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

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...

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Bibliographic Details
Published in:Journal of general virology 1997-06, Vol.78 (6), p.1303-1308
Main Authors: Nishio, M, Tsurudome, M, Ito, M, Watanabe, N, Kawano, M, Komada, H, Ito, Y
Format: Article
Language:English
Subjects:
Animals
Antibodies, Monoclonal - immunology
Blotting, Western
COS Cells
Epitope Mapping
HeLa Cells
Humans
Parainfluenza Virus 2, Human - chemistry
Phosphoproteins - analysis
Phosphoproteins - chemistry
Phosphoproteins - immunology
Viral Proteins - analysis
Viral Proteins - chemistry
Viral Proteins - immunology
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Summary: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.
ISSN:0022-1317
1465-2099
DOI:10.1099/0022-1317-78-6-1303