Chang S C, Yen J H, Kang H Y, Jang M H, Chang M F
Institute of Microbiology, National Taiwan University College of Medicine, Taipei, R.O.C.
Biochem Biophys Res Commun. 1994 Dec 15;205(2):1284-90. doi: 10.1006/bbrc.1994.2804.
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.
丙型肝炎病毒的核心蛋白是通过蛋白水解切割从病毒多聚蛋白的N端191个氨基酸衍生而来。在本研究中，通过间接免疫荧光和细胞化学染色检测了丙型肝炎病毒核心蛋白及其β-半乳糖苷酶融合蛋白在转染细胞中的亚细胞定位。在将编码全长核心蛋白的质粒导入哺乳动物细胞6天后，核心蛋白主要位于细胞质中。核心蛋白C端区域的一个疏水区可能会阻碍核转运效率，因为在转染后24小时，含有缺失C端66个氨基酸的丙型肝炎病毒核心蛋白的β-半乳糖苷酶融合蛋白位于哺乳动物细胞的细胞核内。在丙型肝炎病毒核心蛋白的N端区域进一步鉴定出三个独立的核定位信号。
