Cloning and Bioinformatics Analysis of hcp Gene in Aeromonas hydrophila

Fan Li, Xingjun Fu, Haiyun Feng, Shi Wang, Weijie Zhang, Huanying Pang and Na Wang

Asian Agricultural Research, vol. 16, issue 03

Abstract: [Objectives] To explore the function of hcp gene in Aeromonas hydrophila. [Methods] A pair of specific primers was designed referring to the hcp gene sequence of A. hydrophila. The hcp gene was amplified by PCR, and performed bioinformatics analysis. [Results] The hcp gene had a total length of 1 650 bp and encoded 549 amino acids. The theoretical molecular weight of the protein predicted was about 59 476.44 kDa. After predicting the N-terminal signal peptide structure of the amino acid sequence, neither obvious signal peptide cleavage site nor signal peptide was found, and the protein had no transmembrane region. The amino acid sequence had a N-glycosylation site, 4 protein kinase C phosphorylation sites, 7 casein kinase II phosphorylation sites, 9 N-myristoylation sites, 4 isoprene binding sites, 10 microbody C-terminal target signal sites, and an ATP/GTP binding site motif A (P-ring). The amino acid sequence of hcp gene of A. hydrophila was performed homology analysis with other Aeromonas strains, and it showed higher homology with A. veronii. In the secondary structure, the α-helix, β-sheet, random coil and extended strand accounted for 45.36%, 6.01 %, 37.52% and 11.11%, respectively. The tertiary structure model consisted of 18 α-helix and 22 β-sheet. Analysis of protein-protein network interaction demonstrated that the proteins interacting with Hcp protein were AHA_3407, nrfA, nirB-1, nirB-2 and AHA_1112. [Conclusions] Through the bioinformatics prediction results, the basic information of hcp gene of A. hydrophila is preliminarily understood, and the possible function of this protein is predicted, in order to provide guidance for subsequent vaccine research.

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Persistent link: https://EconPapers.repec.org/RePEc:ags:asagre:349065

DOI: 10.22004/ag.econ.349065

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