Linked Life Data

3972812

Source:http://linkedlifedata.com/resource/pubmed/id/3972812

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1985-4-11
pubmed:abstractText
The hemagglutinin (HA) spike glycoprotein of influenza virus catalyzes a low pH-induced membrane fusion event which releases the viral genome into the host cell cytoplasm. To study the fusion mechanism in more detail, we have prepared the ectodomain of HA in water-soluble form by treating virus particles with bromelain. Under mildly acidic conditions (pH less than or equal to 5.8), the ectodomain undergoes a conformational change which we found to be biochemically and immunologically equivalent to that in native viral HA. It became sensitive to proteinase K, it exposed new antigenic epitopes in its HA1 chain, and it acquired amphiphilic properties, notably the ability to bind to liposomes. The attachment to liposomes exhibited the same pH dependence and rapid kinetics as the conformational change and was mediated by HA2. The nature of the attachment resembled that of an integral membrane protein except that the bound HA was partially removed by base. As observed for virus fusion, attachment is independent of divalent cations and lipid composition. Temperature was found to be a critical parameter only with dimyristoylphosphatidycholine vesicles where attachment was partially blocked below the major phase transition. These and other results obtained indicated that the low pH-induced conformational change in the isolated ectodomain is equivalent to that occurring in intact viral HA, and that its attachment to liposomes can serve as a model for the initial stages in the HA-induced membrane fusion reaction.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
260
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2973-81
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Membrane fusion activity of the influenza virus hemagglutinin. The low pH-induced conformational change.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't