| 刊名 | Agricultural Biotechnology |
| 作者 | Yuyan HE1,2#, Xuelian LIN1,2#, Zhihang CHEN1,2, Xiaoxin WEN1,2, Jianyi WEI3, Huanying PANG1,2* |
| 作者单位 | 1. Fisheries College, Guangdong Ocean University, Zhanjiang 524025, China; 2. Guangdong Provincial Key Laboratory of Aquatic Animal Disease Control and Healthy Culture & Key Laboratory of Control for Diseases of Aquatic Economic Animals of Guangdong Higher Education Institutes, Zhanjiang 524025, China; 3. Guangxi Beihai Nanjiang Aquatic Products Co., Ltd, Beihai 536000, China. |
| DOI | DOI:10.19759/j.cnki.2164-4993.2025.02.001 |
| 年份 | 2025 |
| 刊期 | 2 |
| 页码 | 1-5 |
| 关键词 | Vibrio alginolyticus; Gene cloning; trxB gene; Bioinformatics analysis |
| 摘要 | [Objectives] This study was conducted to investigate the functional characteristics of the trxB gene in Vibrio alginolyticus. [Methods] A pair of specific primers was designed based on the trxB gene sequence of V. alginolyticus for PCR cloning of its full-length sequence. Systematic bioinformatics analyses were conducted to predict the physicochemical properties, secondary structure, and tertiary structure of the encoded protein. [Results] The trxB gene is 960 bp in length, encoding 319 amino acid residues. The deduced protein has a predicted molecular weight of 34.32 kDa and an isoelectric point (pI) of 4.77. Analysis of the amino acid sequence revealed a distinct signal peptide cleavage site at the N-terminus, with no transmembrane domains. The functional sites are as follows: 1 N-glycosylation site, 1 cAMP- and cGMP-dependent protein kinase phosphorylation site, 4 protein kinase C phosphorylation sites, 7 casein kinase II phosphorylation sites, 1 tyrosine kinase phosphorylation site, 11 N-myristoylation sites, 1 prenyl group binding site, 3 microbody C-terminal targeting signal sites, and 1 xanthine nucleotide-disulfide oxidoreductase class II active site. Subcellular localization prediction indicated the highest probability (44.4%) for endoplasmic reticulum localization. The TrxB amino acid sequence of V. alginolyticus shares 97.2-98.4% homology with other Vibrio species, and they were clustered within the same subgroup. Secondary structure prediction showed proportions of random coils (31.97%), alpha-helices (31.66%), extended strands (25.08%), and beta turns (11.29%). The tertiary structure model exhibited 88.68% similarity to template 5vt3.1.A. [Conclusions] This study elucidated the characterization of the TrxB protein in V. alginolyticus, laying a theoretical foundation for the development of outer membrane protein subunit vaccines against this pathogen. |
