Latest Cover

Online Office

Contact Us

Issue:ISSN 1000-7083
          CN 51-1193/Q
Director:Sichuan Association for Science and Technology
Sponsored by:Sichuan Society of Zoologists; Chengdu Giant Panda Breeding Research Foundation; Sichuan Association of Wildlife Conservation; Sichuan University
Address:College of Life Sciences, Sichuan University, No.29, Wangjiang Road, Chengdu, Sichuan Province, 610064, China
Tel:+86-28-85410485
Fax:+86-28-85410485
Email:scdwzz@vip.163.com & scdwzz001@163.com
Your Position :Home->Past Journals Catalog->2014 Vol.33 No.5

Cloning, Identificatin and Molecular Characteristics Analysis of ? Protein Gene of Streptococcus agalactiae from Tilapia
Author of the article:DENG Yongqiang1, 2, WANG Kaiyu1, 3*, WANG Jun1, 3, DENG lüzhou3, 4, FAN Wei3, 4, WANG Erlong1, 3, HUANG Xiaoli3, 4, CHEN Defang3, 4
Author's Workplace:(1. College of Veterinary Medicine, Sichuan Agricultural University, Ya’an, Sichuan Province 625014, China; 2. Sichuan Provincial Center for Animal Disease Prevention and Control, Chengdu 610041, China; 3. Key Laboratory of Animal Disease and Human Health of Sichuan Province, Sichuan Agricultural University, Ya’an, Sichuan Province 625014, China; 4. Department of Aquaculture, College of Animal Science & Technology, Sichuan Agricultural University, Ya’an, Sichuan Province 625014, China)
Key Words:tilapia; Streptococcus agalactiae; α protein gene; cloning; molecular characteristics
Abstract:α Protein gene of Streptococcus agalactiae that isolated from tilapia was cloned in this study. Based on the prediction of bioinformatics analysis, the ORF of α protein gene was composed of 1341 nucleotides and encoded a polypeptide of 446 amino acids. The structure domain analysis showed a conserved YSIRK signal peptide sequence and an alpha C_N super family structure domain in N-terminal, a conserved Gram_pos_anchor super family structure domain in C-terminal, and two Rib structures domain in the median region. Moreover, the main difference was the repeat number of Rib as determined by comparing the structures of α protein of different origins. The homology of α protein was 100% between the strain A909 (this study) and GD201008-001 based on the results of homologous and phylogenetic analysis. Our results also showed that α protein was a hydrophilic protein with trans-membrane region, and had 37 potential phosphorylation sites and one potential N-glycosylation site. Secondary structure analysis showed lots of random coil. It is predicted that the region of 12 amino acids should be B cell epitopes. When Escherichia coli were selected as expressing hosts, the solubility of the recombinant protein could reach 100%. Subcellular localization showed that the protein located in the cell wall.
CopyRight©2020 Editorial Office of Sichuan Journal of Zoology