Linked Life Data

2409671

Source:http://linkedlifedata.com/resource/pubmed/id/2409671

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1985-8-21
pubmed:abstractText
At pH 5 influenza virus hemagglutinin undergoes an irreversible conformational change (J.J. Skehel, P. M. Bayley, E. B. Brown, S. R. Martin, M. D. Waterfield, J. M. White, I. A. Wilson, and D. C. Wiley (1982). Proc. Natl. Acad. Sci. USA 79, 968-972) which parallels the appearance of fusion activity of this molecule. This paper describes experiments which explore the conformational change using a panel of monoclonal antibodies which define four of the major antigenic sites of this protein. The results indicate that three of the major antigenic sites of hemagglutinin undergo changes when exposed to acid pH. These changes have little effect on the binding avidity of influenza virus to glycophorin, the major receptor present on the red blood cell surface. These findings have been used to postulate a mechanism where the molecule flexes around a central region resulting in rearrangement in space of its component domains on exposure to low pH.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0042-6822
pubmed:author
pubmed:issnType
Print
pubmed:volume
145
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
72-83
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Antigenic determinants of influenza virus hemagglutinin. XI. Conformational changes detected by monoclonal antibodies.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't