ArticleACS infectious diseases2016
Binding Site Geometry and Subdomain Valency Control Effects of Neutralizing Lectins on HIV-1 Viral Particles.
Article in ACS infectious diseases, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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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
18 citing papers in PubMed, 23 citations in OpenAlex.
- Engineering Protein-Based HIV Entry Inhibitors: Advances, Challenges, and Translational Strategies.Biomolecules · 2026Review
- Engineered OAA lectins as selective and sensitive high mannose glycan targeting tools.bioRxiv : the preprint server for biology · 2026Article
- An engineered antibody-lectin conjugate targeting the HIV glycan shield protects humanized mice against HIV challenge.Molecular therapy : the journal of the American Society of Gene Therapy · 2025Article
- The Antiviral Potential of Algal Lectins.Marine drugs · 2023Review
- Irreversible Inactivation of SARS-CoV-2 by Lectin Engagement with Two Glycan Clusters on the Spike Protein.Biochemistry · 2023Article
- Article
- Structure and Carbohydrate Recognition by the Nonmitogenic Lectin Horcolin.Biochemistry · 2022Article
- HIV-1 Entry and Prospects for Protecting against Infection.Microorganisms · 2021Review
- A Carbohydrate-Binding Protein from the Edible Lablab Beans Effectively Blocks the Infections of Influenza Viruses and SARS-CoV-2.Cell reports · 2020Article
- Griffithsin Retains Anti-HIV-1 Potency with Changes in gp120 Glycosylation and Complements Broadly Neutralizing Antibodies PGT121 and PGT126.Antimicrobial agents and chemotherapy · 2019Article
- Griffithsin, a Highly Potent Broad-Spectrum Antiviral Lectin from Red Algae: From Discovery to Clinical Application.Marine drugs · 2019Review
- Quantitative mass imaging of single biological macromolecules.Science (New York, N.Y.) · 2018Article
- Restricted HIV-1 Env glycan engagement by lectin-reengineered DAVEI protein chimera is sufficient for lytic inactivation of the virus.The Biochemical journal · 2018Article
- Heterogeneity in glycan composition on the surface of HIV-1 envelope determines virus sensitivity to lectins.PloS one · 2018Article
- An update of the recombinant protein expression systems of Cyanovirin-N and challenges of preclinical development.BioImpacts : BI · 2018Review
- Chemical and Biophysical Approaches for Complete Characterization of Lectin-Carbohydrate Interactions.Methods in enzymology · 2018Article
- The Tetrameric Plant Lectin BanLec Neutralizes HIV through Bidentate Binding to Specific Viral Glycans.Structure (London, England : 1993) · 2017Article
- Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Carbohydrate binding proteins such as griffithsin, cyanovirin-N, and BanLec are potent HIV entry inhibitors and promising microbicides. Each binds to high-mannose glycans on the surface envelope glycoprotein gp120, yet the mechanisms by which they engage viral spikes and exhibit inhibition constants ranging from nanomolar to picomolar are not understood. To determine the structural and mechanistic basis for recognition and potency, we selected a panel of lectins possessing different valencies per subunit, oligomeric states, and relative orientations of carbohydrate binding sites to systematically probe their contributions to inhibiting viral entry. Cryo-electron micrographs and immuno gold staining of lectin-treated viral particles revealed two distinct effects-namely, viral aggregation or clustering of the HIV-1 envelope on the viral membrane-that were dictated by carbohydrate binding site geometry and valency. "Sandwich" surface plasmon resonance experiments revealed that a second binding event occurs only for those lectins that could aggregate viral particles. Furthermore, picomolar K
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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.