Bioinformatic analysis of non-VP1 capsid protein of coxsackievirus A6.
10.1007/s11596-016-1633-4
- Author:
Hong-Bo LIU
1
;
Guang-Fei YANG
2
;
Si-Jia LIANG
3
;
Jun LIN
4
Author Information
1. Department of Laboratory Medicine, the Second Affiliated Hospital of Guilin Medical University, Guilin, 541199, China. hbliu@glmc.edu.cn.
2. College of Pharmacy, Guilin Medical University, Guilin, 541004, China.
3. Department of Laboratory Medicine, the Second Affiliated Hospital of Guilin Medical University, Guilin, 541199, China.
4. College of Bio-technology, Guilin Medical University, Guilin, 541004, China.
- Publication Type:Journal Article
- Keywords:
Coxsackievirus A6 (CVA6);
bioinformatics;
capsid proteins;
linear B cell eiptopes;
physicochemical properties;
structural and functional domains
- MeSH:
Amino Acid Sequence;
Capsid Proteins;
genetics;
immunology;
Computational Biology;
Enterovirus;
genetics;
pathogenicity;
Epitopes, B-Lymphocyte;
genetics;
immunology;
Humans
- From:
Journal of Huazhong University of Science and Technology (Medical Sciences)
2016;36(4):607-613
- CountryChina
- Language:English
-
Abstract:
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 SubLoc, TargetP and the others from ExPASy 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.
