Human parainfluenza virus type 2 phosphoprotein: Mapping of monoclonal antibody epitopes and location of the multimerization domain

被引:43
|
作者
Nishio, M
Tsurudome, M
Ito, M
Watanabe, N
Kawano, M
Komada, H
Ito, Y
机构
[1] Department of Microbiology, Mie University, School of Medicine, Tsu-Shi, Mie-Ken 514
来源
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D O I
10.1099/0022-1317-78-6-1303
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
The epitopes recognized by 42 monoclonal antibodies directed against the human parainfluenza virus type 2 (hPIV-2) phosphoprotein (P) were mapped on the primary structure of the P protein by testing their reactivities with deletion mutants. By Western immunoblotting with these monoclonal antibodies and P protein deletion mutants the region essential for P-P interactions was determined. The P protein region encompassing amino acids 211-248 was required for proper folding and oligomerization which is mediated by predicted coiled-coils in this region. The oligomer was shown to be a homotrimer by chemical cross-linking experiments.
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页码:1303 / 1308
页数:6
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