ArticlePloS one2018
Heterogeneity in glycan composition on the surface of HIV-1 envelope determines virus sensitivity to lectins.
Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- Bird's eye view of natural products for the development of new anti-HIV agents: Understanding from a therapeutic viewpoint.Animal models and experimental medicine · 2025Review
- Swainsonine Protects Human Thyrocytes from Fas-Induced Apoptosis: In vitro Study on Nthy-Ori 3-1 Cell Line.Journal of inflammation research · 2025Article
- HIV-1 interaction with aniScience · 2024Article
- Alterations in N-glycosylation of HCV E2 Protein in Children Patients with IFN-RBV Therapy Failure.Pathogens (Basel, Switzerland) · 2024Article
- Signal peptide exchange alters HIV-1 envelope antigenicity and immunogenicity.Frontiers in immunology · 2024Article
- The role of DC-SIGN as a trans-receptor in infection by MERS-CoV.Frontiers in cellular and infection microbiology · 2023Article
- Lectins and lectibodies: potential promising antiviral agents.Cellular & molecular biology letters · 2022Review
- The Importance of Glycans of Viral and Host Proteins in Enveloped Virus Infection.Frontiers in immunology · 2021Review
- The High Content of Fructose in Human Semen Competitively Inhibits Broad and Potent Antivirals That Target High-Mannose Glycans.Journal of virology · 2020Article
- Article
- Dendritic Cells, the Double Agent in the War Against HIV-1.Frontiers in immunology · 2019Review
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 3 countries.
Funding
Abstract
Lectins that target N-glycans on the surface of HIV-1 envelope (Env) glycoprotein have the potential for use as antiviral agents. Although progress has been made in deciphering the molecular details of lectin and Env glycan interaction, further studies are needed to better understand Env glycan heterogeneity among HIV-1 isolates and its influence on virus-neutralization sensitivity to lectins. This study evaluated a panel of lectins with fine specificity for distinct oligosaccharides and assessed their ability to inhibit infection of HIV-1 viruses known to have differing sensitivity to anti-HIV Env antibodies. The results showed that HIV-1 isolates have different sensitivity to lectins specific for α1-3Man, α1-6Man, and α1-2Man binding lectins. Considering that lectins exclusively recognize the oligosaccharide components of virus Env, these data suggest that glycan heterogeneity among HIV-1 isolates may explain this differential sensitivity. To evaluate this further, chronic and acute viruses were produced in the presence of different glycosidase inhibitors to express more homogenous glycans. Viruses enriched for α1-2Man terminating Man5-9GlcNAc2 glycans became similarly sensitive to α1-2Man-binding lectins. The α1-3Man- and α1-6Man-binding lectins also were more potent against viruses expressing predominantly Man5GlcNAc2 and hybrid type glycans with terminal α1-3Man and α1-6Man. Furthermore, lectin-mediated inhibition was competitively alleviated by mannan and this effect was augmented by enrichment of mannose-type glycans on the virus. In addition, while Env of viruses enriched with mannose-type glycans were sensitive to Endo-H deglycosylation, Env of untreated viruses were partially resistant, indicating that HIV-1 Env glycans are heterogeneously comprised of complex, hybrid, and mannose types. Overall, our data demonstrate that HIV-1 isolates display differential sensitivity to lectins, in part due to the microheterogeneity of N-linked glycans expressed on the surface of the virus Env glycoprotein.
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Registered trials
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