Ovocalyxin-36 and other LBP/BPI/PLUNC-like proteins as molecular actors of the mechanisms of the avian egg natural defences

Author:

Gautron Joël1,Réhault-Godbert Sophie1,Pascal Géraldine2345,Nys Yves1,Hincke Maxwell T.6

Affiliation:

1. INRA, UR83 Recherches avicoles, F-37380 Nouzilly, France

2. INRA, UMR85 Physiologie de la Reproduction et des Comportements, F-37380 Nouzilly, France

3. CNRS, UMR6175, F-37380 Nouzilly, France

4. Université François Rabelais de Tours, F-37041 Tours, France

5. IFCE, F-37380 Nouzilly, France

6. Department of Cellular and Molecular Medicine, University of Ottawa, Ottawa, ON, Canada, K1H 8M5

Abstract

The chicken egg possesses physical and chemical barriers to protect the embryo from pathogens. OCX-36 (ovocalyxin-36) was suggested to be a 36 kDa eggshell-specific protein that is secreted by the regions of the oviduct responsible for eggshell formation. Its expression is strongly up-regulated during shell calcification. This protein was also detected in vitelline membrane and expressed in gut tissues. Analysis of the OCX-36 protein sequence revealed that OCX-36 is related to the BPI (bactericidal permeability-increasing proteins)/LBP [LPS (lipopolysaccharide)-binding proteins]/PLUNC (palate, lung and nasal epithelium clone) superfamily, and that there are strong similarities between the exon/intron organization of the mammalian LBP/BPI and the avian OCX-36 genes. A recent study revealed that OCX-36 originates from a tandem duplication of an ancestral BPI/LBP/PLUNC gene, after the divergence of birds and mammals. Its antimicrobial activity was recently investigated and it was shown that OCX-36 binds to LPS from Escherichia coli. High-throughput methodologies have led to the identification of approximately 1000 new egg proteins. Among these are LBP/BPI proteins that might play a role in the natural defences of the egg to protect the embryo during its development in the external milieu, and may function to keep the table egg free of pathogens. The function of these BPI-like molecules is the subject of intense research to characterize their putative LPS-binding properties and antimicrobial activity.

Publisher

Portland Press Ltd.

Subject

Biochemistry

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