Linked Life Data

8576195

Source:http://linkedlifedata.com/resource/pubmed/id/8576195

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1996-3-12
pubmed:abstractText
We have investigated the influence of influenza-induced membrane fusion on the transverse asymmetry of the viral and target membranes. Large unilamellar vesicles containing headgroup-labeled fluorescent phospholipid analogues in both leaflets of the membrane were treated with phospholipase D, converting all outer membrane phospholipids to phosphatidic acid and leading to the release of the fluorescent label from the outside leaflet. After fusion of virus with these liposomes, addition of the enzyme to the fusion product did not release fluorescent label again, indicating that the phospholipid analogues from the inner leaflet of the membranes had not appeared on the outer leaflet. Moreover, the integral membrane protein hemagglutinin, which is present on the outer leaflet of the viral membrane, was quantitatively digested with protease after fusion, indicating that hemagglutinin remained on the outer leaflet of the fusion product. Therefore, there is no merger of the inner with outer leaflets of the viral or the liposomal membrane during fusion and transverse membrane asymmetry is maintained.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
271
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2383-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Membrane asymmetry is maintained during influenza-induced fusion.
pubmed:affiliation
Department of Biophysical Chemistry, Biozentrum of University of Basel, Switzerland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't