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

Hsin-Chieh Ma; Cheng-Hung Ke; Tsai-Yuan Hsieh; Shih-Yen Lo

doi:10.1099/0022-1317-83-12-3085

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

J Gen Virol. 2002 Dec;83(Pt 12):3085-3092. doi: 10.1099/0022-1317-83-12-3085.

Authors

Hsin-Chieh Ma¹, Cheng-Hung Ke¹, Tsai-Yuan Hsieh², Shih-Yen Lo^{3

1}

Affiliations

¹ Institute of Medical Research1 and Department of Medical Technology2, Tzu Chi University, 701, Section 3, Chung-Yang Road, Hualien, Taiwan 970, Republic of China.
² Department of Internal Medicine, Tri-Service General Hospital, National Defense Medical Center, Taipei, Taiwan, Republic of China4.
³ Department of Medical Technology, Buddhist Tzu Chi General Hospital, Hualien, Taiwan, Republic of China3.

PMID: 12466485
DOI: 10.1099/0022-1317-83-12-3085

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Binding Sites
Capsid Proteins / metabolism*
Endopeptidase K / metabolism
Glutathione Transferase
Glycosylation
Hepacivirus / genetics
Hepacivirus / metabolism*
Humans
Hydrophobic and Hydrophilic Interactions
Protein Binding
Tumor Cells, Cultured
Viral Envelope Proteins / chemistry*
Viral Envelope Proteins / genetics
Viral Envelope Proteins / metabolism*

Substances

Capsid Proteins
E1 protein, Hepatitis C virus
Viral Envelope Proteins
Glutathione Transferase
Endopeptidase K