Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2010-10-29
pubmed:abstractText
Adenovirus disrupts endosomal membranes during cell entry. The membrane lytic capsid protein VI (pVI) facilitates entry by fragmenting membranes. Although an N-terminal amphipathic ?-helix (VI-?) possesses similar membrane affinity as pVI, truncated protein lacking VI-? (VI?54) still possesses moderate membrane affinity. We demonstrate that incorporation of nickel-NTA lipids in membranes enhances the membrane affinity and the membrane lytic activity of VI?54. We also demonstrate that 3 predicted pVI ?-helices within residues 54-114 associate with membranes, sitting roughly parallel to the membrane surface. His-tagged VI?54 is capable of fragmenting membranes similar to pVI and the VI-? peptide. Interestingly, neither VI-? nor His-tagged VI?54 can induce tubule formation in giant lipid vesicles as observed for pVI. These data suggest cooperativity between the amphipathic ?-helix and residues in VI?54 to induce positive membrane curvature and tubule formation. These results provide additional details regarding the mechanism of nonenveloped virus membrane penetration.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1096-0341
pubmed:author
pubmed:copyrightInfo
Copyright © 2010 Elsevier Inc. All rights reserved.
pubmed:issnType
Electronic
pubmed:day
5
pubmed:volume
408
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
31-8
pubmed:dateRevised
2011-10-5
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
N-terminal ?-helix-independent membrane interactions facilitate adenovirus protein VI induction of membrane tubule formation.
pubmed:affiliation
Department of Microbiology and Immunology, Loyola University Chicago Stritch School of Medicine, Maywood, IL 60153, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural