Membrane binding properties and terminal residues of the mature hepatitis C virus capsid protein in insect cells.

ABSTRACT: The immature core protein (p23, residues 1 to 191) of hepatitis C virus undergoes posttranslational modifications including intramembranous proteolysis within its C-terminal signal sequence by signal peptide peptidase to generate the mature form (p21). In this study, we analyzed the cleavage site and other amino acid modifications that occur on the core protein. To produce the posttranslationally modified core protein, we used a baculovirus-insect cell expression model system. As previously reported, p23 is processed to form p21 in insect as well as in mammalian cells. p21 was found to be associated with the cytoplasmic membrane, and its significant portion behaved as an integral membrane protein. The protein was purified from the membrane by a simple and unique procedure on the basis of i

SUBMITTER: Ogino T 

PROVIDER: S-EPMC523247 | biostudies-literature | 2004 Nov

REPOSITORIES: biostudies-literature