganism that causes aspergillosis due to the presence of its allergenic proteins. During the last two years, a few clinical cases have been reported where allergic bronchopulmonary aspergillosis (ABPA) has been detected in COVID-19 patients. The administration of antifungal medicine did not provide satisfactory results. It is a challenging job for medical scientists to protect mankind by designing an epitope-based vaccine against the rare disease aspergillosis. Other than twenty-three allergenic proteins, this microorganism contains an extra-cellular cellulase CelA expansin protein (Afu5g08030), which is allergenic. To design a peptide vaccine against aspergillosis, the identification of B cell and T cell epitopes is state-of-the-art technology. In our latest research, probable T cell and B cell epitopes are predicted. Molecular docking analysis of these predicted epitopes with their receptors is performed. Here, the primary sequence of the expansin protein is extracted and analyzed. Then, its secondary and tertiary structures are predicted using a homology modeling method and validated. Considering the physicochemical properties of this antigenic protein, two short stretches of peptides, namely 80KPQADEDPNASSSSSSS96 and 286DGGKTWQGTTRTS298, are predicted as linear B cell epitopes. Similarly, based on its contacts with the highest number of alleles, the peptide sequence 221LDLFQNAFTQLADVS235 is chosen as the most possible T cell epitope for the protein present in Aspergillus fumigatus with the highest binding energy for MHC II allele HLA-DRB1* 01: 01. Considering the binding energy of the B cell epitope with IgE, the second epitope 286DGGKTWQGTTRTS298 is designated as the most potential epitope of B cells for this protein. Docking studies were performed with the T cell epitope with the human ternary complex of T cell receptor, CD4 receptor, and peptide-MHC II molecule (PDB ID 3T0E) with a binding energy of −192 Kcal/mole. For peptide-based vaccines, the proposed B cell and T cell epitopes may be used against aspergillosis after further experimental analysis.
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Nedyalkova, Miroslava, and Vasil Simeonov. "Multivariate Chemometrics as a Strategy to Predict the Allergenic Nature of Food Proteins." Symmetry 12, no. 10 (September 29, 2020): 1616. http://dx.doi.org/10.3390/sym12101616.
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The purpose of the present study is to develop a simple method for the classification of food proteins with respect to their allerginicity. The methods applied to solve the problem are well-known multivariate statistical approaches (hierarchical and non-hierarchical cluster analysis, two-way clustering, principal components and factor analysis) being a substantial part of modern exploratory data analysis (chemometrics). The methods were applied to a data set consisting of 18 food proteins (allergenic and non-allergenic). The results obtained convincingly showed that a successful separation of the two types of food proteins could be easily achieved with the selection of simple and accessible physicochemical and structural descriptors. The results from the present study could be of significant importance for distinguishing allergenic from non-allergenic food proteins without engaging complicated software methods and resources. The present study corresponds entirely to the concept of the journal and of the Special issue for searching of advanced chemometric strategies in solving structural problems of biomolecules.
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Ballmer-Weber, Barbara K. "Allergic Reactions to Food Proteins." International Journal for Vitamin and Nutrition Research 81, no. 23 (March 1, 2011): 173–80. http://dx.doi.org/10.1024/0300-9831/a000055.
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Four to eight percent of the population are estimated to be food-allergic. Most food allergies in adolescents and adults are acquired on the basis of cross-reaction to pollen allergens. Theses allergens are ubiquitous in the plant kingdom. Therefore pollen-allergic patients might acquire a multitude of different plant food allergies, and even react to novel foods to which they have never previously been exposed. A curative therapy for food allergy does not yet exist. Food-allergic patients have to rely on strict avoidance diets, The widespread use of industrially processed foods poses a general problem for food-allergic patients. Although the most frequent allergens must be declared openly in the list of ingredients, involuntary contamination with allergy-provoking compounds can occur. The precautionary labelling may contain is sometimes applied even if the chance of contamination is very low; on the other hand, foods not declared to contain possible traces of allergenic components may actually contain relevant amounts of allergenic proteins. Switzerland is the only country in Europe with legal regulations on contamination by allergenic food; however, the allowance of 1 g/kg is too high to protect a relevant proportion of food-allergic individuals.
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MATSUDA, Tsukasa, Rieko NOMURA, Makoto SUGIYAMA, and Ryo NAKAMURA. "Immunochemical studies on rice allergenic proteins." Agricultural and Biological Chemistry 55, no. 2 (1991): 509–13. http://dx.doi.org/10.1271/bbb1961.55.509.
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Matsuda, Tsukasa, Rieko Nomura, Makoto Sugiyama, and Ryo Nakamura. "Immunochemical Studies on Rice Allergenic Proteins." Agricultural and Biological Chemistry 55, no. 2 (February 1991): 509–13. http://dx.doi.org/10.1080/00021369.1991.10870603.
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