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Journal articles on the topic "Cross-species reactivity":
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ARLIAN, L., C. RAPP, and E. FERNANDEZCALDAS. "Allergenicity of and its cross-reactivity with species." Journal of Allergy and Clinical Immunology 91, no. 5 (May 1993): 1051–58. http://dx.doi.org/10.1016/0091-6749(93)90219-6.
SU, JUI-LAN, STEVE STIMPSON, CHRISTINE EDWARDS, JOHN VAN ARNOLD, SUSAN BURGESS, and PEIYUAN LIN. "Neutralizing IGF-1 Monoclonal Antibody With Cross-Species Reactivity." Hybridoma 16, no. 6 (December 1997): 513–18. http://dx.doi.org/10.1089/hyb.1997.16.513.
Christensen, L. H., C. Hejl, H. Henmar, N. Johansen, and H. Ipsen. "Extensive IgE Cross-reactivity towards Different US Ragweed Species." Journal of Allergy and Clinical Immunology 125, no. 2 (February 2010): AB17. http://dx.doi.org/10.1016/j.jaci.2009.12.098.
Losada, S., N. Chacón, C.Colmenares, H. Bermúdez, A. Lorenzo, J. P. Pointier, A. Theron, B. Alarcón de Noya, and O. Noya. "Schistosoma: Cross-reactivity and antigenic community among different species." Experimental Parasitology 111, no. 3 (November 2005): 182–90. http://dx.doi.org/10.1016/j.exppara.2005.07.007.
Gersten, Douglas M., and Vincent J. Hearing. "Antigens of Murine Melanoma and Their Cross-Species Reactivity." Pathobiology 60, no. 1 (1992): 49–56. http://dx.doi.org/10.1159/000163697.
Van den Bossche, D., A. De Bel, M. Hendrickx, A. De Becker, R. Jacobs, A. Naessens, and D. Pierard. "Galactomannan Enzymatic Immunoassay Cross-Reactivity Caused by Prototheca Species." Journal of Clinical Microbiology 50, no. 10 (July 25, 2012): 3371–73. http://dx.doi.org/10.1128/jcm.01028-12.
Gupta, R., B. P. Singh, S. Sridhara, S. N. Gaur, R. Kumar, V. K. Chaudhary, and N. Arora. "Allergenic cross-reactivity ofCurvularia lunatawith other airborne fungal species." Allergy 57, no. 7 (July 2002): 636–40. http://dx.doi.org/10.1034/j.1398-9995.2002.03331.x.
Conrad, Melanie L., William C. Davis, and Ben F. Koop. "TCR and CD3 antibody cross-reactivity in 44 species." Cytometry Part A 71A, no. 11 (2007): 925–33. http://dx.doi.org/10.1002/cyto.a.20435.
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.
Dissertations / Theses on the topic "Cross-species reactivity":
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Beale, Janine. "Molecular characterisation of parvalbumin and analysis of cross-reactivity in five fish species using sera from fish-allergic consumers and occupationally exposed workers." Master's thesis, University of Cape Town, 2008. http://hdl.handle.net/11427/3223.
Includes abstract. Includes bibliographical references (leaves 101-108). Parvalbumin, the fish major allergen, accounts for over 95% of clinical symptoms in allergic fish consumers. Importantly, this allergen displays lgE cross-reactivity thus allergic sufferers can exhibit clinical symptoms after the ingestion of non-sesitising fish species. In an occupational setting, fish products have also been shown to cause allergic disease in fish-processing factory workers. Whether parvalbumin is a causative allergen in this occupational environment is unknown. The aim of this study was to evaluate IgE reactivity to parvalbumin and other fish fillet proteins using sera from domestic consumers with ingestion-induced fish allergies and sera from occupationally exposed allergic workers. In addition, cross-reactivity among parvalbumins from five highly consumed fish species in South Africa were assessed by immunoblotting and the most cross-reactive species was characterised further. Pilchard parvalbumin was identified as the most cross-reactive allergen in fish-allergic consumers. The cDNA sequenceß form of pilchard parvalbumin was determined. This is the first time that parvalbumin from the fish order, Clupeiformes, has been characterised and represents a crucual primary step towards the generation of a recombinant form for potential diagnostic and therapeutic use in allergic individuals. Interestingly, sera IgE from fish-processing factory workers displayed no bing to parvalbumin, nor any other fish fillet proteins in immunoblotting. This result has raised several intriguing questions. Namely, does parvalbumin lack the intrinsic features required for eliciting allergic symptoms via inhalation and/or contact, as are primary routes of exposure in workers? Alternatively, could causative occupational allergens that appear to be absent in the fillet of fish occur in the enzyme-rich digestive tract or potentially the skin of fish species? Future studies aim to addess these questions amongst others, which will contribute to preventative and therapeutic strategies of occupational allergies in workers.
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Pruvost, Tiphanie. "Ingénierie moléculaire de la réactivité croisée inter-espèces d’anticorps thérapeutiques par Yeast Surface Display." Electronic Thesis or Diss., université Paris-Saclay, 2023. http://www.theses.fr/2023UPASQ074.
Le succès des anticorps monoclonaux comme outils thérapeutiques s'explique en partie par leur grande spécificité pour leur cible. Celle-ci implique souvent qu'un anticorps développé contre une cible humaine échoue à la reconnaître chez les espèces utilisées lors des essais précliniques. L'objectif de ces travaux est de développer une méthode d'ingénierie de protéine permettant à un anticorps de reconnaître un antigène provenant d'espèces différentes en utilisant comme modèles deux anticorps reconnaissant la protéine LAMP1 humaine mais pas ses versions murine et simienne. Durant ce projet le principe de mutagénèse exhaustive à l'acide aminé près (DMS) est couplé à l'expression de protéines à la surface des levures (YSD) ainsi qu'à la cytométrie en flux. Une première partie détaille l'utilisation de la combinaison de ces techniques pour l'identification des épitopes des deux anticorps sur LAMP1 humain. Les acides aminés situés dans les épitopes ont alors pu être comparés à ceux des protéines murine et simienne ce qui a permis d'expliquer l'absence de reconnaissance pour ces deux protéines. La seconde partie décrit la stratégie d'ingénierie protéique développée sur ces deux anticorps. L'expression des banques de DMS à la surface des levures a permis de sélectionner des mutations améliorant la reconnaissance croisée de LAMP1 sans affecter la fonctionnalité de l'anticorps. Ces mutations ont alors été combinées dans une nouvelle banque qui a été à nouveau criblée à plusieurs reprises pour en extraire les variants les plus promoteurs. L'affinité de ces variants pour différents orthologues de LAMP1 a pu être évaluée afin de confirmer l'efficacité de la stratégie grâce à laquelle plusieurs variants cross-réactifs ont pu être obtenus pour les deux anticorps étudiés Success of the monoclonal antibodies as therapeutic tools is partly due to their high specificity for their targets. Because of this high specificity antibodies developed against a human target often fail to recognize this target in animals used as models in preclinical trials. Thus, the goal of this study is to develop a protein engineering method aiming at conferring an antibody the ability to recognize a same antigen belonging to different species. To do so, two antibodies recognizing the human LAMP1 protein but not the murine and simian LAMP1 are used as models. In this project an exhaustive mutagenesis (DMS) monitored by Yeast Surface Display (YSD) and flow cytometry. The first part describes how these technics are combined in order to identify the epitopes of two antibodies on human LAMP1. The amino acids of epitopes are compared to those of murine and simian LAMP1 to explain the lack of recongnition of this two proteins. The second part focuses on the engineering strategy developped on the two antibodies. The expression of the DMS libraries in YSD allowed to select single mutations improving the cross-reactivity on LMAP1 without affecting the functionality of the antibodies. These mutations have been combined in a second library that has been screened for promissing variants. The affinities of these variants for differents human et simian LAMP1 orthologs has been measured to confirm the succes of the strategy. For each antibody many cross-reactive variants have been obtained
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Shepertycky, Martha Roma. "Humoral immune response in mice following immunization with Prevotella intermedia and cross-reactivity with species of Prevotella, Bacteroides and Porphyromonas." 1992. http://hdl.handle.net/1993/18652.
Book chapters on the topic "Cross-species reactivity":
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Fu, Linglin, Bobby J. Cherayil, Haining Shi, Yanbo Wang, and Yang Zhu. "Species and Structure of Food Allergens: Epitopes and Cross-Reactivity." In Food Allergy, 13–39. Singapore: Springer Singapore, 2019. http://dx.doi.org/10.1007/978-981-13-6928-5_2.
Mohr, H., J. Knüver-Hopf, J. Atzpodien, H. Kirchner, and U. Pohl. "Antibodies to Interleukin-2 (IL-2) in Patients: Cross Reactivity with Different IL-2 Species." In Cytokines in Hemopoiesis, Oncology, and AIDS, 751–56. Berlin, Heidelberg: Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-75510-1_95.
Chen, Ming, and Nian-hui Zhou. "IMMUNOLOGICAL CROSS REACTIVITY OF PARAMYOSINS OF THE STRIATED MUSCLE FROM VARIOUS SPECIES OF ANIMALS." In Retrospect and Prospect of Protein Research, 56–60. WORLD SCIENTIFIC, 1991. http://dx.doi.org/10.1142/9789814360425_0014.
infect a number of host species. This host range is given by an ecological filter (the possibility of encounter) and a physiological one (the capacity of establishing an infection). Host ranges typically are right-skewed, with most parasites infecting only a few, but few infecting very many hosts. There is no universally valid hypothesis that explains host range. However, a number of factors contribute to host range, such as geographical range, phylogenetic distance, host predictability, and parasite virulence. Specificity and cross-reactivity of immune defences are important mechanisms. Moreover, immune memory is based on specificity; transgenerational immune priming protects offspring when parents have already been exposed to the same or similar parasites.
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Rodrigo-Garcia, Maria, Esther Rodriguez-de Haro, Salvador Priego-Poyato, Elena Lima-Cabello, Sonia Morales-Santana, and Jose C. Jimenez-Lopez. "Molecular and Functional Characterisation of Allergenic Non-specific Lipid Transfer Proteins of Sweet Lupin Seed Species." In Legumes Research - Volume 1 [Working Title]. IntechOpen, 2022. http://dx.doi.org/10.5772/intechopen.102889.
Non-specific lipid transfer proteins (nsLTPs) are small proteins abundant in plants, which function in transferring phospholipids and galactolipids across the membrane. nsLTPs also play a key role in plant resistance to biotic and abiotic stresses, growth and development, as well as in sexual reproduction, seed development, and germination. In addition, these proteins have previously been identified as food allergens. In the present study, we carried out a molecular and functional comparative characterisation of 25 sequences of nsLTPs of lupin legumes and other species. Extensive analysis was carried out; including comparison of databases, phylogeny, physical–chemical properties, functional properties of post-translational modifications, protein structure conservation, 2-D and 3D modelling, functional interaction analysis, and allergenicity including identification of IgE, T-cell, and B-cell binding epitopes. The results indicated that particular structural features of nsLTPs are essential to the functionality of these proteins, high level of structural stability and conservation. Information about different functional interactions between nsLTPs and ligands showed that nsLTPs can accommodate several of them with different structure; and that the relationship between structure and allergenicity was investigated through the identification of epitopes susceptible of being involved in cross-reactivity between species of the Fabaceae family.
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Taber, Douglass. "Developments in Alkene and Alkyne Metathesis." In Organic Synthesis. Oxford University Press, 2011. http://dx.doi.org/10.1093/oso/9780199764549.003.0025.
Jon D. Rainier of the University of Utah has put forward (J. Am. Chem. Soc. 2007 , 129 , 12604) an elegant alternative to Ru-catalyzed alkene metathesis, demonstrating that an ω-alkenyl ester such as 1 will cyclize to the enol ether 2 under Tebbe conditions. The particular reactivity of free alcohols in Ru-catalyzed alkene metathesis is underscored by the observation (Tetrahedron Lett. 2007, 48, 6905) by Javed Iqbal of Dr. Reddy’s Laboratories, Ltd., Miyapur that attempted metathesis of the ether 4a failed, but metathesis of the diol 4b proceeded efficiently. Kazunori Koide of the University of Pittsburgh has demonstrated (Organic Lett. 2007, 9, 5235) that the yields of cross-metathesis with an alkenyl alcohol could be enhanced by binding it to a trityl resin. He observed that the Grela catalyst 8 was particularly effective in this application. Residual Ru species do not interfere with some subsequent transformations. Rodrigo B. Andrade of Temple University has demonstrated (Tetrahedron Lett. 2007, 48, 5367) that metathesis with an α, β-unsaturated aldehyde such as 11 can be followed directly by phosphonate condensation to give the doubly-homologated product 12. Philip J. Parsons of the University of Sussex has found (Organic Lett. 2007, 9, 2613) that the nitro functional group is compatible with the Ru catalyst. The product nitro alkene 15 could be cyclized (intramolecular Michael addition) to the cyclopentane 16, or (intramolecular dipolar cycloaddition) to the cyclopentane 17. There has been much interest in carrying out the several alkene metathesis transformations (cross metathesis, ring closing metathesis, ring-opening metathesis polymerization) in water. Robert H. Grubbs of the California Institute of Technology has designed (Angew. Chem. Int. Ed. 2007, 46, 5152) the ammonium salt 18 for this purpose, and Karol Grela of the Polish Academy of Sciences in Warsaw and Marc Mauduit of ENSC Rennes have jointly(Chem. Commun. 2007, 3771) put forward the pyridinium salt 19. Remarkably, Ronald T. Raines of the University of Wisconsin has shown (Organic Lett. 2007, 9, 4885) that the Hoveyda catalyst 20 is sufficiently stable in aqueous acetone and aqueous DME to function efficiently.
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O.M. Al-Dahmoshi, Hussein, and Hayder J. Al-Nayili. "Mitochondrial 16S rRNA Gene-Dependent Blood Typing as a Forensic Tool." In Forensic Analysis [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.98248.
Mitochondrial DNA is an important tool for human identification and is used to differentiate between human and animal blood at the crime scene, because in extreme conditions nuclear DNA is severely destroyed while Mitochondrial DNA contains multiple copies (200–2000) per cell and resists harsh and more stable conditions. Seventy-two blood samples were collected from humans (Homo sapiens), sheep (Ovis aries), goats (Capra hircus), and cows (Bos taurus) (18 blood samples for each). All blood samples were withdrawn by a technician and 5 ml were aspirated using an aseptic technique and transferred to EDTA-Na2 tubes. They were mixed well and stored in a refrigerator. The collection took 2 weeks (May 15, 2019–May 30, 2019). All samples were collected from Al-Diwanyia city. The results of PCR testing revealed that the primer pairs were specific and non-specific products did not appear for all samples. The amplification of Homo sapiens mitochondrial DNA with primer pairs of other (Ovis aries, Capra hircus, and Bos taurus) and amplification of each with primer pairs of another genus gave negative results, and this is primary evidence for primer pair specificity. The amplicon of 16S rRNA gene of Homo sapiens was 1200 bp, Ovis aries was 1060 bp, Capra hircus was 820 bp, and Bos taurus was 1300 bp. The sequencing revealed that no cross-reactivity of designed primer pairs and the PCR assay based on the designed primer pairs will be simple, fast, sensitive, specific, and cost-effective. There is sensitivity, specificity, and accuracy in the designed species-specific primer pairs and applicability of the designed primer pairs in forensics to investigate blood spots or evidence belonging for human, sheep, goat, and cow.
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Osbourn, Jane K. "Selection of antibodies from phage libraries of immunoglobulin genes." In Monoclonal Antibodies, 67–89. Oxford University PressOxford, 2000. http://dx.doi.org/10.1093/oso/9780199637232.003.0003.
Abstract This chapter explains the various approaches it is possible to take in the selection of phage antibodies with specific binding characteristics from large phage display libraries. The particular selection approach taken will be determined by the form and availability of the starting antigen and the desired properties of the selected antibody. One of the main benefits of the phage display approach to antibody generation is the ability to tailor the selection regime to generate antibodies with particular characteristics such as: high affinity, neutralization potency, ability to recognize specific epitopes, or to recognize specific cell types. A variety of screening regimes can also be employed to identify antibodies that can be utilized for particular applications such as: Western blot reagents, immunocytochemistry reagents, or species cross-reactivity. The phage system provides a route to the generation of antibodies to antigens that are normally inaccessible using conventional immunization techniques, for example mAbs to toxic moieties, carbohydrate-containing molecules, and anti-self antigens can easily be selected using the appropriate conditions. Methods for the generation of phage antibody libraries from immunized rodents are described elsewhere (Chapter 2) and these techniques are equally applicable to the generation of human phage antibody libraries if appropriate primers are used (1). The selec tion methods described here can be employed for immunoglobulin genes dis played in scFv, Fab, or diabody formats. The methods described provide a necessarily brief outline of the possible approaches and it should be stressed that there are no hard and fast rules for selection protocols; investigators should use as much imagination as possible in designing selection procedures which will best suit the final application of the antibody. Possible selection methods such as in vivo selection (2), selective infective phage selections (3, 4), and various deselection methods (e.g. 5) have not been discussed in detail here and reference should be made to the appropriate literature for further ideas on these approaches.
Conference papers on the topic "Cross-species reactivity":
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Knaack, A., A. Offt, T. Mill, J. Walewski, and W. Schade. "Picosecond-LIF-Spectroscopy with NO in a High Pressure Cell." In Modern Spectroscopy of Solids, Liquids, and Gases. Washington, D.C.: Optica Publishing Group, 1995. http://dx.doi.org/10.1364/msslg.1995.sthb6.
Flame radicals are fragments of molecules with high reactivity and control the process of combustion to a high degree. Therefore, the knowledge of accurate number densities of these species is very important, e.g. when modelling flames. Because of the relative large cross sections compared to other optical methods, laser-induced fluorescence (LIF) spectroscopy is one of the most sensitive techniques for accurate determination of concentrations and temperatures [1]. However, when LIF is applied for quantitative diagnostics at high pressures (10 bar >p> 1 bar) and high temperatures, which is typical for industrial combustions, several problems associated with the LIF-method itself appear, and limit the accuracy of the method. The laser excites an upper level population of the molecule or atom under investigation, which decays by spontaneous emission and radiationless by collisional induced processes (quenching). The latter one reduces the fluorescence yield considerably, two or three orders of magnitude are typical for atmospheric pressure. If the measurements are performed with a time resolution better than the quenching rates, the LIF-intensities can be used to extract absolute number densities. However, this requires a laser and a detection system with picosecond time resolution. Since important atomic radicals like O, C, N, H or diatomic molecules like NO, CO and OH can only be excited from the ground state via two- or one photon absorption in the spectral range between 200 and 300 nm [2] a powerful ultraviolet laser system is required in these experiments. However, the quantitative interpretation of the picosecond LIF-intensity measurements still needs accurate quenching rate data for the relevant pressures and temperatures and the species that are present in the combustion process. In the data analysis also systematic influences like photodissociation effects by the strong uv-laser pulses have to be considered. Therefore, in this paper improved quenching rate measurements of NO with NO, N2 and O2 for pressures up to p=10 bar, and photodissociation effects of NO are reported.
Reports on the topic "Cross-species reactivity":
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Barefoot, Susan F., Bonita A. Glatz, Nathan Gollop, and Thomas A. Hughes. Bacteriocin Markers for Propionibacteria Gene Transfer Systems. United States Department of Agriculture, June 2000. http://dx.doi.org/10.32747/2000.7573993.bard.
The antibotulinal baceriocins, propionicin PLG-1 and jenseniin G., were the first to be identified, purified and characterized for the dairy propionibaceria and are produced by Propionibacterium thoenii P127 and P. thoenii/jensenii P126, respectively. Objectives of this project were to (a) produce polyclonal antibodies for detection, comparison and monitoring of propionicin PLG-1; (b) identify, clone and characterize the propionicin PLG-1 (plg-1) and jenseniin G (jnG) genes; and (3) develop gene transfer systems for dairy propionibacteria using them as models. Polyclonal antibodies for detection, comparison and monitoring of propionicin PLG-1 were produced in rabbits. Anti-PLG-1 antiserum had high titers (256,000 to 512,000), neutralized PLG-1 activity, and detected purified PLG-1 at 0.10 mg/ml (indirect ELISA) and 0.033 mg/ml (competitive indirect ELISA). Thirty-nine of 158 strains (most P. thoenii or P. jensenii) yielded cross-reacting material; four strains of P. thoenii, including two previously unidentified bacteriocin producers, showed biological activity. Eight propionicin-negative P127 mutants produced neither ELISA response nor biological activity. Western blot analyses of supernates detected a PLG-1 band at 9.1 kDa and two additional protein bands with apparent molecular weights of 16.2 and 27.5 kDa. PLG-1 polyclonal antibodies were used for detection of jenseniin G. PLG-1 antibodies neutralized jenseniin G activity and detected a jenseniin G-sized, 3.5 kDa peptide. Preliminary immunoprecipitation of crude preparations with PLG-1 antibodies yielded three proteins including an active 3-4 kDa band. Propionicin PLG-1 antibodies were used to screen a P. jensenii/thoenii P126 genomic expression library. Complete sequencing of a cloned insert identified by PLG-1 antibodies revealed a putative response regulator, transport protein, transmembrane protein and an open reading frame (ORF) potentially encoding jenseniin G. PCR cloning of the putative plg-1 gene yielded a 1,100 bp fragment with a 355 bp ORF encoding 118 amino acids; the deduced N-terminus was similar to the known PLG-1 N-terminus. The 118 amino acid sequence deduced from the putative plg-1 gene was larger than PLG-1 possibly due to post-translational processing. The product of the putative plg-1 gene had a calculated molecular weight of 12.8 kDa, a pI of 11.7, 14 negatively charged residues (Asp+Glu) and 24 positively charged residues (Arg+Lys). The putative plg-1 gene was expressed as an inducible fusion protein with a six-histidine residue tag. Metal affinity chromatography of the fused protein yielded a homogeneous product. The fused purified protein sequence matched the deduced putative plg-1 gene sequence. The data preliminarily suggest that both the plg-1 and jnG genes have been identified and cloned. Demonstrating that antibodies can be produced for propionicin PLG-1 and that those antibodies can be used to detect, monitor and compare activity throughout growth and purification was an important step towards monitoring PLG-1 concentrations in food systems. The unexpected but fortunate cross-reactivity of PLG-1 antibodies with jenseniin G led to selective recovery of jenseniin G by immunoprecipitation. Further refinement of this separation technique could lead to powerful affinity methods for rapid, specific separation of the two bacteriocins and thus facilitate their availability for industrial or pharmaceutical uses. Preliminary identification of genes encoding the two dairy propionibacteria bacteriocins must be confirmed; further analysis will provide means for understanding how they work, for increasing their production and for manipulating the peptides to increase their target species. Further development of these systems would contribute to basic knowledge about dairy propionibacteria and has potential for improving other industrially significant characteristics.
