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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1996-1-25
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pubmed:abstractText |
The amino-terminal extremity of the human immunodeficiency virus type 1 transmembrane protein (gp41) is thought to play a pivotal role in the fusion of virus membranes with the plasma membrane of the target cell and in syncytium formation. Peptides with sequences taken from the human immunodeficiency virus type 1 gp41 fusogenic (synthetic peptides SPwt and SP-2) and nonfusogenic (SP-3 and SP-4) glycoproteins adopt mainly a beta-sheet conformation in the absence of lipid, as determined by attenuated total reflection Fourier transform infrared spectroscopy, and after interaction with large unilamellar liposomes, the beta-sheet is partly converted into an alpha-helical conformation. Peptides SPwt and SP-2 but not SP-3 or SP-4 were able to promote lipid mixing as assessed by fluorescence energy transfer assay and dye leakage in a vesicle leakage assay. By using polarized attenuated total reflection Fourier transform infrared spectroscopy, SPwt and SP-2 were found to adopt an oblique orientation in the lipid membrane whereas SP-3 and SP-4 were oriented nearly parallel to the plane of the membrane. These findings confirm the correlation between the membrane orientation of the alpha-helix and the lipid mixing ability in vitro. Interestingly, the data provide a direct correlation with the fusogenic activity of the parent glycoproteins in vivo.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523539-1390703,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523539-1915259,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523539-1931950,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523539-2025261,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523539-2184772,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523539-2226461,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523539-2261447,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523539-2541505,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523539-2788443,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523539-2925676,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523539-3404116,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523539-3436962,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523539-3541539,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523539-3571268,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523539-3629244,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523539-3697478,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523539-3753607,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523539-3948290,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523539-4054304,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523539-6313037,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523539-7015107,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523539-7272433,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523539-7284312,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523539-7720880,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523539-7745678,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523539-7811285,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523539-7855879,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523539-8060322,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523539-8289343,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523539-8347581,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8523539-8422404
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0022-538X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
70
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
298-304
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:8523539-Amino Acid Sequence,
pubmed-meshheading:8523539-Binding Sites,
pubmed-meshheading:8523539-Coloring Agents,
pubmed-meshheading:8523539-HIV Envelope Protein gp41,
pubmed-meshheading:8523539-Humans,
pubmed-meshheading:8523539-Lipid Bilayers,
pubmed-meshheading:8523539-Membrane Fusion,
pubmed-meshheading:8523539-Molecular Sequence Data,
pubmed-meshheading:8523539-Protein Conformation,
pubmed-meshheading:8523539-Spectroscopy, Fourier Transform Infrared
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pubmed:year |
1996
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pubmed:articleTitle |
Lipid membrane fusion induced by the human immunodeficiency virus type 1 gp41 N-terminal extremity is determined by its orientation in the lipid bilayer.
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pubmed:affiliation |
Laboratoire de Chimie-Physique des Macromolécules aux Interfaces, Université Libre de Bruxelles, Belgium.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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