Linked Life Data

20219914

Source:http://linkedlifedata.com/resource/pubmed/id/20219914

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2010-4-22
pubmed:abstractText
Influenza A virus buds from cells as spherical (approximately 100-nm diameter) and filamentous (approximately 100 nm x 2 to 20 microm) virions. Previous work has determined that the matrix protein (M1) confers the ability of the virus to form filaments; however, additional work has suggested that the influenza virus M2 integral membrane protein also plays a role in viral filament formation. In examining the role of the M2 protein in filament formation, we observed that the cytoplasmic tail of M2 contains several sites that are essential for filament formation. Additionally, whereas M2 is a nonraft protein, expression of other viral proteins in the context of influenza virus infection leads to the colocalization of M2 with sites of virus budding and lipid raft domains. We found that an amphipathic helix located within the M2 cytoplasmic tail is able to bind cholesterol, and we speculate that M2 cholesterol binding is essential for both filament formation and the stability of existing viral filaments.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1098-5514
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
84
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5078-88
pubmed:dateRevised
2010-11-2
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Influenza virus m2 ion channel protein is necessary for filamentous virion formation.
pubmed:affiliation
Department of Biochemistry, Molecular Biology, and Cell Biology, and Howard Hughes Medical Institute, Northwestern University, Evanston, Illinois 60208-3500, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural