布鲁菌丝氨酸/苏氨酸-蛋白激酶RIO1的生物信息学分析

Bioinformatics analysis of brucella melitensis serine/threonine-protein kinase RIO1

目的 应用在线软件分析布鲁菌丝氨酸/苏氨酸-蛋白激酶RIO1抗原蛋白的生物学信息,为研制布鲁菌病基因疫苗奠定基础。方法 采用蛋白质分析系统Protparam(http://expasy.org/tools/protparam.html)分析布鲁菌丝氨酸/苏氨酸-蛋白激酶RIO1蛋白的理化性质;利用软件Protscale(http://www.espasy.org/cgibin/protscale.p1)蛋白质在线分析RIO1蛋白的脂肪指数、亲(疏)水性;利用SOMPA在线分析软件(https://npsa-prabi.ibcp.fr/cgibin/npsa_automat.pl?page=npsa_sopma.html)获得蛋白质二级结构包括α螺旋、延伸链、β折叠、无规则卷曲卷曲的分布和比例;利用Py MOL viewer软件作图构建三级结构模型。结果 氨基酸序列Leu(L)占13.6%,Glu(E)占10.2%,Gly(G)占8.8%。RIO1蛋白正电荷残基(Arg+Lys)和负电荷残基(Asp+Glu)总数分别为8和为24,不稳定指数24.11,分析为不稳定的亲水蛋白。α螺旋(Hh)占44.22%(65个);无规则卷曲(Cc)占34.02%(50个),延伸链(Ee)占18.37%(27个)。β折叠主要位于21~23、30~32、42~44、70~72和122~126;无规卷曲结构主要位于18~22、27~29、32~35、72~76、83~85和92~94。RIO1蛋白含有糖基化位点,并存在可能的酸磷酸化位点。结论 布鲁菌丝氨酸/苏氨酸-蛋白激酶RIO1 α螺旋及无规卷曲结构较多,易与配体发生结合产生抗原表位,免疫原性良好,可为布鲁菌多价表位疫苗的研发提供参考。

Objective To analyze the biological information of brucella serine/threonine-protein kinase RIO1 antigen protein by using online software,and to lay a foundation for the development of a gene vaccine for brucellosis.Methods The protein analysis system Protparam(http://expasy.org/tools/protparam.html) was used to analyze the physicochemical properties of the brucella serine/threonineprotein kinase RIO1 protein;The software Protscale(http://www.espasy.org/cgibin/protscale.p1)Protein online was used to analyze the affinity(hydrophobicity) of RIO1 protein;Online software SOMPA(https://npsa-prabi.ibcp.fr/cgibin/npsa_automat.pl?page=npsa_sopma.html) was used to predict the secondary structure of brucella RIO1 serine/threonine-protein kinase protein which including the distribution and proportion of α helix,extended chain,β fold and random crimp;Py MOL viewer software was using for mapping to build a three-level structural model.Results The amino acid sequence Leu(L) accounted for 13.6%,Glu(E) accounted for 10.2%,and Gly(G)accounted for 8.8%.The total number of negatively charged residues(Asp+Glu) was 24,the total number of positively charged residues(Arg + Lys) was 8,and the RIO1 protein instability index was24.11.The protein was classified as a stable protein by analysis.Alpha helix(Hh) accounted for44.22%(65);Random coil(Cc) accounted for 34.02%(50),and extended strand(Ee) accounted for 18.37%(27).β-sheets were mainly located at 21-23,30-32,42-44,70-72,122-126;Random coil structures were mainly located at 18-22,27-29,32-35,72-76,83-85,92-94.RIO1contained glycosylation sites,and there were possible acid phosphorylation sites.Conclusions Brucella serine/threonine-protein kinase RIO1 α helix and random coil structure are more,usually on the surface of the protein,which can bind with ligands,and is easy to produce new epitopes.It is immunogenic and can be a high-efficiency epitope vaccine for brucella provides reference.