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Artigos de revistas sobre o tema "Cross-species reactivity"

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Autor: Grafiati

Publicado: 7 de julho de 2024

Última modificação: 7 de julho de 2024

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1

ARLIAN, L., C. RAPP e E. FERNANDEZCALDAS. "Allergenicity of and its cross-reactivity with species". Journal of Allergy and Clinical Immunology 91, n.º 5 (maio de 1993): 1051–58. http://dx.doi.org/10.1016/0091-6749(93)90219-6.

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RESTANI, GAIASCHI, PLEBANI, BERETTA, CAVAGNI, FIOCCHI, POIESI, VELONÀ, UGAZIO e GALLI. "Cross-reactivity between milk proteins from different animal species". Clinical & Experimental Allergy 29, n.º 7 (julho de 1999): 997–1004. http://dx.doi.org/10.1046/j.1365-2222.1999.00563.x.

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3

SU, JUI-LAN, STEVE STIMPSON, CHRISTINE EDWARDS, JOHN VAN ARNOLD, SUSAN BURGESS e PEIYUAN LIN. "Neutralizing IGF-1 Monoclonal Antibody With Cross-Species Reactivity". Hybridoma 16, n.º 6 (dezembro de 1997): 513–18. http://dx.doi.org/10.1089/hyb.1997.16.513.

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4

Christensen, L. H., C. Hejl, H. Henmar, N. Johansen e H. Ipsen. "Extensive IgE Cross-reactivity towards Different US Ragweed Species". Journal of Allergy and Clinical Immunology 125, n.º 2 (fevereiro de 2010): AB17. http://dx.doi.org/10.1016/j.jaci.2009.12.098.

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Losada, S., N. Chacón, C.Colmenares, H. Bermúdez, A. Lorenzo, J. P. Pointier, A. Theron, B. Alarcón de Noya e O. Noya. "Schistosoma: Cross-reactivity and antigenic community among different species". Experimental Parasitology 111, n.º 3 (novembro de 2005): 182–90. http://dx.doi.org/10.1016/j.exppara.2005.07.007.

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6

Gersten, Douglas M., e Vincent J. Hearing. "Antigens of Murine Melanoma and Their Cross-Species Reactivity". Pathobiology 60, n.º 1 (1992): 49–56. http://dx.doi.org/10.1159/000163697.

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Van den Bossche, D., A. De Bel, M. Hendrickx, A. De Becker, R. Jacobs, A. Naessens e D. Pierard. "Galactomannan Enzymatic Immunoassay Cross-Reactivity Caused by Prototheca Species". Journal of Clinical Microbiology 50, n.º 10 (25 de julho de 2012): 3371–73. http://dx.doi.org/10.1128/jcm.01028-12.

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8

Gupta, R., B. P. Singh, S. Sridhara, S. N. Gaur, R. Kumar, V. K. Chaudhary e N. Arora. "Allergenic cross-reactivity ofCurvularia lunatawith other airborne fungal species". Allergy 57, n.º 7 (julho de 2002): 636–40. http://dx.doi.org/10.1034/j.1398-9995.2002.03331.x.

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9

Conrad, Melanie L., William C. Davis e Ben F. Koop. "TCR and CD3 antibody cross-reactivity in 44 species". Cytometry Part A 71A, n.º 11 (2007): 925–33. http://dx.doi.org/10.1002/cyto.a.20435.

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10

Emiliani, Yuliana, Andrés Sánchez, Marlon Munera, Jorge Sánchez e Dilia Aparicio. "In silico analysis of cross reactivity among phospholipases from Hymenoptera species". F1000Research 10 (29 de março de 2021): 2. http://dx.doi.org/10.12688/f1000research.27089.2.

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Background: Phospholipases are enzymes with the capacity to hydrolyze membrane lipids and have been characterized in several allergenic sources, such as hymenoptera species. However, cross-reactivity among phospholipases allergens are little understood. The objective of this study was to determine potential antigenic regions involved in cross-reactivity among allergens of phospholipases using an in silico approach. Methods: In total, 18 amino acids sequences belonging to phospholipase family derived from species of the order hymenoptera were retrieved from the UniProt database to perform phylogenetic analysis to determine the closest molecular relationship. Multialignment was done to identify conserved regions and matched with antigenic regions predicted by ElliPro server. 3D models were obtained from modeling by homology and were used to locate cross-reactive antigenic regions. Results: Phylogenetic analysis showed that the 18 phospholipases split into four monophyletic clades (named here as A, B, C and D). Phospholipases from A clade shared an amino acid sequences’ identity of 79%. Antigenic patches predicted by Ellipro were located in highly conserved regions, suggesting that they could be involved in cross-reactivity in this group (Ves v 1, Ves a 1 and Ves m 1). Conclusions: At this point, we advanced to the characterization of potential antigenic sites involved in cross-reactivity among phospholipases. Inhibition assays are needed to confirm our finding.

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Emiliani, Yuliana, Andrés Sánchez, Marlon Munera, Jorge Sánchez e Dilia Aparicio. "In silico analysis of cross reactivity among phospholipases from Hymenoptera species". F1000Research 10 (5 de janeiro de 2021): 2. http://dx.doi.org/10.12688/f1000research.27089.1.

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Background: Phospholipases are enzymes with the capacity to hydrolyze membrane lipids and have been characterized in several allergenic sources, such as hymenoptera species. However, cross-reactivity among phospholipases allergens are little understood. The objective of this study was to determine potential antigenic regions involved in cross-reactivity among allergens of phospholipases using an in silico approach. Methods: In total, 18 amino acids sequences belonging to phospholipase family derived from species of the order hymenoptera were retrieved from the UniProt database to perform phylogenetic analysis to determine the closest molecular relationship. Multialignment was done to identify conserved regions and matched with antigenic regions predicted by ElliPro server. 3D models were obtained from modeling by homology and were used to locate cross-reactive antigenic regions. Results: Phylogenetic analysis showed that the 18 phospholipases split into four monophyletic clades (named here as A, B, C and D). Phospholipases from A clade shared an amino acid sequences’ identity of 79%. Antigenic patches predicted by Ellipro were located in highly conserved regions, suggesting that they could be involved in cross-reactivity in this group (Ves v 1, Ves a 1 and Ves m 1). Conclusions: At this point, we advanced to the characterization of potential antigenic sites involved in cross-reactivity among phospholipases. Inhibition assays are needed to confirm our finding.

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12

Zhou, Wei, Kaylah Bias, Dylan Lenczewski-Jowers, Jiliah Henderson, Victor Cupp, Anthony Ananga, Joel Winyo Ochieng e Violeta Tsolova. "Analysis of Protein Sequence Identity, Binding Sites, and 3D Structures Identifies Eight Pollen Species and Ten Fruit Species with High Risk of Cross-Reactive Allergies". Genes 13, n.º 8 (17 de agosto de 2022): 1464. http://dx.doi.org/10.3390/genes13081464.

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Fruit allergens are proteins from fruits or pollen that cause allergy in humans, an increasing food safety concern worldwide. With the globalization of food trade and changing lifestyles and dietary habits, characterization and identification of these allergens are urgently needed to inform public awareness, diagnosis and treatment of allergies, drug design, as well as food standards and regulations. This study conducted a phylogenetic reconstruction and protein clustering among 60 fruit and pollen allergens from 19 species, and analyzed the clusters, in silico, for cross-reactivity (IgE), 3D protein structure prediction, transmembrane and signal peptides, and conserved domains and motifs. Herein, we wanted to predict the likelihood of their interaction with antibodies, as well as cross-reactivity between the many allergens derived from the same protein families, as the potential for cross-reactivity complicates the management of fruit allergies. Phylogenetic analysis classified the allergens into four clusters. The first cluster (n = 9) comprising pollen allergens showed a high risk of cross-reactivity between eight allergens, with Bet v1 conserved domain, but lacked a transmembrane helix and signal peptide. The second (n = 10) cluster similarly suggested a high risk of cross-reactivity among allergens, with Prolifin conserved domain. However, the group lacked a transmembrane helix and signal peptide. The third (n = 13) and fourth (n = 29) clusters comprised allergens with significant sequence diversity, predicted low risk of cross-reactivity, and showed both a transmembrane helix and signal peptide. These results are critical for treatment and drug design that mostly use transmembrane proteins as targets. The prediction of high risk of cross-reactivity indicates that it may be possible to design a generic drug that will be effective against the wide range of allergens. Therefore, in the past, we may have avoided the array of fruit species if one was allergic to any one member of the cluster.

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Vordermeier, H. Martin, Jemma Brown, Paul J. Cockle, Willeke P. J. Franken, Sandra M. Arend, Tom H. M. Ottenhoff, Keith Jahans e R. Glyn Hewinson. "Assessment of Cross-Reactivity between Mycobacterium bovis and M. kansasii ESAT-6 and CFP-10 at the T-Cell Epitope Level". Clinical and Vaccine Immunology 14, n.º 9 (1 de agosto de 2007): 1203–9. http://dx.doi.org/10.1128/cvi.00116-07.

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ABSTRACT Cross-reactivity between Mycobacterium kansasii ESAT-6 and CFP-10 homologues and their M. bovis counterparts can confound the interpretation of immunodiagnostic tests for tuberculosis. M. kansasii is a nontuberculous mycobacterial species cultured from skin test-positive cattle in Great Britain. Using peptides derived from M. bovis and M. kansasii ESAT-6 and CFP-10 regions that differ between these species, we investigated the species specificity and cross-reactivity at the level of individual bovine T-cell epitopes. Our results demonstrated that all peptides tested are fully cross-reactive, with the exception of one ESAT-6-derived peptide that harbored an M. bovis-specific epitope(s) when it was recognized in the context of bovine leukocyte antigen (BoLA)-DQ but that was cross-reactive with its M. kansasii homologues when it was restricted by BoLA-DR. This observation further highlights that prediction of species specificity by comparing sequence identity/homology alone is not sufficient and that individuals with diverse major histocompatibility complex constellations need to be tested to characterize the cross-reactivity or species specificity of peptide-based reagents.

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Holm, Bettina E., Noreen Sandhu, Julie Tronstrøm, Magnus Lydolph, Nicole H. Trier e Gunnar Houen. "Species cross-reactivity of rheumatoid factors and implications for immunoassays". Scandinavian Journal of Clinical and Laboratory Investigation 75, n.º 1 (27 de outubro de 2014): 51–63. http://dx.doi.org/10.3109/00365513.2014.965738.

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15

Irani, Yazad, Pierre Scotney, Andrew Nash e Keryn A. Williams. "Species Cross-Reactivity of Antibodies Used to Treat Ophthalmic Conditions". Investigative Opthalmology & Visual Science 57, n.º 2 (17 de fevereiro de 2016): 586. http://dx.doi.org/10.1167/iovs.15-18239.

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16

Hansen, Tine K., Carsten Bindslev-Jensen, Per Stahl Skov e Lars K. Poulsen. "Codfish Allergy in Adults: IgE Cross-Reactivity Among Fish Species". Annals of Allergy, Asthma & Immunology 78, n.º 2 (fevereiro de 1997): 187–94. http://dx.doi.org/10.1016/s1081-1206(10)63386-8.

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17

Plunkett, Greg A., e Michelle L. Bolner. "Defining the Extent of Allergenic Cross-reactivity among Mold Species". Journal of Allergy and Clinical Immunology 139, n.º 2 (fevereiro de 2017): AB254. http://dx.doi.org/10.1016/j.jaci.2016.12.819.

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Palmer, Lee K., Justin T. Marsh, Mei Lu, Richard E. Goodman, Michael G. Zeece e Philip E. Johnson. "Shellfish Tropomyosin IgE Cross‐Reactivity Differs Among Edible Insect Species". Molecular Nutrition & Food Research 64, n.º 8 (março de 2020): 1900923. http://dx.doi.org/10.1002/mnfr.201900923.

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19

Berger, Bradley J., e A. Rashid Bhatti. "Snake venom components and their cross-reactivity: a review". Biochemistry and Cell Biology 67, n.º 9 (1 de setembro de 1989): 597–601. http://dx.doi.org/10.1139/o89-092.

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Snake venoms are complex mixtures of organic and inorganic compounds, many of which display biological activity. It has been demonstrated that antisera raised against whole venom or a single purified venom protein from one species of snake will react with proteins in the venom of other species. This cross-reactivity between species may have applications in determining snake phylogeny, but recent studies on the variation of venom components within a species make these evolutionary conclusions questionable.Key words: snake, venom, cross-reactive, evolution.

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20

Abdullah, Mai Shihah, Ghassan Hadi Kttafah e Muhammad Haidar Nasuruddin. "ALLERGENIC POTENTIAL AND CROSS-REACTIVITY OF FUNGAL SPECIES ISOLATED FROM THE INDOOR ENVIRONMENT". Jurnal Teknologi 84, n.º 3 (31 de março de 2022): 47–57. http://dx.doi.org/10.11113/jurnalteknologi.v84.17742.

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Indoor fungi are potential sensitizing agents. Their detection and quantiﬁcation in indoor environments are important in the diagnosis and environmental management of fungal allergies. This study aims to analyse the allergenic potential of ten fungal species and the cross-reactivity of the two most common fungi isolated from the indoor environment samples from Sultan Idris Education University buildings. Employing in vivo (skin prick test) and in vitro (immunoblotting), the major and minor allergenic proteins of ten fungi sensitized subjects were identified. Aspergillus fumigatus and Penicillium canescens were the most common fungi with the highest potential to trigger allergies. The cross-reactivity between them was detected by immunoblotting inhibition experiments using three selected sera from subjects sensitized to each of the aforementioned species. The immunoblotting test revealed multiple major and minor allergens. Among them were 11, 25, 33, 36 > 100 kDa and were also listed as causative agent triggering allergy by IUIS Allergen Nomenclature Subcommittee. Cross-reactivity of Aspergillus fumigatus against Penicillium canescens revealed that 9(64.29%) allergenic bands and 13(76.47%) allergenic bands were inhibited, respectively. Aspergillus spp. and Penicillium spp. with high cross-reactivity are most prevalent in the indoor environment of identified contaminated buildings at UPSI. Aspergillus fumigatus and Penicillium canescens can elicit sensitization among the atopic population and implicates worsening the condition of the symptomatic subjects with prolonged these fungal exposures.

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Rizk, Raeda Z., Neil D. Christensen, Kristina M. Michael, Martin Müller, Peter Sehr, Tim Waterboer e Michael Pawlita. "Reactivity pattern of 92 monoclonal antibodies with 15 human papillomavirus types". Journal of General Virology 89, n.º 1 (1 de janeiro de 2008): 117–29. http://dx.doi.org/10.1099/vir.0.83145-0.

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Most anti-human papillomavirus (HPV) capsid antibody assays are based on virus-like particles (VLP). We evaluated glutathione S-transferase (GST)–L1 fusion proteins as ELISA antigens for determining type specificity and cross-reactivity of 92 VLP-specific monoclonal antibodies (mAb) generated against nine mucosal alpha papillomavirus types of species 7, 9 and 10. The antibody panel included 25 new mAb, and 24 previously published mAb are further characterized. We determined the cross-reactivity patterns with 15 different HPV types representing 6 species (alpha1, 2, 4, 7, 9 and 10) and neutralization and cross-neutralization properties with HPV types 6, 11, 16, 18 and 45. Eighty-nine (97 %) of the antibodies including 34, 71 and 14 recognizing neutralizing, conformational and linear epitopes, respectively, reacted with the GST–L1 protein of the HPV type used as immunogen, with log titres ranging from 2.0 to 7.3. Of these 89 antibodies, 52 % were monotypic, 20 % showed intra-species and 28 % inter-species cross-reactivity. Log neutralization titres to the immunogen HPV ranged from 1.7 to 5.6. A single cross-neutralizing mAb (H6.L12) was found. ELISA titres were always higher than neutralization titres. All neutralizing epitopes were conformational and mostly type-specific. Our data show that bacterially expressed, affinity-purified GST–L1 fusion proteins display a broad variety of epitopes and thus are well suited for detection of HPV antibodies. Cross-reactivity is associated with linear as well as conformational epitopes. Distantly related mucosal and skin alpha papillomaviruses share some conformational epitopes and the phylogenetic L1-based species definition may not define a serological unit since no species-specific epitope was found.

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Ledsgaard, Line, Timothy Jenkins, Kristian Davidsen, Kamille Krause, Andrea Martos-Esteban, Mikael Engmark, Mikael Rørdam Andersen, Ole Lund e Andreas Laustsen. "Antibody Cross-Reactivity in Antivenom Research". Toxins 10, n.º 10 (27 de setembro de 2018): 393. http://dx.doi.org/10.3390/toxins10100393.

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Antivenom cross-reactivity has been investigated for decades to determine which antivenoms can be used to treat snakebite envenomings from different snake species. Traditionally, the methods used for analyzing cross-reactivity have been immunodiffusion, immunoblotting, enzyme-linked immunosorbent assay (ELISA), enzymatic assays, and in vivo neutralization studies. In recent years, new methods for determination of cross-reactivity have emerged, including surface plasmon resonance, antivenomics, and high-density peptide microarray technology. Antivenomics involves a top-down assessment of the toxin-binding capacities of antivenoms, whereas high-density peptide microarray technology may be harnessed to provide in-depth knowledge on which toxin epitopes are recognized by antivenoms. This review provides an overview of both the classical and new methods used to investigate antivenom cross-reactivity, the advantages and disadvantages of each method, and examples of studies using the methods. A special focus is given to antivenomics and high-density peptide microarray technology as these high-throughput methods have recently been introduced in this field and may enable more detailed assessments of antivenom cross-reactivity.

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Smith, Roger, Joyce C. Kapatsa, Sidney J. Sherwood, Thomas A. Ficht, Joe W. Templeton e L. Garry Adams. "Differential reactivity of bovine lymphocytes to species of Brucella". American Journal of Veterinary Research 51, n.º 4 (1 de abril de 1990): 518–23. http://dx.doi.org/10.2460/ajvr.1990.51.04.518.

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SUMMARY The reactivity of bovine lymphocytes to 4 species of Brucella was tested in thymidine-uptake assays, using long-term cultured lymphocytes and freshly obtained blood mononuclear cells. Lymphocytes were taken from cows that had been challenge exposed with a virulent strain of B abortus at midgestation. The cows were classified retrospectively as being naturally resistant or susceptible to brucellosis. Lymphocytes taken from these cows had 3 patterns of reactivity with species of Brucella: pattern 1 was defined by reactivity with 4 species (B abortus, B canis, B suis, and B melitensis); pattern 2 was defined by reactivity with all these species, except B melitensis; pattern 3 was defined by reactivity with B abortus and B canis, but not with B suis or B melitensis. There was a statistically significant correlation between susceptibility to brucellosis and expression of lymphocyte cross-reactivity with B suis (P < 0.01) and with B melitensis (P < 0.01).

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Vanroye, Fien, Dorien Van den Bossche, Isabel Brosius, Bieke Tack, Marjan Van Esbroeck e Jan Jacobs. "COVID-19 Antibody Detecting Rapid Diagnostic Tests Show High Cross-Reactivity When Challenged with Pre-Pandemic Malaria, Schistosomiasis and Dengue Samples". Diagnostics 11, n.º 7 (25 de junho de 2021): 1163. http://dx.doi.org/10.3390/diagnostics11071163.

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COVID-19 Antibody Detecting Rapid Diagnostic Tests (COVID-19 Ab RDTs) are the preferred tool for SARS-CoV-2 seroprevalence studies, particularly in low- and middle-income countries. The present study challenged COVID-19 Ab RDTs with pre-pandemic samples of patients exposed to tropical pathogens. A retrospective study was performed on archived serum (n = 94) and EDTA whole blood (n = 126) samples obtained during 2010–2018 from 196 travelers with malaria (n = 170), schistosomiasis (n = 25) and dengue (n = 25). COVID-19 Ab RDTs were selected based on regulatory approval status, independent evaluation results and detecting antigens. Among 13 COVID-19 Ab RDT products, overall cross-reactivity was 18.5%; cross-reactivity for malaria, schistosomiasis and dengue was 20.3%, 18.1% and 7.5%, respectively. Cross-reactivity for current and recent malaria, malaria antibodies, Plasmodium species and parasite densities was similar. Cross-reactivity among the different RDT products ranged from 2.7% to 48.9% (median value 14.5%). IgM represented 67.9% of cross-reactive test lines. Cross-reactivity was not associated with detecting antigens, patient categories or disease (sub)groups, except for schistosomiasis (two products with ≥60% cross-reactivity). The high cross-reactivity for malaria, schistosomiasis and—to a lesser extent—dengue calls for risk mitigation when using COVID-19 Ab RDTs in co-endemic regions.

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Watts, M., N. W. Pankhurst, A. Pryce e B. Sun. "Vitellogenin isolation, purification and antigenic cross-reactivity in three teleost species". Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 134, n.º 3 (março de 2003): 467–76. http://dx.doi.org/10.1016/s1096-4959(02)00288-9.

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Farady, Christopher J., Benjamin D. Sellers, Matthew P. Jacobson e Charles S. Craik. "Improving the species cross-reactivity of an antibody using computational design". Bioorganic & Medicinal Chemistry Letters 19, n.º 14 (julho de 2009): 3744–47. http://dx.doi.org/10.1016/j.bmcl.2009.05.005.

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Tanaka, Gabriela D., Osvaldo Augusto Sant'Anna, José Roberto Marcelino, Ana Cristina Lustoza da Luz, Marisa Maria Teixeira da Rocha e Denise V. Tambourgi. "Micrurus snake species: Venom immunogenicity, antiserum cross-reactivity and neutralization potential". Toxicon 117 (julho de 2016): 59–68. http://dx.doi.org/10.1016/j.toxicon.2016.03.020.

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MIJAV, H., M. BURTON e N. YOUNG. "168 Cross-reactivity of extracts of cladosporium species and alternaria alternata". Journal of Allergy and Clinical Immunology 87, n.º 1 (janeiro de 1991): 180. http://dx.doi.org/10.1016/0091-6749(91)91451-x.

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Dimitrov, Ivan, e Mariana Atanasova. "AllerScreener – A Server for Allergenicity and Cross-Reactivity Prediction". Cybernetics and Information Technologies 20, n.º 6 (1 de dezembro de 2020): 175–84. http://dx.doi.org/10.2478/cait-2020-0071.

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Abstract Allergenicity of proteins is a subtle property encoded in their structures. The prediction of allergenicity of novel proteins saves time and resources for subsequent experimental work. In the host antigen-presenting cells, the allergens are processed as antigens by the means of Human Leukocyte Antigens (HLA) class II proteins. Sometimes, people allergic to a given protein show allergic reaction to a different protein, even when the two proteins have different routes of exposure. This phenomenon is termed cross-reactivity. Here, we describe a server for allergenicity and cross-reactivity prediction based on the abilities of allergenic proteins to generate binders to HLA class II proteins. The generated peptides are compared to HLA binders originating from known allergens. As a result, the server returns a list of common binders, origin proteins, and species. Different species generate common HLA binders and this determines their cross-reactivity. The server is named AllerScreener and is freely accessible at: http://www.ddg-pharmfac.net/AllerScreener .

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FAIRLIE-CLARKE, KAREN J., CHRISTINA HANSEN, JUDITH E. ALLEN e ANDREA L. GRAHAM. "Increased exposure to Plasmodium chabaudi antigens sustains cross-reactivity and avidity of antibodies binding Nippostrongylus brasiliensis: dissecting cross-phylum cross-reactivity in a rodent model". Parasitology 142, n.º 14 (22 de outubro de 2015): 1703–14. http://dx.doi.org/10.1017/s0031182015001390.

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SUMMARYMounting an antibody response capable of discriminating amongst and appropriately targeting different parasites is crucial in host defence. However, cross-reactive antibodies that recognize (bind to) multiple parasite species are well documented. We aimed to determine if a higher inoculating dose of one species, and thus exposure to larger amounts of antigen over a longer period of time, would fine-tune responses to that species and reduce cross-reactivity. Using the Plasmodium chabaudi chabaudi (Pcc)–Nippostrongylus brasiliensis (Nb) co-infection model in BALB/c mice, in which we previously documented cross-reactive antibodies, we manipulated the inoculating dose of Pcc across 4 orders of magnitude. We investigated antigen-specific and cross-reactive antibody responses against crude and defined recombinant antigens by enzyme linked immunosorbent assay, Western blot and antibody depletion assays. Contrary to our hypothesis that increasing exposure to Pcc would reduce cross-reactivity to Nb, we found evidence for increased avidity of a subpopulation of antibodies that recognized shared antigens. Western blot indicated proteins of apparent monomer molecular mass 28 and 98 kDa in both Nb and Pcc antigen preparations and also an Nb protein of similar size to recombinant Pcc antigen, merozoite surface protein-119. The implications of antibodies binding antigen from such phylogenetically distinct parasites are discussed.

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GONDIM, LUÍS F. P., JOSÉ R. MINEO e GEREON SCHARES. "Importance of serological cross-reactivity amongToxoplasma gondii, Hammondiaspp.,Neosporaspp.,Sarcocystisspp. andBesnoitia besnoiti". Parasitology 144, n.º 7 (28 de fevereiro de 2017): 851–68. http://dx.doi.org/10.1017/s0031182017000063.

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SUMMARYToxoplasma gondii, Neosporaspp.,Sarcocystisspp.,Hammondiaspp. andBesnoitia besnoitiare genetically related cyst-forming coccidia. Serology is frequently used for the identification ofT. gondii, Neosporaspp. andB. besnoiti-exposed individuals. Serologic cross-reactions occur in different tests among animals infected withT. gondiiandH. hammondi,as well as among animals infected byT. gondiiandN. caninum. Infections caused byN. caninumandN. hughesiare almost indistinguishable by serology.Neospora caninum, B. besnoitiandSarcocystisspp. infections in cattle show some degree of serologic cross-reactivity. Antibody cross-reactivity betweenNeosporaspp. andH. heydorni-infected animals is suspected, but not proven to occur. We review serologic cross-reactivity among animals and/or humans infected withT. gondii, Neosporaspp.,Sarcocystisspp.,Hammondiaspp. andB. besnoiti. Emphasis is laid upon antigens and serological methods forN. caninumdiagnosis which were tested for cross-reactivity with related protozoa. Species-specific antigens, as well as stage-specific proteins have been identified in some of these parasites and have promising use for diagnosis and epidemiological surveys.

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Canettieri, Antonio Carlos Victor, Fujiko Yamasiro Kretchetoff, Cristiane Yumi Koga-Ito, Daniella Moreira, Fabio José Condino Fujarra e Carmelinda Schmidt Unterkircher. "Production of monoclonal antibodies against Streptococcus mutans antigens". Brazilian Oral Research 20, n.º 4 (dezembro de 2006): 297–302. http://dx.doi.org/10.1590/s1806-83242006000400003.

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Several studies have been conducted in the last decades aiming to obtain an anti-caries vaccine, however some studies have demonstrated cross reactivity between Streptococcus mutans surface antigens and the human cardiac tissue. In this work, the reactivity of five anti-Streptococcus mutans monoclonal antibodies (MoAb) (24A, 56G, C8, E8 and F6) was tested against oral streptococci, cardiac antigens and skeletal and cardiac myosins, aiming to evaluate the specificity of these MoAb. The hybrid producers of immunoglobulins of the IgG2b class were cloned by limit dilution and expanded in vivo. MoAb were tested by ELISA. The hybrid 24A reacted with S. mutans CCT 1910, S. salivarius CCT 0365 and S. pyogenes T23. No reactivity difference was observed among the tested species. Cross reactivity with heart and cardiac myosin was not confirmed and only reaction with myosin of skeletal muscle was observed (p = 0.0381). The hybrid 56G reacted with all the tested microorganisms and there was statistically significant difference between S. mutans and S. pyogenes T23 (p < 0.001). This hybrid also reacted with myosin of skeletal muscle (p = 0.0095). C8, E8 and F6 presented low reactivity against oral streptococci strains and no reactivity against cardiac antigens. The data of this study showed that the 24A and 56G anti-S. mutans MoAb presented reactivity with S. pyogenes and S. salivarius, reinforcing the occurrence of common antigens between these species. The tested MoAb presented low cross-reactivity with myosin of skeletal muscle, but anti-heart activity could not be confirmed.

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Grifoni, Alba, Hannah Voic, John Sidney, Aruna D. de Silva, Anna Durbin, Sean A. Diehl, Eva Harris, Alessandro Sette e Daniela Weiskopf. "Crosseactivity of flaviviruses specific CD8+T cell responses across different viral species". Journal of Immunology 202, n.º 1_Supplement (1 de maio de 2019): 76.12. http://dx.doi.org/10.4049/jimmunol.202.supp.76.12.

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Abstract Several flaviviruses, including Dengue Virus (DENV), Zika Virus (ZIKV), Japanese Encephalitis Virus (JEV), West Nile Virus (WNV), and Yellow Fever Virus (YFV), share significant sequence homology and often circulate in the same geographical regions. Significant levels of cross-reactivity could in turn result in pre-existing T cell immunity modulating T cell responses to subsequent flavivirus infections or vaccination. Whether and to what extent cross-reactivity at the level of CD8 responses is detected is currently unclear. Thus we designed pools of epitopes and predicted HLA binding peptides derived from DENV, ZIKV, JEV, WNV and YFV. We then used PBMC of individuals vaccinated with DENV or YF to test their potential to recall antigen specific CD8 memory T cell response in an Intracellular Cytokine Staining (ICS) assay. Significant cross-reactivity of CD8 T cell responses against several of the pools was observed both in the case of DENV and YF vaccinees, but the extent of cross-reactivity varied as a function of the flavivirus species considered, and the cross-reactive responses were significantly lower than the responses to the autologous virus. Phenotypic analyses showed a suboptimal expression of activation markers in cross-reactive responses. We are currently characterizing cross-reactive responses at the single epitope level, and in PBMCs from donors naturally exposed to flaviviruses. Characterization of the extent and functionality of CD8 cross-reaction across different flaviviruses will contribute to the understanding of immunity in the natural infection, and has particular implications for vaccine efficacy and safety in endemic settings.

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Nollens, Hendrik H., Carolina Ruiz, Michael T. Walsh, Frances M. D. Gulland, Gregory Bossart, Eric D. Jensen, James F. McBain e James F. X. Wellehan. "Cross-Reactivity between Immunoglobulin G Antibodies of Whales and Dolphins Correlates with Evolutionary Distance". Clinical and Vaccine Immunology 15, n.º 10 (3 de setembro de 2008): 1547–54. http://dx.doi.org/10.1128/cvi.00219-08.

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ABSTRACT Growing morphological and molecular evidence indicates that the porpoises, dolphins, and whales evolved within the even-toed ungulates, formerly known as Artiodactyla. These animals are now grouped in the Cetartiodactyla. We evaluated the antigenic similarity of the immunoglobulin G (IgG) molecules of 15 cetacean species and the domestic cow. The similarity was scored using three distinct antibodies raised against bottlenose dolphin (Tursiops truncatus) IgG in a Western blot, an indirect enzyme-linked immunosorbent assay (ELISA), and a competitive ELISA format. A score was generated for the genetic distance between each species and T. truncatus using the cytochrome b sequence. Each antibody displayed a distinct pattern of reactivity with the IgG antibodies of the various species. The monoclonal antibody (MAb) specific for the γ heavy chain of T. truncatus was reactive with all monodontids, delphinids, and phocoenids. The light-chain-specific MAb reacted with IgG of delphinoid and phocoenid species and one of the two mysticete species tested. The polyclonal antibody was broadly cross-reactive across all cetaceans and the domestic cow. Using the MAb specific for the γ heavy chain, the degree of IgG cross-reactivity ranged from less than 17% for the mysticetes to 106% for killer whale Orcinus orca. The IgG in beaked whale and baleen whale sera was significantly less cross-reactive with bottlenose dolphin IgG than sera from other toothed whales. A strong negative correlation was demonstrated between antigenic cross-reactivity of IgG molecules and the genetic distance of their hosts. The data generated will be useful for the development of clinical serodiagnostics in diverse cetacean species.

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Ochiai, Yoshihiro, Teruki Kobayashi, Akihiro Handa, Shugo Watabe e Kanehisa Hashimoto. "Immunological cross-reactivity of myosin light chains from various species of fish." NIPPON SUISAN GAKKAISHI 55, n.º 12 (1989): 2151–56. http://dx.doi.org/10.2331/suisan.55.2151.

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Bonura, Angela, Anna Artale, Mauro Marino, Saverio Amoroso, Francesco Marcucci, Domenico Geraci e Paolo Colombo. "Cross-reactivity between Parietaria species using the major rParj1 and rParj2 allergens". Allergy and Asthma Proceedings 27, n.º 5 (1 de setembro de 2006): 378–82. http://dx.doi.org/10.2500/aap.2006.27.2927.

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37

Restani, P., A. Fiocchi, B. Beretta, T. Velonà, M. Giovannini e C. L. Galli. "Meat allergy: III—Proteins involved and cross-reactivity between different animal species." Journal of the American College of Nutrition 16, n.º 4 (agosto de 1997): 383–89. http://dx.doi.org/10.1080/07315724.1997.10718701.

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Haider, Kh Husnain, e W. H. Stimson. "Bovine cardiac troponin-I specific monoclonal antibodies which show species cross reactivity". Experimental & Molecular Medicine 28, n.º 2 (junho de 1996): 71–76. http://dx.doi.org/10.1038/emm.1996.11.

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39

Fichorova, R. N., L. S. Nakov e S. D. Kyurkchiev. "Inter-species cross-reactivity of human sperm antibodies demonstrated by immunoenzyme method". Journal of Reproductive Immunology 15 (julho de 1989): 55. http://dx.doi.org/10.1016/0165-0378(89)90129-0.

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40

Zhao, Xin, Thiago Luiz Alves e. Silva, Laura Cronin, Amy F. Savage, Michelle O’Neill, Barbara Nerima, Loyce M. Okedi e Serap Aksoy. "Immunogenicity and Serological Cross-Reactivity of Saliva Proteins among Different Tsetse Species". PLOS Neglected Tropical Diseases 9, n.º 8 (27 de agosto de 2015): e0004038. http://dx.doi.org/10.1371/journal.pntd.0004038.

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UCHIDA, Tatsuya, HASBULLAH, Takashi NAKAMURA, Yutaka NAKAI e Keiji OGIMOTO. "Cross Reactivity of Serum Antibodies from Chickens Immunized with Three Eimerian Species." Journal of Veterinary Medical Science 56, n.º 5 (1994): 1021–23. http://dx.doi.org/10.1292/jvms.56.1021.

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Nishikawa, A. K., C. P. Caricati, M. L. S. R. Lima, M. C. Dos Santos, T. L. Kipnis, V. R. D. Eickstedt, I. Knysak, M. H. Da Silva, H. G. Higashi e W. Dias Da Silva. "Antigenic cross-reactivity among the venoms from several species of Brazilian scorpions". Toxicon 32, n.º 8 (agosto de 1994): 989–98. http://dx.doi.org/10.1016/0041-0101(94)90377-8.

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Nishikawa, A. K., C. P. Caricati, M. L. S. R. Lima, M. C. dos Santos, T. L. Kipnis, V. R. D. Eickstedt, I. Knysak, M. H. Da Silva, H. G. Higashi e W. Dias da Silva. "Antigenic cross-reactivity among the venoms from several species of Brazilian scorpions". Toxicon 33, n.º 3 (março de 1995): 287. http://dx.doi.org/10.1016/0041-0101(95)99315-t.

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Yamashiro, Yuki, Hiroshi Taniguchi, Shigaeki Baba, Teiichi Taniguchi, Shigeo Aono, Gen Isshiki e Tomio Jinnouchi. "Heterogeneity of human islet cell antibodies in terms of cross-species reactivity". Diabetes Research and Clinical Practice 8, n.º 1 (janeiro de 1990): 13–17. http://dx.doi.org/10.1016/0168-8227(90)90090-g.

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45

Henrich, Vincent C. "Comparison of ecdysteroid production inDrosophila andManduca: Pharmacology and cross-species neural reactivity". Archives of Insect Biochemistry and Physiology 30, n.º 2-3 (1995): 239–54. http://dx.doi.org/10.1002/arch.940300212.

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Fleischauer, Valerie E., Salvador B. Muñoz III, Peter G. N. Neate, William W. Brennessel e Michael L. Neidig. "NHC and nucleophile chelation effects on reactive iron(ii) species in alkyl–alkyl cross-coupling". Chemical Science 9, n.º 7 (2018): 1878–91. http://dx.doi.org/10.1039/c7sc04750a.

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47

Yamada, Yohko, Koji Okamoto e Ikuo Takeuchi. "Comparison of spore proteins among species of the cellular slime moulds Dictyostelium and Polysphondylium as examined by immunological cross-reactivity". Canadian Journal of Microbiology 34, n.º 7 (1 de julho de 1988): 891–96. http://dx.doi.org/10.1139/m88-154.

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Spore proteins of six cellular slime mould species, Dictyostelium discoideum, D. mucoroides, D. purpureum, D. lacteum, Polysphondylium violaceum, and P. pallidum were studied. The spore proteins were cross-reacted with four different polyclonal antibodies produced against D. mucoroides spores and D. discoideum major spore coat proteins SP96, SP70, and SP60 by SDS polyacrylamide gel electrophoresis and immunoblotting. The spore proteins of D. discoideum and D. mucoroides showed the strongest cross-reactivity with all the antisera and also produced many common protein bands, thus reflecting their morphological similarities. Polysphondylium violaceum, which is quite distinct in morphology from D. discoideum and D. mucoroides, produced the second strongest cross-reactivity. In contrast, the proteins of D. purpureum showed little cross-reactivity, although morphologically it closely resembles D. mucoroides. The developmental changes of these spore proteins were investigated by cross-reacting the antisera against vegetative and slug cell proteins. In the cases of D. discoideum and D. mucoroides, the band patterns of slug proteins coincided with those of spores, which suggested that most of the spore proteins had already accumulated at the slug stage. However, this was not the case with P. violaceum, which suggested that spore proteins of this species cross-reactive with the antisera were synthesized or modified at the culmination stage.

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48

Afong, Michael, Kimberley A. Olynyk, Hasmukh V. Patel, John Arnold, Shuen-Kuei Liao e Karl B. Freeman. "Immunological studies of the uncoupling protein of brown adipose tissue". Canadian Journal of Biochemistry and Cell Biology 63, n.º 2 (1 de fevereiro de 1985): 96–101. http://dx.doi.org/10.1139/o85-014.

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The immunological relationship of the uncoupling protein from brown adipose tissue of several mammalian species was examined by using a rabbit antibody preparation against the rat protein. Complete cross-reactivity of the antibody to the protein from hamster, mouse, and rat was found, whereas the protein from rabbit cross-reacted only 25%. Cross-reactivity was also found with the human uncoupling protein, although the human protein was found to be about 1 kdalton smaller than the rat protein. No protein of the size of the uncoupling protein was detected in several tumor cell lines examined.

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49

Borel, Nicole, Nicola Casson, José M. Entenza, Carmen Kaiser, Andreas Pospischil e Gilbert Greub. "Tissue microarray and immunohistochemistry as tools for evaluation of antibodies against Chlamydia-like bacteria". Journal of Medical Microbiology 58, n.º 7 (1 de julho de 2009): 863–66. http://dx.doi.org/10.1099/jmm.0.009159-0.

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Tissue microarray technology was used to establish immunohistochemistry protocols and to determine the specificity of new antisera against various Chlamydia-like bacteria for future use on formalin-fixed and paraffin-embedded tissues. The antisera exhibited strong reactivity against autologous antigen and closely related heterologous antigen, but no cross-reactivity with distantly related species.

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50

Neal, Frances, Joanne Arnold, Christine J. Rossant, Sadhana Podichetty, David Lowne, Claire Dobson, Trevor Wilkinson, Caroline Colley, Rob Howes e Tristan J. Vaughan. "Isolation of Potent CGRP Neutralizing Antibodies Using Four Simple Assays". Journal of Biomolecular Screening 21, n.º 1 (8 de outubro de 2015): 24–34. http://dx.doi.org/10.1177/1087057115610070.

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Calcitonin gene-related peptide (CGRP) is a small neuropeptide and a potent vasodilator that is widely associated with chronic pain and migraine. An antibody that inhibits CGRP function would be a potential therapeutic for treatment of these disorders. Here we describe the isolation of highly potent antibodies to CGRP from phage and ribosome display libraries and characterization of their epitope, species cross-reactivity, kinetics, and functional activity. Homogenous time-resolved fluorescence (HTRF) binding assays identified antibodies with the desired species cross-reactivity from naïve libraries, and HTRF epitope competition assays were used to characterize and group scFv by epitope. The functional inhibition of CGRP and species cross-reactivity of purified scFv and antibodies were subsequently confirmed using cAMP assays. We show that epitope competition assays could be used as a surrogate for functional cell-based assays during affinity maturation, in combination with scFv off-rate ranking by biolayer interferometry (BLI). This is the first time it has been shown that off-rate ranking can be predictive of functional activity for anti-CGRP antibodies. Here we demonstrate how, by using just four simple assays, diverse panels of antibodies to CGRP can be identified. These assay formats have potential utility in the identification of antibodies to other therapeutic targets.

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