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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2007-5-25
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pubmed:abstractText |
The chemokine receptor CXCR4 functions as one of the HIV-1 coreceptors and can be considered as an attractive target for the development of novel anti-HIV drugs. Here, we investigated the effect of its two known N-glycosylation sites g1 (NYT) and g2 (NVS) on the antiviral potential of several classes of entry inhibitors. The lack of g1 clearly affected the binding of the amino-terminal directed 2B11 mAb, but not the 12G5 mAb. No dramatic effects on CXCL-12 binding and CXCL-12-induced intracellular calcium responses were observed. Importantly, the anti-HIV-1 activity and antagonistic activity of the prototype compound of CXCR4 inhibitors, AMD3100, were not affected by the presence or absence of the CXCR4 N-glycans. Since CXCR4 N-glycans play a less important role in viral entry compared to the N-glycans on the HIV envelope, cells expressing CXCR4 N-glycosylation mutants might be no relevant alternative to allow HIV-1 escape from antivirals.
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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/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Anti-HIV Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/CXCL12 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Chemokine CXCL12,
http://linkedlifedata.com/resource/pubmed/chemical/Chemokines, CXC,
http://linkedlifedata.com/resource/pubmed/chemical/HIV Fusion Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Heterocyclic Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/JM 3100,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, CXCR4,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, HIV
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0042-6822
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
363
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
280-7
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:17331556-Amino Acid Sequence,
pubmed-meshheading:17331556-Amino Acids,
pubmed-meshheading:17331556-Anti-HIV Agents,
pubmed-meshheading:17331556-Antibodies,
pubmed-meshheading:17331556-Antibodies, Monoclonal,
pubmed-meshheading:17331556-Binding Sites,
pubmed-meshheading:17331556-Cell Line, Tumor,
pubmed-meshheading:17331556-Chemokine CXCL12,
pubmed-meshheading:17331556-Chemokines, CXC,
pubmed-meshheading:17331556-Drug Resistance, Viral,
pubmed-meshheading:17331556-Glycosylation,
pubmed-meshheading:17331556-HIV Fusion Inhibitors,
pubmed-meshheading:17331556-HIV-1,
pubmed-meshheading:17331556-Heterocyclic Compounds,
pubmed-meshheading:17331556-Humans,
pubmed-meshheading:17331556-Lectins,
pubmed-meshheading:17331556-Molecular Sequence Data,
pubmed-meshheading:17331556-Mutation,
pubmed-meshheading:17331556-Protein Binding,
pubmed-meshheading:17331556-Protein Structure, Secondary,
pubmed-meshheading:17331556-Receptors, CXCR4,
pubmed-meshheading:17331556-Receptors, HIV,
pubmed-meshheading:17331556-Signal Transduction,
pubmed-meshheading:17331556-Virulence,
pubmed-meshheading:17331556-Virus Replication
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pubmed:year |
2007
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pubmed:articleTitle |
The role of N-glycosylation sites on the CXCR4 receptor for CXCL-12 binding and signaling and X4 HIV-1 viral infectivity.
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pubmed:affiliation |
Rega Institute for Medical Research, Katholieke Universiteit Leuven, Minderbroedersstraat 10, B-3000 Leuven, Belgium.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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