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Characterization of enterovirus 71 capsids using subunit protein-specific polyclonal antibodies
Qingwei Liu1, Xulin Huang, Zhiqiang Ku
1Key Laboratory of Molecular Virology & Immunology, Institut Pasteur of Shanghai, Chinese Academy of Sciences, 411 Hefei Road, Shanghai, China.
Journal of Virological Methods
|October 11, 2012
Summary
Enterovirus 71 (EV71) capsid proteins were studied using specific antibodies. Cleavage of VP0 into VP2 and VP4 is crucial for EV71 infectivity and viral assembly.
Area of Science:
- Virology
- Molecular Biology
- Immunology
Background:
- Enterovirus 71 (EV71) is a primary cause of hand-foot-and-mouth disease (HFMD) in the Asia-Pacific region.
- Understanding EV71 capsid protein processing and assembly is key to developing antiviral strategies.
Purpose of the Study:
- To characterize EV71 structural protein processing.
- To determine the composition and assembly of EV71 capsids.
- To investigate the role of VP0 cleavage in viral infectivity.
Main Methods:
- Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE).
- Western blot analysis using capsid subunit protein-specific antibodies.
- Immunofluorescent staining of infected cells.
Main Results:
- Purified, non-infectious EV71 capsids contained processed VP0, VP1, and VP3, which co-assembled.
- Infectious EV71 lysates also showed VP2, indicating VP0 cleavage to VP2 and VP4 is vital for infectivity.
- EV71 capsid proteins were found to co-localize in the cytoplasm of infected cells.
Conclusions:
- New insights into EV71 capsid protein processing, assembly, and cellular localization.
- Capsid protein-specific antibodies are valuable tools for EV71 research.
- These antibodies can aid in developing EV71 vaccines and diagnostic reagents.

