HIV is a virus with envelope proteins in the same way as SARS-CoV-2, and there have been numerous studies on the structure and glycan modification of that protein. The envelope protein of HIV is called gp160 and is made up of two sub-units, gp41 and gp120. HIV infection is initiated by gp120 binding to CD4 receptors on T cells. Gp120 has 27 N-type glycan modification sites and is known to be strongly glycosylated with high mannose.
A group of Univ. of Alabama at Birmingham has reported about the effects of gp120 glycosylation on infectivity and neutralizing antibodies.
https://pubmed.ncbi.nlm.nih.gov/33205023/
As a result, it was confirmed that the infectivity increased by 7 to 9 times when there was N262 glycan modification.
In addition, it was found that N262 glycan modification reduces the neutralization capacity of HIV neutralizing antibodies.
In particular, PGT151, 35022, 2G12, VRC24, PG16, and PGT145 showed a significant decrease in the capacity.
In this paper, they have discussed possible mechanisms behind these changes using molecular dynamics models.