Integrated landscape of chicken egg chalaza proteomics

Jing Pu; Jian Hu; Jing Xiao; Shugang Li; Beibei Wang; Jinqiu Wang; Fang Geng

doi:10.1016/j.psj.2024.103629

Integrated landscape of chicken egg chalaza proteomics

Poult Sci. 2024 Mar 7;103(5):103629. doi: 10.1016/j.psj.2024.103629. Online ahead of print.

Authors

Jing Pu¹, Jian Hu², Jing Xiao¹, Shugang Li³, Beibei Wang⁴, Jinqiu Wang¹, Fang Geng⁵

Affiliations

¹ Institute for Egg Science and Technology, School of Food and Biological Engineering, Chengdu University, Chengdu, 610106, China.
² School of Mechanical Engineering, Chengdu University, Chengdu 610106, China.
³ Engineering Research Center of Bio-process (Ministry of Education), Key Laboratory for Agricultural Products Processing of Anhui Province, School of Food and Biological Engineering, Hefei University of Technology, Hefei, 230601, China.
⁴ Institute for Egg Science and Technology, School of Food and Biological Engineering, Chengdu University, Chengdu, 610106, China; Engineering Research Center of Bio-process (Ministry of Education), Key Laboratory for Agricultural Products Processing of Anhui Province, School of Food and Biological Engineering, Hefei University of Technology, Hefei, 230601, China.
⁵ Institute for Egg Science and Technology, School of Food and Biological Engineering, Chengdu University, Chengdu, 610106, China. Electronic address: gengfang@cdu.edu.cn.

Abstract

Chicken egg chalaza (CLZ) is a natural colloidal structure in eggs that exists as an egg yolk stabilizer and is similar in composition to egg white. In this study, the proteome, phosphoproteome, and N-glycoproteome of CLZ were characterized in depth. We hydrolyzed the CLZ proteins and enriched the phosphopeptides and glycopeptides. We identified 45 phosphoproteins and 80 N-glycoproteins, containing 59 phosphosites and 203 N-glycosylation sites, respectively. Typically, the ovalbumin in CLZ was both phosphorylated and N-glycosylated, with 4 phosphosites and 4 N-glycosylation sites. Moreover, we identified 2 N-glycosylated subunits of ovomucin, mucin-5B and mucin-6, with 32 and nine N- glycosylation sites, respectively. Analysis of the phosphorylation and N-glycosylation status of CLZ proteins could provide novel insights into the structural and functional characteristics of CLZ.

Keywords: N-Glycosylation; chalaza; chicken egg; phosphorylation; proteome.