Target intelligence / Profile preview

High-mannose N-glycans on HIV-1 envelope glycoprotein gp120 (HIV-1 gp120 high-mannose glycans)

Target
HIV-1 gp120 high-mannose glycans
Molecular classification
Glycan, Post-translational modification, Viral surface antigen
01

Overview

High-mannose N-glycans on HIV-1 envelope glycoprotein gp120 are a dense cluster of carbohydrates that form a "glycan shield" on the surface of the HIV-1 envelope protein [nih.gov, 2021]. These glycans are essential for the proper folding of gp120 and play a critical role in shielding the virus from the host's immune system by masking underlying protein epitopes [wikipedia.org, 2024]. Despite their role in immune evasion, specific clusters of these glycans, particularly the "mannose patch," serve as targets for broadly neutralizing antibodies (bNAbs) like PGT121 and 2G12 [nih.gov, 2011]. These antibodies recognize the unique spatial arrangement of the glycans, allowing them to neutralize a wide range of HIV-1 strains [frontiersin.org, 2021]. Therapeutic strategies targeting these glycans include the development of bNAbs for prevention and treatment, as well as lectin-based microbicides like Griffithsin that bind the glycans to block viral entry [nih.gov, 2007].

Other names
Oligomannose glycans on gp120HIV-1 glycan shieldMan9GlcNAc2 glycans on gp120Mannose patch on gp120High-mannose patch
02

Mechanism of action

Neutralization of HIV-1 by binding to the glycan shield, preventing viral attachment to CD4 receptors and co-receptors (CCR5/CXCR4), thereby blocking viral entry [nih.gov, 2024].

03

Biological functions

Viral entryImmune evasionProtein foldingHost cell surface recognition
04

Disease associations

Infection
05

Safety considerations

Viral escape via glycan site mutations [nih.gov, 2007]Potential off-target binding to host glycans [nih.gov, 2002]Immunogenicity of lectin-based therapies [nih.gov, 2007]
06

Interacting drugs

PGT121

7 more in the full profile.

07

Biomarkers

gp120 glycan profile [frontiersin.org, 2021]HIV-1 viral load [nih.gov, 2021]CD4+ T cell count [nih.gov, 2021]N332 glycosylation site presence [nih.gov, 2011]

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