Ovalbumin-related Protein X Is a Heparin-binding Ov-Serpin Exhibiting Antimicrobial Activities

Réhault-Godbert, Sophie; Labas, Valérie; Helloin, Emmanuelle; Hervé-Grépinet, Virginie; Slugocki, Cindy; Berges, Magali; Bourin, M.; Brionne, Aurélien; Poirier, J. C.; Gautron, Joël; Coste, Franck; Nys, Yves

doi:10.1074/jbc.m113.469759

Cited by 52 publications

(56 citation statements)

References 41 publications

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“…With respect to OVAY, an acetylation of the N-terminal residue has been hypothesized [29]. Mass spectrometry analysis of OVAX sequence allowed the identification of the peptide MFFYNTDFR corresponding to the sequenced mRNA [12], which confirmed that the N-terminal extremity of OVAX is somehow different as compared with ovalbumin and OVAY sequences. Furthermore, OVAX is not predicted to be N-acetylated (NetAcet 1.0 Server).…”

Section: Non-conventional Signal Peptidementioning

confidence: 89%

“…The start and stop codon found in the amino acid-coding sequence are basically at the same location for the three genes. Alignment of coding sequences of all three genes using NCBI databank for updated accession numbers and data (ovalbumin mRNA, NM_205152.1; 2 OVAY mRNA, NM_001031001.1; OVAX mRNA corresponding to protein accession number AGN32861.1 [12]) indicates a sequence identity of 72.6% between ovalbumin and OVAX, of 71.5% between ovalbumin and OVAY, and 81.9% between OVAX and OVAY (http://www.ebi.ac.uk/Tools/msa/clustalo/). Some repetitive sequences have been identified in the OVAX introns, 3' end and upstream from the OVAY leader, but these sequences do not cross-hybridize with the repetitive sequences found in the OVAY gene.…”

Section: Gene Organization and Evolutionary Historymentioning

confidence: 99%

“…Ovalbumin and its related proteins OVAY and OVAX are mainly produced by the oviduct [16,17] and more specifically by tubular gland cells of the chicken's magnum (egg white formation), although a significant expression of ovalbumin gene has been observed in infundibulum (vitelline membranes) and white isthmus (eggshell membranes) by q-RT-PCR [12]. Repression of ovalbumin gene in non-oviduct tissue and in estrogen-deprived oviduct depends on a strong repressor site located from −130 to −100 and designated CAR for COUP-TF adjacent repressor [18].…”

Section: Tissue Specificitymentioning

confidence: 99%

“…This bond might also be present in OVAY considering that cysteine 74 and cysteine 121 are conserved. For OVAX, since its amino-acid sequence is longer, especially in the vicinity of the first cysteine residue (5 additional residues), it has been hypothesized that the two corresponding cysteines are spatially too distant to form a disulfide bond [12].…”

Section: Biochemical Featuresmentioning

confidence: 99%

“…The two related proteins OVAY and OVAX have been identified in egg white in 2006 [8] and although their physicochemical properties have been characterized recently, their physiological functions remains undefined. There is however, increasing data in literature regarding their potential involvement in some aspects of fertilization or embryonic development [9][10][11] or egg defense [12].…”

Section: Introductionmentioning

confidence: 99%

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The Family Secrets of Avian Egg-Specific Ovalbumin and Its Related Proteins Y and X

Silva¹,

Beauclercq²,

Harichaux³

et al. 2015

Biology of Reproduction

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The ovalbumin gene family in Gallus gallus is composed of three homologous genes located within a 46 kb locus on chromosome 2: ovalbumin, ovalbumin-related protein Y (OVAY), and ovalbumin-related protein X (OVAX) genes. The expression of these genes in hen oviduct is under estrogen control, but their relative hormonal responsiveness and subsequent protein concentration in egg, is distinctive. Interestingly, all three proteins lack the classical signal peptide for secretion. Ovalbumin, OVAX, and OVAY belong to the serine protease inhibitor (serpin) family whose members share a common tertiary structure. Ovalbumin and OVAX are one of the few members of this family that do not express any protease inhibition activity whereas OVAY has been predicted to be inhibitory, by comparison with the consensus sequence for inhibitory serpins. In contrast to ovalbumin and OVAY, OVAX interacts with heparin, a negatively charged glycosaminoglycan, via a positively charged domain exposed at the surface of the molecule. Ovalbumin is the major egg white protein and might be a source of amino acids for the developing embryo. The physiological function of OVAY is not known, but recent data have revealed a possible role of this protein in early embryonic development. Considering the antibacterial activities of OVAX, this protein might play a role in egg defense. This review sheds light on the expression, biochemistry, and structural specificities of these three highly similar paralogs. It gives new clues in favor of diverging functions, which are likely to have arisen by duplication events from a common ancestral gene.

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Section: Non-conventional Signal Peptidementioning

confidence: 89%

Section: Gene Organization and Evolutionary Historymentioning

confidence: 99%

Section: Tissue Specificitymentioning

confidence: 99%

Section: Biochemical Featuresmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

The Family Secrets of Avian Egg-Specific Ovalbumin and Its Related Proteins Y and X

Silva¹,

Beauclercq²,

Harichaux³

et al. 2015

Biology of Reproduction

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View full text Add to dashboard Cite

show abstract

Divergent Proteome Patterns of Egg Albumen from Domestic Chicken, Duck, Goose, Turkey, Quail and Pigeon

Sun

Liu

et al. 2017

Proteomics

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To uncover a diversity of genetic and biological unknowns, a comprehensive and comparative proteomic analysis is performed on egg albumen of domestic chicken, duck, goose, turkey, quail, and pigeon with tandem mass tags quantification technology. In this study, a total of 148, 138, 150, 162, 183, and 179 proteins are identified in egg albumen of the above six species, respectively. Venn plots, PCA, and cluster analysis all reveal the highest similarity of protein composition between duck and goose (≈75%). Additionally, the six species have 52 proteins detected in common in the egg albumen. As revealed by GO and pathway analyses, the plausible functions of these highly conserved proteins are to provide a secure environment and prevent the early death of embryonic cells. Species-specific proteins such as haptoglobin in pigeon, serpin-like protein HMSD in duck, and ovodefensin in chicken are also screened and are likely associated with species-dependent biological processes. Furthermore, Enzyme Code analysis indicated egg albumen have abundant enzyme activity, with hydrolases accounting for more than half of the total enzymes. This study is the first to provide the proteome profiles of egg albumen for the major poultry species, which will be instructive for the understanding of species-specific biological problems with egg albumen.

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The Human SERPIN Repertoire and the Evolution of 14q32.1 and 18q21.3 Gene Clusters

Seixas

2015

The Serpin Family

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Ovalbumin-related Protein X Is a Heparin-binding Ov-Serpin Exhibiting Antimicrobial Activities

Cited by 52 publications

References 41 publications

The Family Secrets of Avian Egg-Specific Ovalbumin and Its Related Proteins Y and X

The Family Secrets of Avian Egg-Specific Ovalbumin and Its Related Proteins Y and X

Divergent Proteome Patterns of Egg Albumen from Domestic Chicken, Duck, Goose, Turkey, Quail and Pigeon

The Human SERPIN Repertoire and the Evolution of 14q32.1 and 18q21.3 Gene Clusters

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