| pubmed-article:10756055 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10756055 | lifeskim:mentions | umls-concept:C0019704 | lld:lifeskim |
| pubmed-article:10756055 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:10756055 | lifeskim:mentions | umls-concept:C1332823 | lld:lifeskim |
| pubmed-article:10756055 | lifeskim:mentions | umls-concept:C0017982 | lld:lifeskim |
| pubmed-article:10756055 | lifeskim:mentions | umls-concept:C0370215 | lld:lifeskim |
| pubmed-article:10756055 | lifeskim:mentions | umls-concept:C0024861 | lld:lifeskim |
| pubmed-article:10756055 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:10756055 | pubmed:dateCreated | 2000-5-18 | lld:pubmed |
| pubmed-article:10756055 | pubmed:abstractText | The chemokine receptors CXCR4 and CCR5 are the principal coreceptors for infection of X4 and R5 human immunodeficiency virus type 1 (HIV-1) isolates, respectively. Here we report on the unexpected observation that the removal of the N-linked glycosylation sites in CXCR4 potentially allows the protein to serve as a universal coreceptor for both X4 and R5 laboratory-adapted and primary HIV-1 strains. We hypothesize that this alteration unmasks existing common extracellular structures reflecting a conserved three-dimensional similarity of important elements of CXCR4 and CCR5 that are involved in HIV envelope glycoprotein (Env) interaction. These results may have far-reaching implications for the differential recognition of cell type-dependent glycosylated CXCR4 by HIV-1 isolates and their evolution in vivo. They also suggest a possible explanation for the various observations of restricted virus entry in some cell types and further our understanding of the framework of elements that represent the Env-coreceptor contact sites. | lld:pubmed |
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| pubmed-article:10756055 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10756055 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
