The Chikungunya Virus Capsid Protein Contains Linear B Cell Epitopes in the N- and C-Terminal Regions that are Dependent on an Intact C-Terminus for Antibody Recognition

Viruses

卷:7

Jody Hobson-Peters¹  Kelly Baker¹  Roy A. Hall¹  Natalie A. Prow¹  Lucas Y. H. Goh¹  Thisun B. H. Piyasena¹  Marcus L. Hastie²  Jeff J. Gorman²  Ashok Rana²  Carmel T. Taylor³ 

[1] Australian Infectious Diseases Research Centre, School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, Queensland 4072, Australia;

[2] Protein Discovery Centre, QIMR Berghofer Medical Research Institute, Herston, Queensland 4029, Australia;

[3] Public Health Virology, Queensland Health Forensic and Scientific Services, Coopers Plain, Queensland 4108, Australia;

关键词: chikungunya virus;    monoclonal antibodies;    capsid protein;    epitope mapping;    linear B cell epitope;    C-terminus;    N-terminus;   

DOI  :  10.3390/v7062754

来源: DOAJ

【 摘 要 】

Chikungunya virus (CHIKV) is an arthropod-borne agent that causes severe arthritic disease in humans and is considered a serious health threat in areas where competent mosquito vectors are prevalent. CHIKV has recently been responsible for several millions of cases of disease, involving over 40 countries. The recent re-emergence of CHIKV and its potential threat to human health has stimulated interest in better understanding of the biology and pathogenesis of the virus, and requirement for improved treatment, prevention and control measures. In this study, we mapped the binding sites of a panel of eleven monoclonal antibodies (mAbs) previously generated towards the capsid protein (CP) of CHIKV. Using N- and C-terminally truncated recombinant forms of the CHIKV CP, two putative binding regions, between residues 1–35 and 140–210, were identified. Competitive binding also revealed that five of the CP-specific mAbs recognized a series of overlapping epitopes in the latter domain. We also identified a smaller, N-terminally truncated product of native CP that may represent an alternative translation product of the CHIKV 26S RNA and have potential functional significance during CHIKV replication. Our data also provides evidence that the C-terminus of CP is required for authentic antigenic structure of CP. This study shows that these anti-CP mAbs will be valuable research tools for further investigating the structure and function of the CHIKV CP.

【 授权许可】

Unknown