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| 1 | Molecular Cloning and Bioinformatics Analysis of TypeⅢSecretion System Effector Protein Va1686 Gene of Vibrio alginolyticus显示文摘In this study,Va1686 gene was cloned from Vibrio alginolyticus. The total length of the gene is 1 164 bp,and it could encode 387 amino acids. The physicochemical properties,protein structure,genetic evolutionary relationship and antigenic characteristics of the effect protein Va1686 of V. alginolyticus HY9901 type Ⅲ secretion system were studied and analyzed by bioinformatics methods and tools. The results showed that Va1686 is a stable hydrophilic and acidic protein without a transmembrane region and a signal peptide,and secondary structure to α-helix. The evolutionary analysis showed that V. alginolyticus HY9901 and V.harveyi were clustered together,which indicated that the genetic relationship between the two species was the closest. Va1686 contains a Fic superfamily conserved domain associated with cell division. Bioinformatics analysis showed that the B-cell preponderant epitopes of Va1686 might be localized in the regions of 48-49,82-85,125-126,150-153,185-186,236-237 and so on. The 3D structure model of Va1686 subunit was simulated by SWISS-MODEL software and it was found that the vop S of V. parahaemolyticus was similar and the similarity was 89. 46%. In this study,the feasibility of Va1686 as a common antigen of Vibrio was verified from the perspective of bioinformatics,which laid the foundation for the next step in vaccine development. | Zhihao WU Mingjie FAN Jiaming LIAO Huanying PANG Chuanhao PAN Dawei SONG Mingsheng QIU Shuanghu CAI Jichang JIAN | 2018 | Agricultural Biotechnology2018，7，5： | 2 |
| 2 | Cloning and Bioinformatics Analysis of pepck Gene in Vibrio alginolyticus显示文摘[Objectives]To clone the pepck gene of Vibrio alginolyticus strain HY9901 and analyze its sequence by bioinformatics.[Methods]According to the complete gene sequence of V.alginolyticus on GenBank,specific primers were designed to amplify the target gene pepck by PCR.The sequence of the pepck gene was analyzed using bioinformatics.The phylogenic tree of pepck gene and the corresponding single-subunit three-dimensional structure were constructed.[Results]The pepck gene of V.alginolyticus strain HY9901 has a full length of 1629 bp,with theoretical molecular weight of 60.12 kD.The prediction results show that there is no signal peptide or transmembrane region at the N-terminus of the sequence,the amino acid sequence contains 11 phosphorylation sites of casein kinase II.The prediction results of protein subcellular localization indicate that PEPEK protein is localized in the cytoplasm.The protein is stable and hydrophobic.The tertiary structure of the PEPCK protein of V.alginolyticus is similar to that of Vibrio parahaemolyticus.It is predicted that PEPCK has a major functional domain PEPCK_ATP.In the secondary structure,alpha helix,random coil,and extended strand accounted for 21.96%,52.03%and 26.01%,respectively.The PEPCK homology between V.alginolyticus and Vibrio diabolicus is as high as 99%.[Conclusions]This study lays the foundation for further understanding the function of pepck gene in V.alginolyticus. | Fuyuan ZENG Yin ZHAO Shihui ZHOU Chuanhao PAN Miao XIE Huanying PANG | 2020 | Asian Agricultural Research2020，12，8： | 0 |
| 3 | Molecular Cloning and Bioinformatics Analysis of TypeⅢSecretion System Effector Protein HY 322 Gene of Vibrio alginolyticus显示文摘In this study,Hy322 gene was cloned from Vibrio alginolyticus.The total length of its gene was 969 bp,and it could encode 322 amino acids.The physicochemical properties,protein structure,genetic evolutionary relationship and antigenic characteristics of the effector protein Hy322 of V.alginolyticus HY9901 type Ⅲ secretion system were studied and analyzed by bioinformatics methods and tools.The results showed that Hy322 is an unstable hydrophilic and acidic protein without a transmembrane region and a signal peptide,and secondary structure to α-helix.The evolutionary analysis showed that V.alginolyticus HY9901 and V.harveyi were clustered together,which indicated that the genetic relationship between the two species was closest.HY322 contains a FliN super family conserved domain associated with Flagellar motor switch.Bioinformatics analysis showed that the B-cell preponderant epitopes of Hy322 might be localized in the regions of 32-33,100-102,138-140,215-216,235-238 and 246-249.The 3D structure model of Hy322 subunit was simulated by SWISS-MODEL software and itwas found that the yscQ of Yersinia were similar and the similarity was 42.25%.In this study,the feasibility of Hy322 as a common antigen of Vibrio was verified from the perspective of bioinformatics,which laid the foundation for the next step in vaccine development. | Shanshan LIANG Mingjie FAN Weijian LIANG Huanying PANG Chuanhao PAN Dawei SONG Mingsheng QIU Jichang JIAN | 2018 | Agricultural Biotechnology2018，7，6： | 0 |
| 4 | Molecular Cloning and Bioinformatics Analysis of araC Gene of Vibrio alginolyticus显示文摘[Objective]To clone araC gene of Vibrio alginolyticus HY9901 strain,and analyze bioinformatics.[Methods]the whole genome sequence of Vibrio alginolyticus on GenBank was used to design specific primers.According to the principle of PCR amplification sequence,the target gene araC was amplified,and then the sequence was further analyzed by bioinformatics method to establish the phylogenetic tree of araC gene and its corresponding subunit three-dimensional structure model.[Results]Sequence analysis revealed araC gene is 711 bp and encodes a putative protein of 236 amino acids.The predicted molecular mass of AraC was 26.92 ku.Using Signal P 4.0 and TMHMM Server 2.0 software for analysis,it was predicted that the AraC protein did not contain a signal peptide or a transmembranous region.The AraC protein had two cAMP and cGMP dependent protein kinase phosphorylation site,five protein kinase C phosphorylation sites,three casein kinase II phosphorylation sites,one prenyl group binding site(CAAX box)and five microbodies C-terminal targeting signal.The predicted results of protein subcellular localization showed that AraC was located in the mitochondria,nucleus and cytoplasm.Its protein is unstable and hydrophilic.The AraC protein is a transcriptional regulatory protein which belongs to HTH_18 superfamily.According to the prediction,secondary structure:a-helix(Alpha helix)accounted for 52.12%,random coil(31.78%),extended strand(11.02%),b-fold(Beta turn)accounted for 5.08%.V.alginolyticus,Vibrio parahaemolyticus and Vibrio palustris were clustered together,which implies that the genetic relationship between these three species was the closest. | Fangling MO Gyamfua AFRIYIE Jialing HU Junling WANG Shihui ZHOU Zhongduo WANG F.K.A.KUEBUTORNYE Chuanhao PAN Huanying PANG | 2021 | Asian Agricultural Research2021，13，2： | 0 |
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