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柯萨奇病毒A6型VP1蛋白的生物信息学分析 被引量:14
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作者 刘洪波 阳广菲 +1 位作者 欧维琳 沈关心 《中国免疫学杂志》 CAS CSCD 北大核心 2016年第4期536-541,共6页
目的:预测柯萨奇病毒A组6型(Coxsackievirus A6,CVA6)的衣壳蛋白VP1的基本理化性质、结构功能及线性B细胞表位。方法:应用Bioedit软件、Sub Loc、Target P和生物信息学资源门户Ex PASy中的多种在线工具对CVA6 VP1的氨基酸序列进行... 目的:预测柯萨奇病毒A组6型(Coxsackievirus A6,CVA6)的衣壳蛋白VP1的基本理化性质、结构功能及线性B细胞表位。方法:应用Bioedit软件、Sub Loc、Target P和生物信息学资源门户Ex PASy中的多种在线工具对CVA6 VP1的氨基酸序列进行分析。结果:CVA6 VP1为一亲水性蛋白,其相对分子量为33.6 k D,等电点为7.92,含有24个可能的磷酸化位点,没有信号肽、跨膜区和可能的脂酰化位点;其二级结构中以无规则卷曲居多,有48.52%的氨基酸残基暴露于溶液界面;该分子内存在多个潜在的线性B细胞表位,其中的155~165位氨基酸残基区域的抗原指数最高。结论:成功预测到CVA6 VP1的基本理化性质、结构功能特征及可能的线性B细胞表位,为该蛋白的进一步研究及疫苗和免疫诊断试剂的研制打下基础。 展开更多
关键词 柯萨奇病毒A组6型 VP1蛋白 生物学信息 B细胞表位 理化性质
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Bioinformatic Analysis of Non-VP1 Capsid Protein of Coxsackievirus A6 被引量:4
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作者 刘洪波 阳广菲 +1 位作者 梁思佳 林军 《Journal of Huazhong University of Science and Technology(Medical Sciences)》 SCIE CAS 2016年第4期607-613,共7页
This study bioinformatically analyzed the non-VP1 capsid proteins(VP2-VP4) of Coxasckievirus A6(CVA6), with an attempt to predict their basic physicochemical properties, structural/functional features and linear B... This study bioinformatically analyzed the non-VP1 capsid proteins(VP2-VP4) of Coxasckievirus A6(CVA6), with an attempt to predict their basic physicochemical properties, structural/functional features and linear B cell eiptopes. The online tools Sub Loc, Target P and the others from Ex PASy Bioinformatics Resource Portal, and SWISS-MODEL(an online protein structure modeling server), were utilized to analyze the amino acid(AA) sequences of VP2-VP4 proteins of CVA6. Our results showed that the VP proteins of CVA6 were all of hydrophilic nature, contained phosphorylation and glycosylation sites and harbored no signal peptide sequences and acetylation sites. Except VP3, the other proteins did not have transmembrane helix structure and nuclear localization signal sequences. Random coils were the major conformation of the secondary structure of the capsid proteins. Analysis of the linear B cell epitopes by employing Bepipred showed that the average antigenic indices(AI) of individual VP proteins were all greater than 0 and the average AI of VP4 was substantially higher than that of VP2 and VP3. The VP proteins all contained a number of potential B cell epitopes and some eiptopes were located at the internal side of the viral capsid or were buried. We successfully predicted the fundamental physicochemical properties, structural/functional features and the linear B cell eiptopes and found that different VP proteins share some common features and each has its unique attributes. These findings will help us understand the pathogenicity of CVA6 and develop related vaccines and immunodiagnostic reagents. 展开更多
关键词 Coxsackievirus A6 (CVA6) capsid proteins bioinformatics physicochemical properties structural and functional domains linear B cell eiptopes
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