Processing of the hepatitis C virus precursor protein.
Proteins of hepatitis C virus (HCV) are produced from a polyprotein precursor by post-translational processing. Production of HCV proteins was analyzed with in vitro translation, as well as plasmid-based transient gene expression, in mammalian cell lines. A minimum of three different processing pathways yielded at least 10 viral proteins from the polyprotein precursor. One pathway depended on signal protease processing, and the other two pathways utilized viral proteinases. The signal peptidase cleaved the viral structural proteins, and two viral activities broke up the viral nonstructural proteins. With staggered cleavages, the signal peptidase produced two E2 products from the E2 region, gp70 type A and type B, differing in the C-terminal structure. Two viral proteinases partially overlapped in the N-terminal region of NS3; the functional amino acid residues required for those two activities differed. Most of the processed viral proteins bound together; some of the associated proteins were membrane bound.
Shimotohno
K
K
Virology Division, National Cancer Center Research Institute, Tokyo, Japan.
Tanji
Y
Y
Hirowatari
Y
Y
Komoda
Y
Y
Kato
N
N
Hijikata
M
M
D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D004285:Dogs; D015967:Gene Expression Regulation, Viral / Q000502:physiology; D018014:Gene Transfer Techniques; D016174:Hepacivirus; D066298:In Vitro Techniques; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases / Q000378:metabolism*; D014176:Protein Biosynthesis; D011498:Protein Precursors / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D011817:Rabbits; D014764:Viral Proteins / Q000378:metabolism*
D011498:Protein Precursors; D014764:Viral Proteins; D010447:Peptide Hydrolases