Ovalbumin-related protein X is a heparin-binding ov-serpin exhibiting antimicrobial activities
2013
Rehault-Godbert , Sophie(auteur de correspondance) (INRA , Nouzilly (France). UR 0083 Recherches Avicoles) | Labas , Valérie (INRA , Nouzilly (France). UMR 0085 Physiologie de la Reproduction et des Comportements) | Helloin , Emmanuelle (INRA , Nouzilly (France). UMR 1282 Infectiologie et Santé Publique) | Hervé-Grépinet , Virginie (Institut Naltional de la Santé et de la Recherche Médicale , Tours(France). UMR 1100, EA 6305 Centre d’Etude des Pathologies Respiratoires) | Slugocki , Cindy (INRA , Nouzilly (France). UMR 1282 Infectiologie et Santé Publique) | Berges , Magali (INRA , Nouzilly (France). UR 0083 Recherches Avicoles) | Bourin , Marie-Christine (Institut Technique de l'Aviculture et des Elevages de Petits Animaux, Nouzilly(France).) | Brionne , Aurelien (INRA , Nouzilly (France). UR 0083 Recherches Avicoles) | Poirier , Jean-Claude (INRA , Nouzilly (France). UR 0083 Recherches Avicoles) | Gautron , Joël (INRA , Nouzilly (France). UR 0083 Recherches Avicoles) | Coste , Franck (Centre National de la Recherche Scientifique, Orléans(France). UPR4301 Centre de Biophysique Moléculaire, Réparation de l’acide de désoxyribonucléique : approches structurales et fonctionnelles) | Nys , Yves (INRA , Nouzilly (France). UR 0083 Recherches Avicoles)
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 Lys(367)-His(368) 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.
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