The Role of Carbohydrate at Asparagine 386 in HIV-1 gp120
Author Information
Author(s): Sanders Rogier W, van Anken Eelco, Nabatov Alexei A, Liscaljet I Marije, Bontjer Ilja, Eggink Dirk, Melchers Mark, Busser Els, Dankers Martijn M, Groot Fedde, Braakman Ineke, Berkhout Ben, Paxton William A
Primary Institution: Academic Medical Center of the University of Amsterdam
Hypothesis
The carbohydrate at asparagine 386 on HIV-1 gp120 is not essential for protein folding and function but is involved in immune evasion.
Conclusion
The carbohydrate at position 386 is not essential for protein folding and function, but is involved in the protection of the CD4 binding site from antibodies.
Supporting Evidence
- The removal of the 386 glycan improved the folding of a gp120 variant lacking the 385–418 disulfide bond.
- The 386 carbohydrate was not critical for gp120 binding to dendritic cells.
- Neutralization by soluble CD4 was significantly enhanced in the absence of the 386 sugar.
- Removal of the 386 glycan may improve the elicitation of neutralizing CD4 binding site antibodies.
Takeaway
The sugar at position 386 on the HIV-1 virus helps hide an important part of the virus from the immune system, but it isn't necessary for the virus to work properly.
Methodology
The study involved evolution experiments, virus replication assays, and neutralization assays to assess the role of the N386 glycan.
Limitations
The study may not fully capture the role of the N386 glycan in different biological contexts or in primary immune cells.
Digital Object Identifier (DOI)
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