Characterization of monoclonal antibodies against the nonstructural 5A protein of hepatitis C virus |
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Authors: | Sang Min Kang Hyun-Jung Jun Yun-Sook Lim Soo-Ho Choi and Soon B Hwang |
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Institution: | (1) National Research Laboratory of Hepatitis C Virus, Ilsong Institute of Life Science, Hallym University, 1605-4 Gwanyang-dong, Dongan-gu, Anyang, 431-060, Korea |
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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. |
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Keywords: | |
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