Molecular Cloning of sodB Gene from Vibrio alginolyticus HY9901 and Its Bioinformatics Analysis
刊名 Asian Agricultural Research
作者 Shuai YANG, Yingying JIANG, Haiyun FENG, Weijie ZHANG, Na WANG, Xiaonan LU, Huanying PANG
作者单位 Fisheries College, Guangdong Ocean University; 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; Chinese Academy of Inspection and Quarantine; Department of Food Science and Agricultural Chemistry,Faculty of Agricultural and Environmental Sciences,McGill University, Sainte-Anne-de-Bellevue H9X 3V9
DOI 10.19601/j.cnki.issn1943-9903.2024.07.009
年份 2024
刊期 7
页码 42-47
关键词 Vibrio alginolyticus, Gene cloning, sodB gene, Bioinformatics analysis
摘要 Vibrio alginolyticus is a zoonotic bacterium. A pair of specific primers was designed using the sodB gene sequence of Vibrio alginolyticus HY9901 in order to amplify the full length of the gene by PCR. The results indicated that the total length of the sodB gene was 585 bp and that it could encode 194 amino acids. The predicted amino acid sequence derivation indicated that the molecular weight of the protein was approximately 21.56 kDa, with an isoelectric point of 4.95. Upon prediction of the N-terminal signal peptide structure of the protein, no significant signal peptide cleavage site was observed, indicating that the protein lacked both a signal peptide and a transmembrane region. The amino acid sequence contained an N-glycosylation site, a casein kinase II phosphorylation site, a microsomal C-terminal target signal site, and a manganese and iron superoxide dismutase signal site. The probability of intracytoplasmic localization of the SodB protein was 56.5%, which was analyzed according to the subcellular localization of the protein. The amino acid sequence of the sodB gene of V. alginolyticus exhibited 98%-100% homology to other Vibrio species, clustering into the same subfamily with V. parahaem, indicating a relatively close relationship between them. In the prediction of protein structure, the proportions of α-helix, random coil, β-sheet, and extended strand were 48.45%, 30.41%, 5.67%, and 15.46%, respectively. The similarity to template 1dt0.1.A reached 71.58%. A PTM site analysis revealed the presence of phosphorylation, glycosylation, ubiquitination, sumoylation, acetylation, and methylation modification sites, as well as the absence of lactylation modification sites.