细胞自噬是广泛存在于真核细胞内的一种溶酶体依赖性降解途径,涉及细胞内成分如长寿蛋白和受损伤细胞器以及外源病原微生物的吞噬、降解,是机体内一种重要的保护和防御机制。自噬起源于希腊文＂eating of self（自食）＂,最早由比利时...细胞自噬是广泛存在于真核细胞内的一种溶酶体依赖性降解途径,涉及细胞内成分如长寿蛋白和受损伤细胞器以及外源病原微生物的吞噬、降解,是机体内一种重要的保护和防御机制。自噬起源于希腊文＂eating of self（自食）＂,最早由比利时科学家Christian de Duve在1963年溶酶体国际会议中提出,他基于在灌注胰高血糖素的大鼠肝脏里,发现能降解线粒体和其他细胞内结构的溶酶体而提出自噬的概念.展开更多
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
文摘细胞自噬是广泛存在于真核细胞内的一种溶酶体依赖性降解途径,涉及细胞内成分如长寿蛋白和受损伤细胞器以及外源病原微生物的吞噬、降解,是机体内一种重要的保护和防御机制。自噬起源于希腊文＂eating of self（自食）＂,最早由比利时科学家Christian de Duve在1963年溶酶体国际会议中提出,他基于在灌注胰高血糖素的大鼠肝脏里,发现能降解线粒体和其他细胞内结构的溶酶体而提出自噬的概念.
基金supported by the National Natural Science Foundation of China(No.81460304)Guangxi Natural Science Foundation(No.2015GXNSFDA139020)a research program sponsored by the Health Bureau of Guangxi Zhuang Autonomous Region,China(No.Z2014298)
文摘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.
