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J. Biol. Chem., Vol. 282, Issue 8, 5273-5286, February 23, 2007

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Cloning of Ovocalyxin-36, a Novel Chicken Eggshell Protein Related to Lipopolysaccharide-binding Proteins, Bactericidal Permeability-increasing Proteins, and Plunc Family Proteins^*

Joël Gautron¹, Emi Murayama, Alain Vignal^¶, Mireille Morisson^¶, Marc D. McKee^||, Sophie Réhault, Valérie Labas^**, Maya Belghazi^**, Mary-Laure Vidal, Yves Nys, and Maxwell T. Hincke

From the INRA (Institut National de la Recherche Agronomique), UR83 Unité de Recherches Avicoles, F-37380 Nouzilly, France, Unité Macrophages et Développement de l'Immunité, Institut Pasteur, 25 Rue du Dr Roux, 75724 Paris Cedex 15, France, ^¶INRA (Institut National de la Recherche Agronomique) UR 444 Laboratoire de Génétique Cellulaire, F-31326 Castanet-Tolosan, France, ^||Faculty of Dentistry, and Department of Anatomy and Cell Biology, McGill University, Montreal, Quebec H3A 2B2, Canada, ^**INRA (Institut National de la Recherche Agronomique) UMR85 Physiologie de la Reproduction et des Comportements, Service de Spectrométrie de Masse et de Protéomique, F-37380 Nouzilly, France, and Department of Cellular and Molecular Medicine, University of Ottawa, Ottawa, Ontario K1H 8M5, Canada

The avian eggshell is a composite biomaterial composed of noncalcifying eggshell membranes and the overlying calcified shell matrix. The shell is deposited in a uterine fluid where the concentration of different protein species varies at different stages of its formation. The role of avian eggshell proteins during shell formation remains poorly understood, and we have sought to identify and characterize the individual components in order to gain insight into their function during elaboration of the eggshell. In this study, we have used direct sequencing, immunochemistry, expression screening, and EST data base mining to clone and characterize a 1995-bp full-length cDNA sequence corresponding to a novel chicken eggshell protein that we have named Ovocalyxin-36 (OCX-36). Ovocalyxin-36 protein was only detected in the regions of the oviduct where egg-shell formation takes place; uterine OCX-36 message was strongly up-regulated during eggshell calcification. OCX-36 localized to the calcified eggshell predominantly in the inner part of the shell, and to the shell membranes. BlastN data base searching indicates that there is no mammalian version of OCX-36; however, the protein sequence is 20–25% homologous to proteins associated with the innate immune response as follows: lipopolysaccharide-binding proteins, bactericidal permeability-increasing proteins, and Plunc family proteins. Moreover, the genomic organization of these proteins and OCX-36 appears to be highly conserved. These observations suggest that OCX-36 is a novel and specific chicken eggshell protein related to the superfamily of lipopolysaccharide-binding proteins/bactericidal permeability-increasing proteins and Plunc proteins. OCX-36 may therefore participate in natural defense mechanisms that keep the egg free of pathogens.

Received for publication, November 3, 2006 , and in revised form, December 14, 2006.

^* This work was supported by grants from the European Commission Eggdefence, QLRT-2001-01606, and the Canadian Natural Sciences and Engineering Council Discovery and Collaborative Research Opportunities Programs (to M. H. and M. D. M.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AJ968387 [GenBank] .

¹ To whom correspondence should be addressed. Tel.: 33-247427540; Fax: 33-247427778; E-mail: gautron{at}tours.inra.fr.

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