rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
5505
|
pubmed:dateCreated |
2001-3-1
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pubmed:abstractText |
Human immunodeficiency virus type-1 (HIV-1) membrane fusion is promoted by the formation of a trimer-of-hairpins structure that brings the amino- and carboxyl-terminal regions of the gp41 envelope glycoprotein ectodomain into close proximity. Peptides derived from the carboxyl-terminal region (called C-peptides) potently inhibit HIV-1 entry by binding to the gp41 amino-terminal region. To test the converse of this inhibitory strategy, we designed a small protein, denoted 5-Helix, that binds the C-peptide region of gp41. The 5-Helix protein displays potent (nanomolar) inhibitory activity against diverse HIV-1 variants and may serve as the basis for a new class of antiviral agents. The inhibitory activity of 5-Helix also suggests a strategy for generating an HIV-1 neutralizing antibody response that targets the carboxyl-terminal region of the gp41 ectodomain.
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pubmed:grant |
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Feb
|
pubmed:issn |
0036-8075
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
2
|
pubmed:volume |
291
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
884-8
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:11229405-Amino Acid Sequence,
pubmed-meshheading:11229405-Anti-HIV Agents,
pubmed-meshheading:11229405-Carrier Proteins,
pubmed-meshheading:11229405-Cell Line,
pubmed-meshheading:11229405-Drug Design,
pubmed-meshheading:11229405-Giant Cells,
pubmed-meshheading:11229405-HIV Antibodies,
pubmed-meshheading:11229405-HIV Envelope Protein gp41,
pubmed-meshheading:11229405-HIV-1,
pubmed-meshheading:11229405-Humans,
pubmed-meshheading:11229405-Membrane Fusion,
pubmed-meshheading:11229405-Molecular Sequence Data,
pubmed-meshheading:11229405-Neutralization Tests,
pubmed-meshheading:11229405-Peptide Fragments,
pubmed-meshheading:11229405-Peptides,
pubmed-meshheading:11229405-Protein Conformation,
pubmed-meshheading:11229405-Protein Folding,
pubmed-meshheading:11229405-Protein Structure, Secondary,
pubmed-meshheading:11229405-Tumor Cells, Cultured
|
pubmed:year |
2001
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pubmed:articleTitle |
Protein design of an HIV-1 entry inhibitor.
|
pubmed:affiliation |
Howard Hughes Medical Institute, Whitehead Institute for Biomedical Research, Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02142, USA. kimadmin@wi.mit.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|