ArticlePloS one2014
Deletion of the highly conserved N-glycan at Asn260 of HIV-1 gp120 affects folding and lysosomal degradation of gp120, and results in loss of viral infectivity.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- N-linked glycosylation of GETV envelope proteins affect viral infection and pathogenicity.Virulence · 2026Article
- An Evolutionary Distinct Nipah Virus N-Glycosylation Site Provides Stability for Receptor Engagement.Molecular & cellular proteomics : MCP · 2026Article
- Glycosylated NS3/NS3A protein of bluetongue virus facilitates efficient viral egress via lipid raft anchoring.Journal of virology · 2026Article
- The Role of Glycans in Human Immunity-A Sweet Code.Molecules (Basel, Switzerland) · 2025Review
- Mannose-specific plant and microbial lectins as antiviral agents: A review.Glycoconjugate journal · 2024Review
- Signal peptide exchange alters HIV-1 envelope antigenicity and immunogenicity.Frontiers in immunology · 2024Article
- Review
- HBZ upregulates myoferlin expression to facilitate HTLV-1 infection.PLoS pathogens · 2023Article
- Glycosylation of viral proteins: Implication in virus-host interaction and virulence.Virulence · 2022Review
- Glycosylation States on Intact Proteins Determined by NMR Spectroscopy.Molecules (Basel, Switzerland) · 2021Article
- The Role of Glycosylation in Infectious Diseases.Advances in experimental medicine and biology · 2021Review
- Changes in Protein Glycosylation in Head and Neck Squamous Cell Carcinoma.Journal of Cancer · 2021Review
- Quantification of the Resilience and Vulnerability of HIV-1 Native Glycan Shield at Atomistic Detail.iScience · 2020Article
- Glycan Positioning Impacts HIV-1 Env Glycan-Shield Density, Function, and Recognition by Antibodies.iScience · 2020Article
- Engineering of a Lectibody Targeting High-Mannose-Type Glycans of the HIV Envelope.Molecular therapy : the journal of the American Society of Gene Therapy · 2019Article
- HIV-1 subtype C Envelope function becomes less sensitive to N-glycosylation deletion during disease progression.BMC research notes · 2019Article
- Glycosylation of viral surface proteins probed by mass spectrometry.Current opinion in virology · 2019Review
- Stabilization of the V2 loop improves the presentation of V2 loop-associated broadly neutralizing antibody epitopes on HIV-1 envelope trimers.The Journal of biological chemistry · 2019Article
- Defining HIV-1 Envelope N-Glycan Microdomains through Site-Specific Heterogeneity Profiles.Journal of virology · 2019Article
- Global site-specific analysis of glycoprotein N-glycan processing.Nature protocols · 2018Article
Corrections and comments
- Erratum issued
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
N-linked glycans covering the surface of the HIV-1 glycoprotein gp120 are of major importance for the correct folding of this glycoprotein. Of the, on average, 24 N-linked glycans present on gp120, the glycan at Asn260 was reported to be essential for the correct expression of gp120 and gp41 in the virus particle and deletion of the N260 glycan in gp120 heavily compromised virus infectivity. We show here that gp160 containing the N260Q mutation reaches the Golgi apparatus during biosynthesis. Using pulse-chase experiments with [35S] methionine/cysteine, we show that oxidative folding was slightly delayed in case of mutant N260Q gp160 and that CD4 binding was markedly compromised compared to wild-type gp160. In the search of compensatory mutations, we found a mutation in the V1/V2 loop of gp120 (S128N) that could partially restore the infectivity of mutant N260Q gp120 virus. However, the mutation S128N did not enhance any of the above-mentioned processes so its underlying compensatory mechanism must be a conformational effect that does not affect CD4 binding per se. Finally, we show that mutant N260Q gp160 was cleaved to gp120 and gp41 to a much lower extent than wild-type gp160, and that it was subject of lysosomal degradation to a higher extent than wild-type gp160 showing a prominent role of this process in the breakdown of N260-glycan-deleted gp160, which could not be counteracted by the S128N mutation. Moreover, at least part of the wild-type or mutant gp160 that is normally targeted for lysosomal degradation reached a conformation that enabled CD4 binding.
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