Structural Analysis of the Protein Encoded by PLA2G7 Gene in Chicken

WU Mingyin; XIE Lu; HE Jingyi; CHEN Yuting; XIE Chunlin; LUO Chenglong; JI Jian

doi:10.19978/j.cnki.xmsy.2025.03.05

Abstract：Lipoprotein-associated phospholipase A2(Lp-PLA2),encoded by PLA2G7 gene,is mainly secreted by inflammatory cells and is associated with various metabolic and immune dysfunctions,as well as other related diseases.The sequence characteristics and physical and chemical properties of the protein encoded by PLA2G7 gene were analyzed to provide a theoretical basis for studying the mechanism of Lp-PLA2 protein in chicken growth,development and avian disease immunity.Here,bioinformatic methods were used to analyze the physical and chemical properties,hydrophilicity/hydrophobicity,protein structure,phosphorylation sites and transmembrane region of chicken PLA2G7 at the molecular level,and combined with protein interaction network analysis for comprehensive evaluation.The results showed that the chicken PLA2G7 gene was 1 923 bp in length and encoded a protein consisting of 641 amino acids,which was mainly distributed in the cytoplasm and belonged to a hydrophilic secreted protein;The secondary structure is mainly composed of irregular coil(48.36%),α-helix(31.36%),extended chain(12.79%)and β-Sheet(7.49%).Functional prediction revealed that the protein has 46 potential phosphorylation sites,29 of which may be serine phosphorylation sites.Based on the STRING protein interaction network,four proteins involved in immune response and regulation of phospholipid metabolism were preliminarily analyzed.Conclusion:the sequence characteristics and structure of the protein encoded by PLA2G7 gene reveal that it may be closely related to the regulation of phospholipid metabolism and immune response in chickens.This finding provides a theoretical basis for further exploring the functional mechanism of Lp-PLA2.