ArticleStructure (London, England : 1993)2017
The Tetrameric Plant Lectin BanLec Neutralizes HIV through Bidentate Binding to Specific Viral Glycans.
Article in Structure (London, England : 1993), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 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
26 citing papers in PubMed, 80 citations in OpenAlex.
- Engineering Protein-Based HIV Entry Inhibitors: Advances, Challenges, and Translational Strategies.Biomolecules · 2026Review
- Comparative Analysis of Banana Lectins rBanLec-Like and H84T-BanLec: An In Silico and In Vitro Approach.The protein journal · 2026Article
- The Biological Role of Enveloped Virus Glycosylation and Its Interactions with Antiviral Lectins.Advances in experimental medicine and biology · 2026Review
- Natural Compounds with Antiviral Activity Against Clinically Relevant RNA Viruses: Advances of the Last Decade.Biomolecules · 2025Review
- Exploration of structural space of Cus17 lectin with glycans using molecular docking and simulation studies.Computational and structural biotechnology journal · 2025Article
- Characterization of a Molecularly Engineered Banlec-Type Lectin (rBTL).Molecular biotechnology · 2024Article
- Mannose-specific plant and microbial lectins as antiviral agents: A review.Glycoconjugate journal · 2024Review
- Lectins from plants and algae act as anti-viral against HIV, influenza and coronaviruses.Molecular biology reports · 2022Review
- A molecularly engineered, broad-spectrum anti-coronavirus lectin inhibits SARS-CoV-2 and MERS-CoV infection in vivo.Cell reports. Medicine · 2022Article
- Antiviral plant-derived natural products to combat RNA viruses: Targets throughout the viral life cycle.Letters in applied microbiology · 2022Review
- Comparison of Enzyme-Linked Lectin Sorbent Assay and Flow Cytometry for Profiling Microbial Glycans.Applied biochemistry and biotechnology · 2022Article
- Structure and Carbohydrate Recognition by the Nonmitogenic Lectin Horcolin.Biochemistry · 2022Article
- H84T BanLec has broad spectrum antiviral activity against human herpesviruses in cells, skin, and mice.Scientific reports · 2022Article
- Review
- BanLec-eGFP Chimera as a Tool for Evaluation of Lectin Binding to High-Mannose Glycans on Microorganisms.Biomolecules · 2021Article
- Glycan Nanostructures of Human Coronaviruses.International journal of nanomedicine · 2021Review
- Glycoprotein Targeted CAR-NK Cells for the Treatment of SARS-CoV-2 Infection.Frontiers in immunology · 2021Article
- Establishing Rules for Self-Adhesion and Aggregation ofLangmuir : the ACS journal of surfaces and colloids · 2020Article
- The barley lectin, horcolin, binds high-mannose glycans in a multivalent fashion, enabling high-affinity, specific inhibition of cellular HIV infection.The Journal of biological chemistry · 2020Article
- Click-Particle Display for Base-Modified Aptamer Discovery.ACS chemical biology · 2019Article
Corrections and comments
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Authors and funding
16 authors at 5 institutions in 2 countries.
Funding
Abstract
Select lectins have powerful anti-viral properties that effectively neutralize HIV-1 by targeting the dense glycan shield on the virus. Here, we reveal the mechanism by which one of the most potent lectins, BanLec, achieves its inhibition. We identify that BanLec recognizes a subset of high-mannose glycans via bidentate interactions spanning the two binding sites present on each BanLec monomer that were previously considered separate carbohydrate recognition domains. We show that both sites are required for high-affinity glycan binding and virus neutralization. Unexpectedly we find that BanLec adopts a tetrameric stoichiometry in solution whereby the glycan-binding sites are positioned to optimally target glycosylated viral spikes. The tetrameric architecture, together with bidentate binding to individual glycans, leads to layers of multivalency that drive viral neutralization through enhanced avidity effects. These structural insights will prove useful in engineering successful lectin therapeutics targeting the dense glycan shield of HIV.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.