Abstract
ABSTRACTThe 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.
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Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 27, 2002, 6:06 a.m.) |
Deposited | 1 year, 8 months ago (Jan. 5, 2024, 7:26 p.m.) |
Indexed | 1 week, 4 days ago (Aug. 26, 2025, 2:58 a.m.) |
Issued | 25 years, 4 months ago (May 1, 2000) |
Published | 25 years, 4 months ago (May 1, 2000) |
Published Print | 25 years, 4 months ago (May 1, 2000) |
@article{Chabot_2000, title={N-Linked Glycosylation of CXCR4 Masks Coreceptor Function for CCR5-Dependent Human Immunodeficiency Virus Type 1 Isolates}, volume={74}, ISSN={1098-5514}, url={http://dx.doi.org/10.1128/jvi.74.9.4404-4413.2000}, DOI={10.1128/jvi.74.9.4404-4413.2000}, number={9}, journal={Journal of Virology}, publisher={American Society for Microbiology}, author={Chabot, Donald J. and Chen, Hong and Dimitrov, Dimiter S. and Broder, Christopher C.}, year={2000}, month=may, pages={4404–4413} }