1. Ovalbumin-related Protein X Is a Heparin-binding Ov-Serpin Exhibiting Antimicrobial Activities
- Author
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Joël Gautron, Valérie Labas, Yves Nys, Cindy Slugocki, Emmanuelle Helloin, Franck Coste, Jean-Claude Poirier, Marie-Christine Bourin, Sophie Réhault-Godbert, Virginie Hervé-Grépinet, Magali Berges, Aurélien Brionne, Unité de Recherches Avicoles (URA), Institut National de la Recherche Agronomique (INRA), Physiologie de la reproduction et des comportements [Nouzilly] (PRC), Institut National de la Recherche Agronomique (INRA)-Institut Français du Cheval et de l'Equitation [Saumur]-Université de Tours (UT)-Centre National de la Recherche Scientifique (CNRS), Infectiologie et Santé Publique (UMR ISP), Institut National de la Recherche Agronomique (INRA)-Université de Tours (UT), Centre de biophysique moléculaire (CBM), Université d'Orléans (UO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC), National French Agency (OVO-mining) , ANR-09-BLAN-0136-01, European Commission ('Reducing Egg Susceptibility to Contamination in Avian Production in Europe,') FOOD-CT-2006-036018, Institut National de la Recherche Agronomique (INRA)-Institut Français du Cheval et de l'Equitation [Saumur]-Université de Tours-Centre National de la Recherche Scientifique (CNRS), Institut National de la Recherche Agronomique (INRA)-Université de Tours, Centre National de la Recherche Scientifique (CNRS)-Université de Tours-Institut Français du Cheval et de l'Equitation [Saumur]-Institut National de la Recherche Agronomique (INRA), Université d'Orléans (UO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), UR83 recherches avicoles, and Rehault Godbert, Sophie
- Subjects
glycoprotein ,Cathepsin G ,Glycosylation ,Amino Acid Motifs ,heparin binding protein ,Biochemistry ,Chromatography, Affinity ,Protein Structure, Secondary ,antibacterial proteins ,chemistry.chemical_compound ,Protein structure ,spectrométrie de masse ,Fibrinolysin ,innate immunity ,chemistry.chemical_classification ,0303 health sciences ,biology ,030302 biochemistry & molecular biology ,serpin ,respiratory system ,Trypsin ,Anti-Bacterial Agents ,protéine antimicrobienne ,3. Good health ,Organ Specificity ,embryonic structures ,Protein Structure and Folding ,Trypsin Inhibitors ,Protein Binding ,Autre (Sciences du Vivant) ,Egg white ,medicine.drug ,animal structures ,Ovalbumin ,Molecular Sequence Data ,poulet ,Microbial Sensitivity Tests ,héparine ,Serpin ,Gram-Positive Bacteria ,serine protéase ,spectroscopie ,Avian Proteins ,03 medical and health sciences ,Sequence Homology, Nucleic Acid ,Gram-Negative Bacteria ,test antimicrobien ,medicine ,Animals ,rt pcr ,[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology ,Amino Acid Sequence ,RNA, Messenger ,protein structure ,chicken egg ,Molecular Biology ,Serpins ,030304 developmental biology ,Serine protease ,Base Sequence ,blanc d'oeuf ,Heparin ,analyse biochimique ,Cell Biology ,Molecular biology ,carbohydrates (lipids) ,ovalbumine ,chemistry ,Structural Homology, Protein ,biology.protein ,Glycoprotein ,Chickens ,Protein Processing, Post-Translational - Abstract
Background: Ovalbumin-related protein X (OVAX) is an uncharacterized ovalbumin-serpin. Results: This egg white-specific serpin lacks protease inhibitory activity, but unlike its ovalbumin homolog, OVAX exhibits antibacterial properties, partly through its heparin-binding site(s). Conclusion: OVAX, a non-inhibitory serpin is a heparin-binding molecule with antibacterial activity. Significance: OVAX participates in egg defense and constitutes a natural agent against Listeria and Salmonella., Ovalbumin family contains three proteins with high sequence similarity: ovalbumin, ovalbumin-related protein Y (OVAY), and ovalbumin-related protein X (OVAX). Ovalbumin is the major egg white protein with still undefined function, whereas the biological activity of OVAX and OVAY has not yet been explored. Similar to ovalbumin and OVAY, OVAX belongs to the ovalbumin serine protease inhibitor family (ov-serpin). We show that OVAX is specifically expressed by the magnum tissue, which is responsible for egg white formation. OVAX is also the main heparin-binding protein of egg white. This glycoprotein with a predicted reactive site at Lys367-His368 is not able to inhibit trypsin, plasmin, or cathepsin G with or without heparin as a cofactor. Secondary structure of OVAX is similar to that of ovalbumin, but the three-dimensional model of OVAX reveals the presence of a cluster of exposed positive charges, which potentially explains the affinity of this ov-serpin for heparin, as opposed to ovalbumin. Interestingly, OVAX, unlike ovalbumin, displays antibacterial activities against both Listeria monocytogenes and Salmonella enterica sv. Enteritidis. These properties partly involve heparin-binding site(s) of the molecule as the presence of heparin reverses its anti-Salmonella but not its anti-Listeria potential. Altogether, these results suggest that OVAX and ovalbumin, although highly similar in sequence, have peculiar sequential and/or structural features that are likely to impact their respective biological functions.
- Published
- 2013
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