Source:http://linkedlifedata.com/resource/pubmed/id/15476879
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2004-10-12
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pubmed:abstractText |
Human immunodeficiency virus type 1 (HIV-1) binds to the human CD4 (hCD4) and a coreceptor to enter permissive human cells. The chemokine receptors, hCCR5 and hCXCR4, are the primary coreceptors used by HIV-1 isolates in vivo, however, hCCR3 has been implicated as a coreceptor for HIV infection of the central nervous system. To determine the domains and amino acids important in hCCR3 coreceptor activity, chimeras between the permissive hCCR3 and the non-permissive rhesus macaque CCR3 (RhCCR3) were constructed and assessed for coreceptor activity for two R5 strains of HIV-1 (YU-2 and ADA) and one R5X4 strain (89.6). Even though three extracellular domains of CCR3 participated in coreceptor activity for the two R5 isolates (ECD-1, ECD-3, and ECD-4), for the R5X4 isolate, ECD-4, and to a lesser extent ECD-3, were critical for coreceptor activity. In addition, residues 13 and 20 in ECD-1, residue 179 in ECD-3, and residue in 271 in ECD-4 of CCR3 were identified for HIV-1 envelope-mediated entry for R5 isolates. In contrast, all the residues on ECD-4 appeared necessary for coreceptor activity for HIV-1(89.6). Therefore, multiple residues on multiple extracellular domains of hCCR3 are important for coreceptor activity for HIV-1.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CCR3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, CCR3,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Chemokine,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, HIV,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0042-6822
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
329
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
109-18
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:15476879-Amino Acid Sequence,
pubmed-meshheading:15476879-Animals,
pubmed-meshheading:15476879-Cell Line,
pubmed-meshheading:15476879-HIV-1,
pubmed-meshheading:15476879-Humans,
pubmed-meshheading:15476879-Macaca mulatta,
pubmed-meshheading:15476879-Molecular Sequence Data,
pubmed-meshheading:15476879-Point Mutation,
pubmed-meshheading:15476879-Receptors, CCR3,
pubmed-meshheading:15476879-Receptors, Chemokine,
pubmed-meshheading:15476879-Receptors, HIV,
pubmed-meshheading:15476879-Recombinant Fusion Proteins
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pubmed:year |
2004
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pubmed:articleTitle |
Multiple residues in the extracellular domains of CCR3 are critical for coreceptor activity.
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pubmed:affiliation |
Department of Biology, School of Medicine, East Carolina University, 600 Moye Boulevard, Greenville, NC 27834, USA. phong.ho@duke.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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