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Journal of General Virology (2002), 83, 3085-3092.
© 2002 Society for General Microbiology


Animal: RNA Viruses

The first hydrophobic domain of the hepatitis C virus E1 protein is important for interaction with the capsid protein

Hsin-Chieh Ma1, Cheng-Hung Ke1, Tsai-Yuan Hsieh4 and Shih-Yen Lo1,2,3

Institute of Medical Research1 and Department of Medical Technology2, Tzu Chi University, 701, Section 3, Chung-Yang Road, Hualien, Taiwan 970, Republic of China
Department of Medical Technology, Buddhist Tzu Chi General Hospital, Hualien, Taiwan, Republic of China3
Department of Internal Medicine, Tri-Service General Hospital, National Defense Medical Center, Taipei, Taiwan, Republic of China4

Author for correspondence: Shih-Yen Lo at Department of Medical Technology. Fax +886 3 8571917. e-mail losylo{at}mail.tcu.edu.tw

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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