Intracellular localization of full-length and truncated hepatitis C virus core protein expressed in mammalian cells.
The putative hepatitis C virus core protein has a predicted molecular weight of about 22 kD and contains two carboxy (COOH)-terminal hydrophobic domains. The cleavages generating the hepatitis C virus structural proteins (core, E1 and E2) are catalyzed by host signal peptidases. In the present study, we investigated the processing and intracellular localization of the hepatitis C virus core protein expressed in mammalian cells. Expression vectors encoding the entire core protein or COOH-terminal deletion mutants under the control of SV40 regulatory sequences were transfected in COS cells. Immunofluorescent staining with either polyclonal immunoglobulin or monoclonal anti-core antibodies showed that fragments containing the COOH-terminal hydrophobic stretch were retained in the cytoplasm of transfected cells, whereas truncated core proteins deleted of 28 or more residues were located in the nucleus. Our results suggest that a putative nuclear targeting sequence is contained in the first 40 residues of the core protein.
Ravaggi
A
A
Consorzio per le Biotecnologie, Consiglio Nazionale delle Ricerche (CNR), School of Medicine, University of Brescia, Italy.
Natoli
G
G
Primi
D
D
Albertini
A
A
Levrero
M
M
Cariani
E
E
D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D016174:Hepacivirus / Q000737:chemistry*; D006801:Humans; D008969:Molecular Sequence Data; D014758:Viral Core Proteins / Q000032:analysis*
D014758:Viral Core Proteins