Characterization of monoclonal antibodies against the nonstructural 5A protein of hepatitis C virus

Characterization of monoclonal antibodies against the nonstructural 5A protein of hepatitis C virus The nonstructural 5A (NS5A) protein of hepatitis C virus (HCV) is a multifunctional protein that leads to pleiotropic responses, in part by regulating cell growth and cellular signaling pathways. Here, we produced monoclonal antibodies (mAbs) directed against the HCV NS5A protein. The N-terminal epitope was mapped to amino acids 60–80 of the NS5A protein, and the epitope in the middle region was mapped to amino acids 221–236. Because these epitopes overlap with binding regions of human vesicle-associated membrane-protein-associated protein (hVAP)-B and TNF-receptor-associated factor 2 (TRAF2), respectively, we investigated these mAbs for their potential capacity to inhibit viral and cellular interactions. We found that NS5A and hVAP-B interaction was abolished by mAb E5D3, and NS5A and TRAF2 interaction was inhibited by mAb C6D4. Since hVAP-B is necessary for HCV replication and TRAF2 is the major transducer in TNF signaling cascades, these data may provide further insights into the mechanisms underlying HCV replication and viral modulation of host signal transduction. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Virology Springer Journals

Characterization of monoclonal antibodies against the nonstructural 5A protein of hepatitis C virus

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Publisher
Springer Journals
Copyright
Copyright © 2009 by Springer-Verlag
Subject
Biomedicine; Infectious Diseases; Medical Microbiology ; Virology
ISSN
0304-8608
eISSN
1432-8798
D.O.I.
10.1007/s00705-009-0386-9
Publisher site
See Article on Publisher Site

Abstract

The nonstructural 5A (NS5A) protein of hepatitis C virus (HCV) is a multifunctional protein that leads to pleiotropic responses, in part by regulating cell growth and cellular signaling pathways. Here, we produced monoclonal antibodies (mAbs) directed against the HCV NS5A protein. The N-terminal epitope was mapped to amino acids 60–80 of the NS5A protein, and the epitope in the middle region was mapped to amino acids 221–236. Because these epitopes overlap with binding regions of human vesicle-associated membrane-protein-associated protein (hVAP)-B and TNF-receptor-associated factor 2 (TRAF2), respectively, we investigated these mAbs for their potential capacity to inhibit viral and cellular interactions. We found that NS5A and hVAP-B interaction was abolished by mAb E5D3, and NS5A and TRAF2 interaction was inhibited by mAb C6D4. Since hVAP-B is necessary for HCV replication and TRAF2 is the major transducer in TNF signaling cascades, these data may provide further insights into the mechanisms underlying HCV replication and viral modulation of host signal transduction.

Journal

Archives of VirologySpringer Journals

Published: May 1, 2009

References

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