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, El 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. (C) Journal of Hepatology.
INTRACELLULAR-LOCALIZATION OF FULL-LENGTH AND TRUNCATED HEPATITIS-C VIRUS CORE PROTEIN EXPRESSED IN MAMMALIAN-CELLS / Antonella, Ravaggi; Gioacchino, Natoli; Daniele, Primi; Alberto, Albertini; Levrero, Massimo; Elisabetta, Cariani. - In: JOURNAL OF HEPATOLOGY. - ISSN 0168-8278. - 20:6(1994), pp. 833-836. [10.1016/s0168-8278(05)80157-6]
INTRACELLULAR-LOCALIZATION OF FULL-LENGTH AND TRUNCATED HEPATITIS-C VIRUS CORE PROTEIN EXPRESSED IN MAMMALIAN-CELLS
LEVRERO, Massimo;
1994
Abstract
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, El 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. (C) Journal of Hepatology.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
