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CD81-dependent binding of hepatitis C virus E1E2 heterodimers
Laurence Cocquerel1, Chiung-Chi Kuo, Jean Dubuisson
1Department of Medicine, Stanford University Medical Center, Stanford, California 94305, USA.
Journal of Virology
|September 13, 2003
Summary
Hepatitis C virus (HCV) E1E2 complexes bind efficiently to CD81, unlike truncated E2. This finding offers insights into HCV-associated B-cell disorders and virus-host interactions.
Area of Science:
- Virology
- Immunology
- Cell Biology
Background:
- Hepatitis C virus (HCV) causes chronic liver disease and mixed cryoglobulinemia.
- Studying native HCV proteins is challenging; truncated E2 envelope proteins were previously used.
- Truncated E2 may not accurately represent the HCV virion surface due to E1E2 heterodimerization.
Purpose of the Study:
- To investigate the binding of E1E2 heterodimers to CD81.
- To develop a method for isolating functional E1E2 complexes.
- To explore the role of E1E2 complexes in B-cell activation and HCV-associated diseases.
Main Methods:
- Isolation of properly folded E1E2 heterodimer complexes.
- Assessment of E1E2 binding to cells via CD81.
- Analysis of B-cell responses, including aggregation and protein tyrosine phosphorylation, upon E1E2 engagement.
Main Results:
- E1E2 complexes exhibit efficient binding to CD81, superior to truncated E2.
- Purified E1E2 heterodimers bind cells in a CD81-dependent manner.
- Engagement of B cells by E1E2 leads to aggregation and B-cell activation markers.
Conclusions:
- E1E2 heterodimers are better tools than truncated E2 for studying HCV-cell interactions.
- These findings suggest a mechanism for HCV-associated B-cell lymphoproliferative disorders.
- A method for isolating functional E1E2 complexes is established for future research.