Oligomannose glycan on viral envelope

Oligomannose glycans are N-linked glycans composed primarily of five to nine mannose residues (Man5-9GlcNAc2) found on the envelope glycoproteins of many enveloped viruses, including HIV-1, Ebola virus, and Hepatitis C virus[1][5][7]. These glycans create a "glycan shield" that covers significant portions of the viral protein surface, protecting viral envelope proteins from neutralizing antibodies and immune recognition[3][5]. The oligomannose patch is unusually conserved compared to host glycoproteins, as viral glycoproteins are often partially processed by host glycosylation enzymes, resulting in the retention of under-processed, high-mannose glycans[1][3][5]. This structural motif plays key roles in mediating virus-host interactions (e.g., binding to C-type lectin receptors such as DC-SIGN), facilitating virus attachment, entry, and immune evasion[1][6][7][9]. Because of its conservation and immunological distinctness, the oligomannose glycan patch is recognized as a potential therapeutic target for broadly neutralizing antibodies and glycan-binding antiviral drugs, although the similarity to host glycans and high variability between viruses remain challenges for drug and vaccine development[1][3][5].

Other names

oligomannose-type glycanoligomannose patchhigh-mannose glycanMan5–9GlcNAc2 glycanviral N-linked oligomannose glycan

Neutralization by binding to oligomannose glycans and blocking virus-receptor interaction (e.g., by broadly neutralizing antibodies). Lectin-mediated binding to oligomannose glycans, leading to viral aggregation or entry inhibition.