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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2003-3-12
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pubmed:abstractText |
CD38 is a progression marker in HIV-1 infection, it displays lateral association with CD4, and down-modulates gp120/CD4 binding. The aim of this study was to elucidate the mechanism behind the interplay between CD4, CD38, and HIV-1. We used mouse cell transfectants expressing human CD4 and either CD38 or other CD4-associated molecules to show that CD38 specifically inhibits gp120/CD4 binding. Human cell transfectants expressing truncated forms of CD38 and bioinformatic analysis were used to map the anti-HIV activity and show that it is concentrated in the membrane-proximal region. This region displayed significant sequence-similarity with the V3 loop of the HIV-1 gp120 glycoprotein. In line with this similarity, synthetic soluble peptides derived from this region reproduced the anti-HIV effects of full-length CD38 and inhibited HIV-1 and HIV-2 primary isolates from different subtypes and with different coreceptor use. A multiple-branched peptide construct presenting part of the sequence of the V3-like region potently and selectively inhibited HIV-1 replication in the nanomolar range. Conversely, a deletion in the V3-like region abrogated the anti-HIV-1 activity of CD38 and its lateral association with CD4. These findings may provide new insights into the early events of HIV-1 fusion and strategies to intervene.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/ADP-ribosyl Cyclase,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD38,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD4,
http://linkedlifedata.com/resource/pubmed/chemical/CD38 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cd38 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/HIV Envelope Protein gp120,
http://linkedlifedata.com/resource/pubmed/chemical/HIV Fusion Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Virus
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1530-6860
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pubmed:author |
pubmed-author:BensiTheaT,
pubmed-author:BottarelFlaviaF,
pubmed-author:ButtòStefanoS,
pubmed-author:CafaroAurelioA,
pubmed-author:CalossoLilianaL,
pubmed-author:ChiocchettiAnnalisaA,
pubmed-author:DeaglioSilviaS,
pubmed-author:DianzaniUmbertoU,
pubmed-author:EnsoliBarbaraB,
pubmed-author:FerreroEnzaE,
pubmed-author:KatadaToshiakiT,
pubmed-author:MalavasiFabioF,
pubmed-author:MesturiniRiccardoR,
pubmed-author:OrtolanErikaE,
pubmed-author:SavarinoAndreaA
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pubmed:issnType |
Electronic
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pubmed:volume |
17
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
461-3
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pubmed:dateRevised |
2005-11-17
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pubmed:meshHeading |
pubmed-meshheading:12551845-ADP-ribosyl Cyclase,
pubmed-meshheading:12551845-Amino Acid Motifs,
pubmed-meshheading:12551845-Animals,
pubmed-meshheading:12551845-Antigens, CD,
pubmed-meshheading:12551845-Antigens, CD38,
pubmed-meshheading:12551845-Antigens, CD4,
pubmed-meshheading:12551845-Cell Line,
pubmed-meshheading:12551845-Down-Regulation,
pubmed-meshheading:12551845-HIV Envelope Protein gp120,
pubmed-meshheading:12551845-HIV Fusion Inhibitors,
pubmed-meshheading:12551845-HIV-1,
pubmed-meshheading:12551845-Humans,
pubmed-meshheading:12551845-Membrane Fusion,
pubmed-meshheading:12551845-Membrane Glycoproteins,
pubmed-meshheading:12551845-Mice,
pubmed-meshheading:12551845-Models, Biological,
pubmed-meshheading:12551845-Peptides,
pubmed-meshheading:12551845-Protein Structure, Tertiary,
pubmed-meshheading:12551845-Receptors, Virus,
pubmed-meshheading:12551845-Sequence Homology, Amino Acid,
pubmed-meshheading:12551845-Transfection,
pubmed-meshheading:12551845-Virus Replication
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pubmed:year |
2003
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pubmed:articleTitle |
Human CD38 interferes with HIV-1 fusion through a sequence homologous to the V3 loop of the viral envelope glycoprotein gp120.
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pubmed:affiliation |
Laboratory of Immunology, Interdisciplinary Research Center of Autoimmune Diseases, Department of Medical Science, University of Eastern Piedmont, Novara, Italy. asavarino@medscape.com
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pubmed:publicationType |
Journal Article
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