Ovalbumin-Related Gene Y Protein Bears Carbohydrate Chains of the Ovomucoid Type

Hirose, Junko; Doi, Yukio; Kitabatake, Naofumi; Narita, Hiroshi

doi:10.1271/bbb.70.144

Cited by 18 publications

(16 citation statements)

References 28 publications

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“…The two related proteins OVAY and OVAX have been described. Although the biochemical characteristics of OVAY have been published recently (28, 29), there are, to date, no data regarding OVAX and its related function.…”

Section: Discussionmentioning

confidence: 99%

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

Réhault-Godbert¹,

Labas

Helloin

et al. 2013

Journal of Biological Chemistry

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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.

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Section: Discussionmentioning

confidence: 99%

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

Réhault-Godbert¹,

Labas

Helloin

et al. 2013

Journal of Biological Chemistry

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“…The glycosylation sites of OVAY need to be further identified but in addition to N293, three potential N-glycosylated sites were predicted on asparagines at position 95, 215, and 312. OVAY seems to have a carbohydrate moiety similar to that of egg white ovomucoid [40]. Regarding OVAX, two N-glycosylated sites were confirmed by MS/MS analysis: N111YS and N229NS [12] whereas a third glycosylation site has been recently identified on N326LT (G. Harichaux, personal communication).…”

Section: Biochemical Featuresmentioning

confidence: 88%

“…Ovalbumin and OVAY are closely related in terms of sequence, pI, molecular weight except that OVAY seems to bears carbohydrate chains with specificities allowing its purification using antibodies against ovomucoid carbohydrates [40]. Concerning OVAX, many different properties can be exploited to selectively purify this protein from egg (pI, molecular weight).…”

Section: Biochemical Featuresmentioning

confidence: 99%

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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“…While a prerequisite for accurate CRD is the use of highly purified allergen preparations for testing, commercially available preparations of ovomucoid, ovalbumin, conalbumin and lysozyme, have been reported to contain other egg-white allergens [12,13,14]. Further purification of such crude egg allergen preparations has been described in a number of publications using different chromatography techniques [12,13,14,15,16]. Characterization of crude and purified allergen preparations have generally been performed by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE), IgE immunoblotting and IgE ELISA using human serum samples.…”

Section: Introductionmentioning

confidence: 99%

Affinity Purification of Egg-White Allergens for Improved Component-Resolved Diagnostics

Everberg¹,

Brostedt²,

Öman³

et al. 2010

Int Arch Allergy Immunol

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Background: Egg is a common cause of food-allergic reactions, especially among young children. Some egg-allergic patients do, however, tolerate heated egg products and component-resolved diagnostics (CRD) may facilitate prediction of different disease manifestations. Commercially available preparations of the egg-white allergens, ovomucoid, ovalbumin, conalbumin and lysozyme, have been reported to contain impurities which interfere with accurate CRD. Methods: Commercial preparations of the 4 egg-white allergens were characterized using allergen-specific monoclonal chimeric human/mouse IgE antibodies in experimental ImmunoCAP® tests. Further purification of commercial ovomucoid, ovalbumin and conalbumin preparations was performed by chromatography based on affinity to monoclonal antibodies. Purity was monitored by size exclusion chromatography, SDS-PAGE, Western blotting and experimental ImmunoCAP tests using allergen-specific chimeric IgE antibodies. IgE reactivity to the highly purified egg components was analyzed in 83 samples from egg white-sensitized individuals. Results: Preparations of commercially available ovomucoid, ovalbumin and conalbumin were found to contain other egg allergens which were removed by chromatographic purification. No impurities were detected in the commercial lysozyme preparation. Previously unknown complexes between the target allergens and contaminating allergens were detected and removed by affinity chromatography. IgE reactivity to ovalbumin was most common in the analyzed samples (87%), followed by ovomucoid (72%), conalbumin (69%) and lysozyme (58%). Conclusions: In this study we demonstrate the advantage of using monoclonal antibodies for purification, and monoclonal chimeric IgE antibodies for characterization, of egg allergens intended for CRD. Our study also established that ovalbumin, ovomucoid, conalbumin and lysozyme are all major allergens.

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Ovalbumin-Related Gene Y Protein Bears Carbohydrate Chains of the Ovomucoid Type

Cited by 18 publications

References 28 publications

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

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

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

Affinity Purification of Egg-White Allergens for Improved Component-Resolved Diagnostics

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