AI Article Synopsis
- About 50% of the HIV-1 Envelope glycoprotein (gp120) mass consists of N-linked carbohydrates, previously thought to lack O-linked carbohydrates.
- A study reveals that some HIV-1 patient isolates do contain O-linked carbohydrates on the variable 1 (V1) domain of gp120.
- This O-glycosylation significantly decreases the virus's sensitivity to neutralization by certain antibodies, indicating a potential strategy for the virus to evade the immune response.
Article Abstract
Approximately 50% of the mass of the Envelope (Env) glycoprotein surface subunit (gp120) of human immunodeficiency virus type 1 (HIV-1) is composed of N-linked carbohydrate. Until now, the dogma has been that HIV-1 lacks O-linked carbohydrate on Env. Here we show that a subset of patient-derived HIV-1 isolates contain O-linked carbohydrate on the variable 1 (V1) domain of Env gp120. We demonstrate the presence of this O-glycosylation both on virions and on gp120 expressed as a secreted protein. Further, we establish that these O-linked glycans can confer a more than 1,000-fold decrease in neutralization sensitivity (IC) to V3-glycan broadly neutralizing antibodies. These findings uncover a structural modification to the HIV-1 Env and suggest a functional role in promoting viral escape from one category of broadly neutralizing antibodies.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7904042 | PMC |
| http://dx.doi.org/10.1016/j.celrep.2020.01.056 | DOI Listing |
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