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Journal of General Virology, Vol 78, 1303-1308, Copyright © 1997 by Society for General Microbiology
ARTICLES |
M Nishio, M Tsurudome, M Ito, N Watanabe, M Kawano, H Komada and Y Ito
Department of Microbiology, Mie University School of Medicine, Japan. nishio@doc.medic.mie-u.ac.jp
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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