Source:http://linkedlifedata.com/resource/pubmed/id/20869737
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2010-10-29
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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.
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pubmed:grant |
http://linkedlifedata.com/resource/pubmed/grant/AI007508,
http://linkedlifedata.com/resource/pubmed/grant/AI082430,
http://linkedlifedata.com/resource/pubmed/grant/HL054352,
http://linkedlifedata.com/resource/pubmed/grant/R01 HL054352-16,
http://linkedlifedata.com/resource/pubmed/grant/R01 HL054352-17,
http://linkedlifedata.com/resource/pubmed/grant/R21 AI082430-01
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1096-0341
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pubmed:author | |
pubmed:copyrightInfo |
Copyright © 2010 Elsevier Inc. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
5
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pubmed:volume |
408
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
31-8
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pubmed:dateRevised |
2011-10-5
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pubmed:meshHeading |
pubmed-meshheading:20869737-Adenoviridae,
pubmed-meshheading:20869737-Capsid Proteins,
pubmed-meshheading:20869737-Cell Membrane,
pubmed-meshheading:20869737-Models, Molecular,
pubmed-meshheading:20869737-Protein Binding,
pubmed-meshheading:20869737-Protein Structure, Secondary,
pubmed-meshheading:20869737-Protein Structure, Tertiary,
pubmed-meshheading:20869737-Sequence Deletion,
pubmed-meshheading:20869737-Virus Internalization
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pubmed:year |
2010
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pubmed:articleTitle |
N-terminal ?-helix-independent membrane interactions facilitate adenovirus protein VI induction of membrane tubule formation.
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pubmed:affiliation |
Department of Microbiology and Immunology, Loyola University Chicago Stritch School of Medicine, Maywood, IL 60153, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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