Linked Life Data

2724410

Source:http://linkedlifedata.com/resource/pubmed/id/2724410

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1989-6-27
pubmed:abstractText
Flaviviruses are enveloped viruses which accumulate in cellular vacuoles prior to release. The membrane of cell-associated virus contains the proteins pre-M and E. During release of virus the pre-M protein is cleaved, and only its carboxy-terminal segment remains associated with the virus as M protein. Studies of the association of membrane proteins of intracellular and extracellular particles of West Nile virus show that in cell-associated virus the pre-M and E proteins are present as E+pre-M heterodimers. Cleavage of pre-M during release leads to dissociation of the heterodimers: the amino-terminal region of the pre-M protein is lost from the virus, whereas the proteins M and E remain associated with the viral membrane as separate molecules. The E protein of extracellular virus has a tendency to oligomerize into trimers, and both E-protein monomers and trimers are present on extracellular virions. We have prepared partially purified extracellular virus without loss of viral infectivity. These preparations contain approximately 600 physical particles for each PFU. Since purification of cell-associated virus results in significant loss of PFU, an inactivation of virus may occur during this procedure. Preparations of cell-associated virus contained approximately 40,000 physical particles for each PFU.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/2724410-2992152, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724410-3000978, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724410-3035906, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724410-3629975, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724410-3811228, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724410-3855247, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724410-4360393, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724410-462816, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724410-4629690, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724410-5432063, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724410-7126526, http://linkedlifedata.com/resource/pubmed/commentcorrection/2724410-7381430
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0022-538X
pubmed:author
pubmed:issnType
Print
pubmed:volume
63
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2521-6
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Cell-associated West Nile flavivirus is covered with E+pre-M protein heterodimers which are destroyed and reorganized by proteolytic cleavage during virus release.
pubmed:affiliation
Institut für Virologie, Justus-Liebig-Universität, Giessen, Federal Republic of Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't