The glycan shield of HIV is predominantly oligomannose independently of production system or viral clade.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 21858152.
- Also identified by DOI 10.1371/journal.pone.0023521 and PMC identifier 3156772.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
The N-linked oligomannose glycans of HIV gp120 are a target for both microbicide and vaccine design. The extent of cross-clade conservation of HIV oligomannose glycans is therefore a critical consideration for the development of HIV prophylaxes. We measured the oligomannose content of virion-associated gp120 from primary virus from PBMCs for a range of viral isolates and showed cross-clade elevation (62-79%) of these glycans relative to recombinant, monomeric gp120 (∼30%). We also confirmed that pseudoviral production systems can give rise to notably elevated gp120 oligomannose levels (∼98%), compared to gp120 derived from a single-plasmid viral system using the HIV(LAI) backbone (56%). This study highlights differences in glycosylation between virion-associated and recombinant gp120.
Medical subject headings
- HIV Envelope Protein gp120
- HIV-1
- Oligosaccharides
- Polysaccharides