| 摘要 |
[Objectives] To clone the fbpA gene from Vibrio alginolyticus strain HY9901 and perform bioinformatic analyses, aiming to preliminarily elucidate the structure and function of the FbpA protein. [Methods] The fbpA gene was amplified using PCR and sequenced. Bioinformatics software was employed to analyze the fbpA gene sequence and the deduced FbpA protein for physicochemical properties, signal peptides, transmembrane structures, functional sites, subcellular localization, homology comparisons, phylogenetic analysis, and structural prediction. [Results] The fbpA gene (1 014 bp, encoding 337 amino acids, GenBank accession number PP707017) was successfully cloned. The FbpA protein was identified as a stable hydrophilic protein (molecular weight 37.589 kD, pI 5.97) containing a signal peptide, lacking transmembrane domains, and predicted to be localized extracellularly. It harbors 7 N-myristoylation sites, 8 phosphorylation sites, 2 N-glycosylation sites, and 7 microbody C-terminal targeting signal sites. The protein is highly conserved within the Vibrio genus, exhibiting 99.41% and 99.40% similarity to the Vibrio diabolicus subgroup and Vibrio antiquarius, respectively, with all three clustering together on the same evolutionary branch. Secondary structure prediction indicated a predominance of alpha-helices (49.85%) and random coils (30.27%). [Conclusions] This study successfully cloned the fbpA gene and characterized the structural features and evolutionary relationships of the FbpA protein, laying a foundation for further investigation into its role in the pathogenesis of V. alginolyticus and the development of vaccines. |
