Title : N-linked glycosylation of
CXCR4 masks
coreceptor function for
CCR5-dependent human immunodeficiency virus type 1 isolates
Abstract :
- 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
Output (sent_index, trigger,
protein,
sugar,
site):
- 0. glycosylation, , CXCR4, -, -
- 2. glycosylation, , -, -, sites
- 3. glycoprotein, , Env, -, -
- 3. glycoprotein, , HIV envelope glycoprotein, -, -
- 4. glycosylated, , CXCR4, -, -
Output(Part-Of) (sent_index,
protein,
site):
- 2. CXCR4, sites
- 5. Env, sites
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):