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Biochem Biophys Res Commun. 1994 Dec 15;205(2):1284-90.

Nuclear localization signals in the core protein of hepatitis C virus.

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  • 1Institute of Microbiology, National Taiwan University College of Medicine, Taipei, R.O.C.

Abstract

The core protein of the hepatitis C virus is derived from the N-terminal 191 amino acids of the viral polyprotein by proteolytic cleavage. In the current study, subcellular localizations of the HCV core and its beta-galactosidase fusion proteins in transfected cells were examined by indirect immunofluorescence and cytochemical staining. The core protein was located predominantly in the cytoplasm 6 days after a plasmid encoding the full-length core protein had been introduced into mammalian cells. A hydrophobic domain in the C-terminal region of the core protein may block the efficiency of nuclear transport, since a beta-galactosidase fusion protein that contains HCV core protein lacking the C-terminal 66-amino-acid was located within the nuclei of mammalian cells 24 hours posttransfection. Three independent nuclear localization signals were further identified in the N-terminal region of the HCV core protein.

PMID:
7802660
[PubMed - indexed for MEDLINE]
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