|
|
|
题名
|
作者
|
年代
|
出处
|
被引量
|
| 1 | Cloning,expression,identification and bioinformatics analysis of Rv3265c gene from Mycobacterium tuberculosis in Escherichia coli显示文摘Objective:To clone and express Rv3265c gene of Mycobacterium tuberculosis in Escherichia coli (E.coli) under optimistic conditions,obtain and identify protein expressed,analyze the structure and characteristics of the protein using bioinformatics methods for future applications.Methods: Rv3265c gene from Mycobacterium tuberculosis H37Rv was amplified by polymerase chain reaction,and was cloned into the pET-30a vector after purification and recovery.The recombinant plasmid was sequenced and expressed in E.coli BL21(DE3),and then purified and identified by western blotting.The essential physical-chemical properties of the protein were predicated by bioinformatics tools,including subcellular location,secondary structure,domains,antigenic epitopes,etc.Tertiary structure of the protein based on homology modeling was estabUshed,while multi-sequence homological alignment and phylogenetic analysis were preformed.Results:The recombinant protein was obtained in soluble fraction from expression system in E.coli B121(DE3) carrying pET30- Rv3265c plasmid,and Rv3265c gene was expressed correctly.Bioinformatics analysis showed the protein contained no signal peptide and transmembrane helices,located outside of membrane.Secondary structure analysis revealed it containedα-helix,extended strand and random coil,46.8%,14.6%,38.6%,respectively.Furthermore,it possessed six potential antigenic epitopes,one glycosyl transferase domain.A simple three-dimensional model of this protein was constructed by Swiss-model sever.Both sequences and structures were conservative and especial either in gene or in protein.Conclusions:Rv3265c gene might be a desirable molecular target for anti-tuberculosis drug and vaccine.The purified protein from expression will be utilized to study the kinetics of L-rhamnosyltransferase and to develope an enzyme assay for screening vaccine or drug. | Qiang Wu Peng Zhou Shiyun Qian Xi Qin Qiongyao Fu Zhinong Zhan Hua Pei | 2011 | Asian Pacific Journal of Tropical Medicine2011，4，4： | 2 |
| 2 | Identification,structure and function of a novel tetraspaninhoniologue from Spirometra erinaceieuropaei显示文摘Objective:To identify a full length cDNA sequence of a novel tetraspanin(TSP) homologue from Spirometra erinaceieuropaei and to predict the structure and function of its encoding protein using bioinformatics methods.Methods:Using the NCBI,EMBI,Expasy and other online sites, the open reading frame(ORF),conserved domain,physical and chemical parameters,signal peptide,transmembrane domain,epitope,topological structures of the protein sequences were predicted.And Vector NTI software was used for multiple sequence alignment and phylogenetic tree construction.Results:’Hie target sequence was 1 132 hp length with a 681 hp biggest ORF encoding 226 amino acids protein with typical TSP conserved domain.It was confirmed as full length cDNA of TSP16 from Spirometra erinaceieuropaei and named as SeTSP16 (GenBank accession number:JF728872).The predicted molecular weight and isoelectric point of the deduced protein were 24 750.5 Da and 7.88 Da,respectively.Compared with TSP16s from Schistosoma japonicum and Schistosoma mansoni.it showed similarity of 59%and 59%, respectively.SeTSP16 contained four transmembrane domains(TM 1-4),intracellular N and C-termini,one short small extracellular loop and one large extracellular loop.Four major epitopes that were significant different from the corresponding epitope regions of TSP16 from Schistosoma mansoni and Schistosoma japonicum were predicted.Conclusions:The full length cDNA sequences of SeTSP16 arc identified.It encodes a transmembrane protein which might be an ideal diagnosis antigen and target molecule for antiparasitic drugs. | Fu Qiongyao Lu Yajun Rao Langyu Chen Jinglong Wu Qiang Cai Qunfang Li Lihua Wu Lixian Lu Gang | 2011 | Asian Pacific Journal of Tropical Medicine2011，4，9： | 1 |
| 3 | Antioxidant induced bulk passivation for efficient and stable hole transport layer-free carbon electrode perovskite solar cells显示文摘Defect passivation is one of the important strategies to improve the efficiency and stability of perovskite solar cells.In this work,2,6-di-tert-butyl-4-methylphenol(BHT)as antioxidant was introduced into the perovskite precursor solution to improve the quality of the prepared perovskite films,so that these films performed a larger and uniform grain size.Moreover,the-OH functional group in BHT interacts with I-,thus reducing the density of defect states and inhibiting the non-radiative recombination.The presence of hydrophobic groups in BHT protects the film from moisture erosion and improves the long-term stability of PSCs devices.The maximum photoelectric conversion efficiency of the constructed ITO/SnO_(2)/BHTMAPbI_(3)/Carbon device is 16.88%,and the unpackaged cell maintains the initial efficiency of 99.3%after698 h of storage under the environmental condition of 30%humidity.This work provides an efficient approach to improve the performance of printable hole transport layer-free carbon electrode perovskite solar cells. | Yetai Cheng Qingbo Wei Nannan Wang Zhangwen Ye Yanbin Zhao Qiongyao Wang Depeng Chu Lingxing Zan Feng Fu Yucheng Liu | 2023 | Chinese Chemical Letters2023，34，6： | 0 |
| 4 | Prokaryotic expression,identification and bioinformatics analysis of fbpB-esxA fusing gene from Mycobacterium tuberculosis显示文摘Objective:To obtain fbpB-esxA fusing gene of Mycobacterium tuberculosis(MTU),express the encoded fusing protein in Escherichia coli(E.coli),identify protein acquired,and predict the structure and function of the protein utilizing methods of bioinformatics.Methods:fbpB and esxA gene were amplified from genome of MTB H37Rv by PCR.The fbpB-esxA fusing gene Iigated by(Gly4Ser)3 linker was gained by means of Gene Splicing by Overlapping Extension PCU(SOEPCR), and fusing gene was cloned into expression vector pET-30a.The recombinant plasmid was sequenced and expressed in E.coli BL21(DE3).The protein was identified by Western blot using anti-HIS antibody.Secondary structure and antigenic epitopes of the protein were predicting using tools of bioinformatics.Results:The UNA sequences fbpB-esxA were identical with that published by GenBank.The Ag85B-ESAT-6 fusion protein about 50 kDa comprised 485 amino acids was efficiently produced from expression system in E.coli B1.21(DE3) under the induction of IPTG.Bioinformatics analysis showed the protein contained one transmembrane region and fourteen potential antigenic epitopes.Conclusions:The Ag85B-ESAT-6 fusion protein is successfully expressed with N-terminal HIS-tag.Gel filtration demonstrated that it exists as insoluble inclusion bodies mainly.The existence of linker doesn’t affect immunogenicity of Ag85B and ESAT-6.It will allow lor characterization in vitro and establish a foundation of further function research such as vaccine or diagnostic reagent. | Qiang Wu Qiongyao Fu Qian Chen Qunfang Cai Zhigang Fan Zhinong Zhan Lina Niu Hua Pei Peng Zhou | 2011 | Asian Pacific Journal of Tropical Medicine2011，4，7： | 0 |
您所在的机构暂未开通此部分的功能，请联系管理员