| Content Provider |
World Health Organization (WHO)-Global Index Medicus |
| Author |
Zhang, Ke Xia, Ning-shao Li, Xiao-jing Yang, Fan Tang, Zi-min Zhao, Min Wang, Si-ling Zheng, Zi-zheng Cai, Wei |
| Description |
Author Affiliation: Zhao M ( From the State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, National Institute of Diagnostics and Vaccine Development in Infectious Diseases, School of Life Sciences, and.); Li XJ ( From the State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, National Institute of Diagnostics and Vaccine Development in Infectious Diseases, School of Life Sciences, and.); Tang ZM ( the School of Public Health, Xiamen University, Xiamen, Fujian 361005, People's Republic of China.); Yang F ( the School of Public Health, Xiamen University, Xiamen, Fujian 361005, People's Republic of China.); Wang SL ( the School of Public Health, Xiamen University, Xiamen, Fujian 361005, People's Republic of China.); Cai W ( From the State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, National Institute of Diagnostics and Vaccine Development in Infectious Diseases, School of Life Sciences, and.); Zhang K ( the School of Public Health, Xiamen University, Xiamen, Fujian 361005, People's Republic of China.); Xia NS ( From the State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, National Institute of Diagnostics and Vaccine Development in Infectious Diseases, School of Life Sciences, and the School of Public Health, Xiamen University, Xiamen, Fujian 361005, People's Republic of China nsxia@xmu); Zheng ZZ ( the School of Public Health, Xiamen University, Xiamen, Fujian 361005, People's Republic of China zhengzizheng@xmu.edu.cn.) |
| Abstract |
The hepatitis E virus (HEV) ORF2 encodes a single structural capsid protein. The E2s domain (amino acids 459-606) of the capsid protein has been identified as the major immune target. All identified neutralizing epitopes are located on this domain; however, a comprehensive characterization of antigenic sites on the domain is lacking due to its high degree of conformation dependence. Here, we used the statistical software SPSS to analyze cELISA (competitive ELISA) data to classify monoclonal antibodies (mAbs), which recognized conformational epitopes on E2s domain. Using this novel analysis method, we identified various conformational mAbs that recognized the E2s domain. These mAbs were distributed into 6 independent groups, suggesting the presence of at least 6 epitopes. Twelve representative mAbs covering the six groups were selected as a tool box to further map functional antigenic sites on the E2s domain. By combining functional and location information of the 12 representative mAbs, this study provided a complete picture of potential neutralizing epitope regions and immune-dominant determinants on E2s domain. One epitope region is located on top of the E2s domain close to the monomer interface; the other is located on the monomer side of the E2s dimer around the groove zone. Besides, two non-neutralizing epitopes were also identified on E2s domain that did not stimulate neutralizing antibodies. Our results help further the understanding of protective mechanisms induced by the HEV vaccine. Furthermore, the tool box with 12 representative mAbs will be useful for studying the HEV infection process. |
| ISSN |
00219258 |
| e-ISSN |
1083351X |
| Journal |
Journal of Biological Chemistry |
| Issue Number |
32 |
| Volume Number |
290 |
| Language |
English |
| Publisher |
American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date |
2015-08-07 |
| Publisher Place |
United States |
| Access Restriction |
Open |
| Subject Keyword |
Antibodies, Monoclonal Chemistry Antibodies, Neutralizing Antibodies, Viral Antigens, Viral Hepatitis E Virus Viral Proteins Genetics Immunology Capsid Cluster Analysis Enzyme-Linked Immunosorbent Assay Statistics & Numerical Data Epitope Mapping Epitopes Escherichia Coli Metabolism Gene Expression Models, Molecular Peptide Library Protein Conformation Protein Structure, Tertiary Recombinant Proteins Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type |
Text |
| Resource Type |
Article |
| Subject |
Cell Biology Biochemistry Molecular Biology |
