Human parainfluenza virus type 2 phosphoprotein: mapping of monoclonal antibody epitopes and location of the multimerization domain.
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.
Nishio
M
M
Department of Microbiology, Mie University School of Medicine, Japan. nishio@doc.medic.mie-u.ac.jp
Tsurudome
M
M
Ito
M
M
Watanabe
N
N
Kawano
M
M
Komada
H
H
Ito
Y
Y
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology*; D015153:Blotting, Western; D019556:COS Cells; D018604:Epitope Mapping; D006367:HeLa Cells; D006801:Humans; D010223:Parainfluenza Virus 2, Human / Q000737:chemistry*; D010750:Phosphoproteins / Q000032:analysis* / Q000737:chemistry / Q000276:immunology; D014764:Viral Proteins / Q000032:analysis* / Q000737:chemistry / Q000276:immunology
D000911:Antibodies, Monoclonal; D010750:Phosphoproteins; D014764:Viral Proteins