Research Note: Comprehensive proteomic, phosphoproteomic, and N-glycoproteomic analysis of chicken egg yolk plasma

• Published in: Poultry science Vol. 103; no. 12; p. 104253
• Main Authors: Xiao, Di, Hu, Gan, Ding, Qianying, He, Hong, Wang, Jinqiu, Geng, Fang
• Format: Journal Article
• Language: English
• Published: England Elsevier Inc 01.12.2024; Elsevier
• Subjects: chicken egg; METABOLISM AND NUTRITION; N-glycosylation; phosphorylation; proteome; yolk plasma; chicken egg; phosphorylation; N-glycosylation; yolk plasma; proteome
• ISSN: 0032-5791; 1525-3171; 1525-3171
• DOI: 10.1016/j.psj.2024.104253

Chicken egg yolk plasma (EYP), the supernatant fraction of egg yolk obtained by water dilution and centrifugation, is a rich source of various bioactive substances and a significant bearer of yolk-emulsifying properties. This study utilized proteomics to conduct a comprehensive and in-depth analysis of both common and modified EYP proteins (phosphorylated proteins and N-glycosylated proteins). Total of 208 proteins were identified in EYP, including 42 phosphorylated proteins with 137 phosphorylation sites and 150 N-glycoproteins with 332 N-glycosylation sites. Among the phosphorylation sites, tyrosine accounted for 80.6%, while the N-glycosylation sites predominantly featured “N-X-T” motifs, accounting for 58.7%. Functional enrichment analysis revealed that most proteins were involved in regulating enzyme activity and inhibition with a particular focus on modulating peptidase activity. Notably, vitellogenins-2 (30 phosphorylation sites, 9 N-glycosylation sites) and apolipoprotein B (10 phosphorylation sites, 56 N-glycosylation sites) were the 2 proteins with the most modification sites. Additionally, EYP was found to contain the highly N-glycosylated complement proteins C3 and C4. These findings provide new insights into the protein composition of EYP and its roles in chicken embryo development and immune defense, offering a theoretical foundation for the application of EYP in various fields.