ArticleMolecular pharmaceutics2013
Inhibition of hepatitis C virus by the cyanobacterial protein Microcystis viridis lectin: mechanistic differences between the high-mannose specific lectins MVL, CV-N, and GNA.
Article in Molecular pharmaceutics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 49 citations in OpenAlex.
- Phycocompounds from Cyanobacteria: Exploring Synergistic Effects with Conventional Anticancer and Antimicrobial Properties.ACS omega · 2025Review
- Mannose-specific plant and microbial lectins as antiviral agents: A review.Glycoconjugate journal · 2024Review
- Cyanometabolites: molecules with immense antiviral potential.Archives of microbiology · 2023Review
- A novel plant lectin, NTL-125, interferes with SARS-CoV-2 interaction with hACE2.Virus research · 2022Article
- Lectins and lectibodies: potential promising antiviral agents.Cellular & molecular biology letters · 2022Review
- Legume Lectins with Different Specificities as Potential Glycan Probes for Pathogenic Enveloped Viruses.Cells · 2022Review
- Revisiting the role of cyanobacteria-derived metabolites as antimicrobial agent: A 21st century perspective.Frontiers in microbiology · 2022Review
- Algal and Cyanobacterial Lectins and Their Antimicrobial Properties.Marine drugs · 2021Review
- Evaluation of Microalgae Antiviral Activity and Their Bioactive Compounds.Antibiotics (Basel, Switzerland) · 2021Review
- Antiviral Cyanometabolites-A Review.Biomolecules · 2021Review
- Exploring algae and cyanobacteria as a promising natural source of antiviral drug against SARS-CoV-2.Biomedical journal · 2021Review
- Article
- Biolayer interferometry provides a robust method for detecting DNA binding small molecules in microbial extracts.Analytical and bioanalytical chemistry · 2021Article
- N-Linked Surface Glycan Biosynthesis, Composition, Inhibition, and Function in Cnidarian-Dinoflagellate Symbiosis.Microbial ecology · 2020Article
- Article
- Lectin microarray and mass spectrometric analysis of hepatitis C proteins reveals N-linked glycosylation.Medicine · 2018Article
- Determinants in the Ig Variable Domain of Human HAVCR1 (TIM-1) Are Required To Enhance Hepatitis C Virus Entry.Journal of virology · 2018Article
- Glycan Shielding and Modulation of Hepatitis C Virus Neutralizing Antibodies.Frontiers in immunology · 2018Review
- Lectins as Promising Therapeutics for the Prevention and Treatment of HIV and Other Potential Coinfections.BioMed research international · 2018Review
- Effects of microvirin monomers and oligomers on hepatitis C virus.Bioscience reports · 2017Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 1 country.
Funding
Abstract
Plant or microbial lectins are known to exhibit potent antiviral activities against viruses with glycosylated surface proteins, yet the mechanism(s) by which these carbohydrate-binding proteins exert their antiviral activities is not fully understood. Hepatitis C virus (HCV) is known to possess glycosylated envelope proteins (gpE1E2) and to be potently inhibited by lectins. Here, we tested in detail the antiviral properties of the newly discovered Microcystis viridis lectin (MVL) along with cyanovirin-N (CV-N) and Galanthus nivalis agglutinin (GNA) against cell culture HCV, as well as their binding properties toward viral particles, target cells, and recombinant HCV glycoproteins. Using infectivity assays, CV-N, MVL, and GNA inhibited HCV with IC50 values of 0.6 nM, 30.4 nM, and 11.1 nM, respectively. Biolayer interferometry analysis demonstrated a higher affinity of GNA to immobilized recombinant HCV glycoproteins compared to CV-N and MVL. Complementary studies, including fluorescence-activated cell sorting (FACS) analysis, confocal microscopy, and pre- and post-virus binding assays, showed a complex mechanism of inhibition for CV-N and MVL that includes both viral and cell association, while GNA functions by binding directly to the viral particle. Combinations of GNA with CV-N or MVL in HCV infection studies revealed synergistic inhibitory effects, which can be explained by different glycan recognition profiles of the mainly high-mannoside specific lectins, and supports the hypothesis that these lectins inhibit through different and complex modes of action. Our findings provide important insights into the mechanisms by which lectins inhibit HCV infection. Overall, the data suggest MVL and CV-N have the potential for toxicity due to interactions with cellular proteins while GNA may be a better therapeutic agent due to specificity for the HCV gpE1E2.
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Registered trials
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