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.<\/p>\n
A group of Univ. of Alabama at Birmingham has reported about the effects of gp120 glycosylation on infectivity and neutralizing antibodies. As a result, it was confirmed that the infectivity increased by 7 to 9 times when there was N262 glycan modification. In this paper, they have discussed possible mechanisms behind these changes using molecular dynamics models.<\/p>\n","protected":false},"excerpt":{"rendered":" HIV is a virus with envelope proteins in the same way as SARS-CoV-2, and there have been numerous studies on t<\/p><\/div>\n
\nhttps:\/\/pubmed.ncbi.nlm.nih.gov\/33205023\/<\/a><\/p>\n
\nIn addition, it was found that N262 glycan modification reduces the neutralization capacity of HIV neutralizing antibodies.
\nIn particular, PGT151, 35022, 2G12, VRC24, PG16, and PGT145 showed a significant decrease in the capacity.<\/p>\n