The highly conserved glycan at asparagine 260 of HIV-1 gp120 is indispensable for viral entry.

@article{Franois2011TheHC,
  title={The highly conserved glycan at asparagine 260 of HIV-1 gp120 is indispensable for viral entry.},
  author={Katrien O. François and Jan Balzarini},
  journal={The Journal of biological chemistry},
  year={2011},
  volume={286 50},
  pages={42900-10}
}
Carbohydrate-binding agents bind to the N-glycans of HIV-1 envelope gp120 and prevent viral entry. Carbohydrate-binding agents can select for mutant viruses with deleted envelope glycans. Not all glycosylation motifs are mutated to the same extent. Site-directed mutagenesis revealed that deletions destroying the highly conserved (260)NGS(262) glycosylation motif resulted in non-infectious virus particles. We observed a significant lower CD4 binding in the case of the N260Q mutant gp120 virus… CONTINUE READING
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