| pubmed-article:18925934 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18925934 | lifeskim:mentions | umls-concept:C0019704 | lld:lifeskim |
| pubmed-article:18925934 | lifeskim:mentions | umls-concept:C0021311 | lld:lifeskim |
| pubmed-article:18925934 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
| pubmed-article:18925934 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
| pubmed-article:18925934 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:18925934 | lifeskim:mentions | umls-concept:C0205107 | lld:lifeskim |
| pubmed-article:18925934 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:18925934 | lifeskim:mentions | umls-concept:C1999216 | lld:lifeskim |
| pubmed-article:18925934 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
| pubmed-article:18925934 | lifeskim:mentions | umls-concept:C0439751 | lld:lifeskim |
| pubmed-article:18925934 | lifeskim:mentions | umls-concept:C0913822 | lld:lifeskim |
| pubmed-article:18925934 | lifeskim:mentions | umls-concept:C0913823 | lld:lifeskim |
| pubmed-article:18925934 | pubmed:dateCreated | 2008-11-21 | lld:pubmed |
| pubmed-article:18925934 | pubmed:abstractText | The membrane proximal region (MPR) of the transmembrane subunit, gp41, of the HIV envelope glycoprotein plays a critical role in HIV-1 infection of CD4+ target cells and CD4-independent mucosal entry. It contains continuous epitopes recognized by neutralizing IgG antibodies 2F5, 4E10 and Z13, and is therefore considered to be a promising target for vaccine design. Moreover, some MPR-derived peptides, such as T20 (enfuvirtide), are in clinical use as HIV-1 inhibitors. We have shown that an extended MPR peptide, P5, harbouring the lectin-like domain of gp41 and a calcium-binding site, is implicated in the interaction of HIV with its mucosal receptor. We now investigate the potential antiviral activities of P5 and other such long MPR-derived peptides. Structural studies of gp41 MPR-derived peptides using circular dichroism showed that the peptides P5 (a.a.628-683), P1 (a.a.648-683), P5L (a.a.613-683) and P7 (a.a.613-746) displayed a well-defined alpha-helical structure. Peptides P5 inhibited HIV-1 envelope mediated cell-cell fusion and infection of peripheral blood mononuclear cells by both X4- and R5-tropic HIV-1 strains, whereas peptides P5 mutated in the calcium binding site or P1 lacked antiviral activity, when P5L blocked cell fusion in contrast to P7. Strikingly, P5 inhibited CD4-dependent infection by T20-resistant R5-tropic HIV-1 variants. Cell-cell fusion studies indicated that the anti-HIV-1 activity of P5, unlike T20, could not be abrogated in the presence of the N-terminal leucine zipper domain (LZ). These results suggested that P5 could serve as a potent fusion inhibitor. | lld:pubmed |
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| pubmed-article:18925934 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:18925934 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:18925934 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18925934 | pubmed:issn | 1742-4690 | lld:pubmed |
| pubmed-article:18925934 | pubmed:author | pubmed-author:ClavelFrançoi... | lld:pubmed |
| pubmed-article:18925934 | pubmed:author | pubmed-author:BomselMorgane... | lld:pubmed |
| pubmed-article:18925934 | pubmed:author | pubmed-author:AlfsenAnnette... | lld:pubmed |
| pubmed-article:18925934 | pubmed:author | pubmed-author:TudorDanielaD | lld:pubmed |
| pubmed-article:18925934 | pubmed:author | pubmed-author:YuHuifengH | lld:pubmed |
| pubmed-article:18925934 | pubmed:author | pubmed-author:LabrosseBeatr... | lld:pubmed |
| pubmed-article:18925934 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18925934 | pubmed:volume | 5 | lld:pubmed |
| pubmed-article:18925934 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18925934 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18925934 | pubmed:pagination | 93 | lld:pubmed |
| pubmed-article:18925934 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:18925934 | pubmed:meshHeading | pubmed-meshheading:18925934... | lld:pubmed |
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| pubmed-article:18925934 | pubmed:meshHeading | pubmed-meshheading:18925934... | lld:pubmed |
| pubmed-article:18925934 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18925934 | pubmed:articleTitle | Peptide P5 (residues 628-683), comprising the entire membrane proximal region of HIV-1 gp41 and its calcium-binding site, is a potent inhibitor of HIV-1 infection. | lld:pubmed |
| pubmed-article:18925934 | pubmed:affiliation | Departement de Biologie Cellulaire, (Cell Biology Department), Institut Cochin, Université Paris Descartes, CNRS (UMR 8104), 22 rue Mechain, 75014 Paris, France. yu@cochin.inserm.fr | lld:pubmed |
| pubmed-article:18925934 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18925934 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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