TY - JOUR
T1 - Phosphorylation of nonstructural 5A protein of hepatitis C virus
T2 - HCV group-specific hyperphosphorylation
AU - Hirota, Masami
AU - Satoh, Shinya
AU - Asabe, Shin Ichi
AU - Kohara, Michinori
AU - Tsukiyama-Kohara, Kyoko
AU - Kato, Nobuyuki
AU - Hijikata, Makoto
AU - Shimotohno, Kunitada
N1 - Funding Information:
This work was supported by grants-in-aid for cancer research and for second-term comprehensive 10-year strategy for cancer control from the Ministry of Health and Welfare, by a grant-in-aid for scientific research from the Ministry of Education, Science, and Culture, and by the program for Promotion of Fundamental Studies in Health Sciences of the Organization for Drug ADR Relief, R&D Promotion and Product Review of Japan.
PY - 1999/4/25
Y1 - 1999/4/25
N2 - We previously showed that two proteins with molecular weights of 56 and 58 kDa are produced from nonstructural protein 5A (NS5A) derived from hepatitis C virus (HCV)-lb genotype. The 56-kDa protein is phosphorylated at serine residues in NS5A, including those located in the C-terminal region of NS5A, while the 58-kDa protein, the hyperphosphorylated form of the 56-kDa protein, is phosphorylated at serine residues in the central region. This hyperphosphorylation is dependent on the presence of HCV NS4A protein. To clarify whether NS4A-dependent phosphorylation also occurs in other HCV genotypes, phosphorylation of NS5A was analyzed by two-dimensional gel electrophoresis. Here, we report that NS5A from the HCV-2a genotype was phosphorylated. However, hyperphosphorylation of NS5A occurs in the HCV-lb genotype but not in the -2a genotype. This result suggests that modification of NS5A phosphorylation reflects the virological features of HCV and that there are physiological differences in the roles of differently phosphorylated NS5A between HCV genotypes.
AB - We previously showed that two proteins with molecular weights of 56 and 58 kDa are produced from nonstructural protein 5A (NS5A) derived from hepatitis C virus (HCV)-lb genotype. The 56-kDa protein is phosphorylated at serine residues in NS5A, including those located in the C-terminal region of NS5A, while the 58-kDa protein, the hyperphosphorylated form of the 56-kDa protein, is phosphorylated at serine residues in the central region. This hyperphosphorylation is dependent on the presence of HCV NS4A protein. To clarify whether NS4A-dependent phosphorylation also occurs in other HCV genotypes, phosphorylation of NS5A was analyzed by two-dimensional gel electrophoresis. Here, we report that NS5A from the HCV-2a genotype was phosphorylated. However, hyperphosphorylation of NS5A occurs in the HCV-lb genotype but not in the -2a genotype. This result suggests that modification of NS5A phosphorylation reflects the virological features of HCV and that there are physiological differences in the roles of differently phosphorylated NS5A between HCV genotypes.
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U2 - 10.1006/viro.1999.9658
DO - 10.1006/viro.1999.9658
M3 - Article
C2 - 10208927
AN - SCOPUS:0033602572
SN - 0042-6822
VL - 257
SP - 130
EP - 137
JO - Virology
JF - Virology
IS - 1
ER -
