ArticlePloS one2015
Several N-Glycans on the HIV Envelope Glycoprotein gp120 Preferentially Locate Near Disulphide Bridges and Are Required for Efficient Infectivity and Virus Transmission.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 19 citations in OpenAlex.
- FUT8-mediated core fucosylation of receptor APN drives entry of multiple alphacoronaviruses.PLoS pathogens · 2026Article
- Therapeutic Targeting of Viral N-Glycosylation Modification: From Molecular Mechanisms to Clinical Application Prospects.Infectious diseases and therapy · 2025Review
- Role of N-linked glycosylation in porcine reproductive and respiratory syndrome virus (PRRSV) infection.The Journal of general virology · 2024Article
- Glycosylation of viral proteins: Implication in virus-host interaction and virulence.Virulence · 2022Review
- African Swine Fever Vaccinology: The Biological Challenges from Immunological Perspectives.Viruses · 2022Review
- Hidden Relationships betweenInternational journal of molecular sciences · 2022Review
- Deep Gene Sequence Cluster Analyses of Multi-Virus-Infected Mucosal Tissue Reveal Enhanced Transmission of Acute HIV-1.Journal of virology · 2021Article
- Studying the Expression Efficiencies of Human Clotting Factor IX Analogs, Rationally-designed for Hyper-glycosylation.Iranian journal of pharmaceutical research : IJPR · 2021Article
- The Importance of Glycans of Viral and Host Proteins in Enveloped Virus Infection.Frontiers in immunology · 2021Review
- Synthetic Carbohydrate Chemistry and Translational Medicine.The Journal of organic chemistry · 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
- Human Influenza A Virus Hemagglutinin Glycan Evolution Follows a Temporal Pattern to a Glycan Limit.mBio · 2019Article
- Griffithsin carrageenan fast dissolving inserts prevent SHIV HSV-2 and HPV infections in vivo.Nature communications · 2018Article
- Global aspects of viral glycosylation.Glycobiology · 2018Article
- Viral glycoproteins: biological role and application in diagnosis.Virusdisease · 2016Review
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The HIV envelope glycoprotein gp120 contains nine disulphide bridges and is highly glycosylated, carrying on average 24 N-linked glycans. Using a probability calculation, we here demonstrate that there is a co-localization of disulphide bridges and N-linked glycans in HIV-1 gp120, with a predominance of N-linked glycans in close proximity to disulphide bridges, at the C-terminal side of the involved cysteines. Also, N-glycans are frequently found immediately adjacent to disulphide bridges in gp120 at the N-terminal side of the involved cysteines. In contrast, N-glycans at positions close to, but not immediately neighboring disulphide bridges seem to be disfavored at the N-terminal side of the involved cysteines. Such a pronounced co-localization of disulphide bridges and N-glycans was also found for the N-glycans on glycoprotein E1 of the hepatitis C virus (HCV) but not for other heavily glycosylated proteins such as E2 from HCV and the surface GP from Ebola virus. The potential functional role of the presence of N-glycans near disulphide bridges in HIV-1 gp120 was studied using site-directed mutagenesis, either by deleting conserved N-glycans or by inserting new N-glycosylation sites near disulphide bridges. The generated HIV-1NL4.3 mutants were subjected to an array of assays, determining the envelope glycoprotein levels in mutant viral particles, their infectivity and the capture and transmission efficiencies of mutant virus particles by DC-SIGN. Three N-glycans located nearby disulphide bridges were found to be crucial for the preservation of several of these functions of gp120. In addition, introduction of new N-glycans upstream of several disulphide bridges, at locations where there was a significant absence of N-glycans in a broad variety of virus strains, was found to result in a complete loss of viral infectivity. It was shown that the N-glycan environment around well-defined disulphide bridges of gp120 is highly critical to allow efficient viral infection and transmission.
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