The first hydrophobic domain of the hepatitis C virus E1 protein (aa 261-291) is crucial for its interaction with the capsid protein in the endoplasmic reticulum membrane.
No immediate clinical implications; leaves open E1 domain as potential HCV assembly target pending human validation.
The interaction between the hepatitis C virus capsid protein and the envelope protein E1 has been demonstrated previously in vivo. To determine the binding region of the E1 protein with the capsid protein, this interaction was characterized in vitro. This study shows that the interaction between these proteins should occur in the endoplasmic reticulum membrane rather than in the cytosol and that the first hydrophobic domain of the E1 protein (aa 261-291) is important for the interaction with the capsid protein.
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Ma et al. (2002) studied this question.
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