Research Article

Molecular Cloning and Bioinformatics Analysis of T3SS Inner Membrane Ring HrpQ from Vibrio harveyi  

F.K.A.  Kuebutornye , Jiaming  Liao , Huanying Pang , Yishan Lu , S.  Ayiku , M.E.  Sakyi
1 College of Fishery, Guangdong Ocean University, Zhanjiang 524088, China
2 Guangdong Provincial Key Laboratory of Pathogenic Biology and Epidemiology for Aquatic Animals, Zhanjiang, 524088, China
3 Key Laboratory of Control for Diseases of Aquatic Animals of Guangdong Higher Education Institutes, Zhanjiang, 524088, China

Author    Correspondence author
Genomics and Applied Biology, 2018, Vol. 9, No. 7   doi: 10.5376/gab.2018.09.0007
Received: 15 Aug., 2018    Accepted: 23 Sep., 2018    Published: 10 Sep., 2018
© 2018 BioPublisher Publishing Platform
This is an open access article published under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Preferred citation for this article:

Kuebutornye F.K.A., Liao J.M., Pang H.Y., Lu Y.S., Ayiku S., and Sakyi M.E., 2018, Molecular cloning and bioinformatics analysis of T3SS inner membrane ring HrpQ from Vibrio harveyi, Genomics and Applied Biology, 9(7): 40-47 (doi: 10.5376/gab.2018.09.0007)

Abstract

In this study, Vibrio harveyi strain HY99 was isolated from a diseased Epinephelus coioides. A full-length HrpQ gene of the bacteria was cloned and the amino acid sequence analyzed. The length of HrpQ gene sequence was 1,302 bp and coded 433 Amino acids. HrpQ relative molecular weight of theoretical prediction and isoelectric point were 48.002 kDa and 5.08 respectively. This protein was hydrophilic and there was one transmembrane region. There were three N-glycosylation sites. Structural analysis showed that the protein belonged to the FHA, Yop-YscD ppl superfamily. Secondary structure was composed of 31.41% α-helices, 21.71% extension chains, 7.16% beta turns and 39.72% random curls. The 3D structure of HrpQ protein was predicted to be a monomer similar to the 3D structure of the YscD putative type III secretion protein confirming that HrpQ is a T3SS protein and can be activated in vivo. This study provides a theoretical basis for further study on the function of HrpQ protein.

Keywords
Type III secretion system; Vibrio harveyi; HrpQ gene; Bioinformatics analysis
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