4株滑液囊支原体分离株P80脂蛋白的基因克隆及序列分析OACHSSCDCSTPCD

To investigate the function and diversity within the P80 lipoprotein family of Mycoplasma synoviae(MS),genes encoding P80-1,P80-2,and P80-3 proteins were amplified from four MS isolates using PCR and sequenced.Bioinformatics methods were applied to analyze the protein sequences of the P80 family lipopro-teins,identify their conserved structural domains and antigenic epitopes,and predict their functions.The results indicated that the P80 family lipoproteins were basic,hydrophilic,stable proteins,with a strong hydro-phobic region at the N-terminus;only the P80-2 protein had a transmembrane helix region.The positions of the signal peptides and hydrophobic regions of the P80 family lipoproteins are consistent;the three P80 proteins share 12 conserved structural domains and have 2 to 4 distinct structural domains;there are 31 to 32 antigenic epitope sites;their secondary structures are primarily composed of α-helices and random coils;and the tertiary structure predictions show that the P80-1 protein may function as an ABC transporter,the P80-2 protein as a periplasmic binding protein type Ⅱ,and the P80-3 protein is associated with cell adhesion functions.These find-ings provide a reference for further research into the function of the MS P80 family lipoproteins,as well as insights into MS pathogenic mechanisms,pathogen diagnosis,and vaccine development.