共 41 条
Characterization of a slow-migrating component of the rabies virus matrix protein strongly associated with the viral glycoprotein
被引:3
作者:
Nakahara, T
[1
]
Toriumi, H
[1
]
Irie, T
[1
]
Takahashi, T
[1
]
Ameyama, S
[1
]
Mizukoshi, M
[1
]
Kawai, A
[1
]
机构:
[1] Kyoto Univ, Grad Sch Pharmaceut Sci, Dept Mol Microbiol, Sakyo Ku, Kyoto 6068501, Japan
关键词:
rabies virus;
matrix protein;
conformational change;
monoclonal antibody #3-9-16;
dimer formation;
D O I:
10.1111/j.1348-0421.2003.tb03458.x
中图分类号:
R392 [医学免疫学];
Q939.91 [免疫学];
学科分类号:
100102 ;
摘要:
We investigated multiple forms of rabies virus matrix (M) protein. Under non-reducing electrophoretic conditions, we detected, in addition to major bands of monomer forms (23- and 24-kDa) of M protein, an M antigen-positive slow-migrating minor band (about 54 kDa) in both the virion and infected cells. Relative contents of the 54-kDa and monomer components in the virion were about 20-30% and 70-80% of the whole M protein, respectively, while the content of the 54-kDa component was smaller (about 10-20% of the total M protein) in the cell than in the virion. The 54-kDa components could be extracted from the infected cells with sodium deoxycholate, but they were quite resistant to extraction with 1% nonionic detergents by which most monomer components were solubilized. The 54-kDa component was precipitated more efficiently than the monomer by a monoclonal antibody (mAb; #3-9-16), which recognized a linear epitope located at the N-terminal of the M protein. The mAb #3-9-16 coprecipitated the viral glycoprotein (G), which was demonstrated to be due to strong association between the G and 54-kDa component of the M protein. Monomers and the 54-kDa polypeptide migrated to the same isoelectric point (pI) in two-dimensional (2-D) gel electrophoresis, implicating that the 54-kDa component was composed of component(s) of the same pI as that of the M protein monomers. From these results, we conclude that the M antigen-positive 54-kDa polypeptide is a homodimer of M protein, taking an N-terminal-exposed conformation, and is strongly associated with the viral glycoprotein. Possible association with a membrane microdomain of the cell will be discussed.
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页码:977 / 988
页数:12
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