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PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1997-7-3
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0022-1317
pubmed:author
pubmed:issnType
Print
pubmed:volume
78 ( Pt 6)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1303-8
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Human parainfluenza virus type 2 phosphoprotein: mapping of monoclonal antibody epitopes and location of the multimerization domain.
pubmed:affiliation
Department of Microbiology, Mie University School of Medicine, Japan. nishio@doc.medic.mie-u.ac.jp
pubmed:publicationType
Journal Article