ArticleThe Journal of antimicrobial chemotherapy2015
NICTABA and UDA, two GlcNAc-binding lectins with unique antiviral activity profiles.
Article in The Journal of antimicrobial chemotherapy, 2015. 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, 43 citations in OpenAlex.
- Dataset of manually curated peptides against arthropod-borne viruses.Data in brief · 2026Article
- The Biological Role of Enveloped Virus Glycosylation and Its Interactions with Antiviral Lectins.Advances in experimental medicine and biology · 2026Review
- Bridging Viral Glycobiology and Lectin Biotechnology for Antiviral and Diagnostic Strategies.ACS bio & med chem Au · 2025Review
- Stinging Nettle (Plants (Basel, Switzerland) · 2025Review
- The crystal structure of Nictaba reveals its carbohydrate-binding properties and a new lectin dimerization mode.Glycobiology · 2024Article
- Glycosylated SARs Cov 2 interaction with plant lectins.Glycoconjugate journal · 2024Review
- Cyanovirin-N Binding toBiochemistry · 2024Article
- A Complex-TypeInternational journal of molecular sciences · 2024Article
- Mannose-specific plant and microbial lectins as antiviral agents: A review.Glycoconjugate journal · 2024Review
- Article
- Antimicrobial peptides: A promising tool to combat multidrug resistance in SARS CoV2 era.Microbiological research · 2022Review
- Plant lectins as potent Anti-coronaviruses, Anti-inflammatory, antinociceptive and antiulcer agents.Saudi journal of biological sciences · 2022Review
- Lectins and lectibodies: potential promising antiviral agents.Cellular & molecular biology letters · 2022Review
- Plant lectins as prospective antiviral biomolecules in the search for COVID-19 eradication strategies.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2022Review
- Legume Lectins with Different Specificities as Potential Glycan Probes for Pathogenic Enveloped Viruses.Cells · 2022Review
- Carbohydrate-binding protein from stinging nettle as fusion inhibitor for SARS-CoV-2 variants of concern.Frontiers in cellular and infection microbiology · 2022Article
- Plant-Derived Antimicrobial Peptides as Potential Antiviral Agents in Systemic Viral Infections.Pharmaceuticals (Basel, Switzerland) · 2021Review
- Review
- A Simple Biomimetic Receptor Selectively Recognizing the GlcNAcAngewandte Chemie (International ed. in English) · 2021Article
- Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
objectivesThis study aimed to assess the antiviral properties of a unique lectin (NICTABA) produced by the tobacco plant, Nicotiana tabacum.
methodsCellular assays were used to investigate the antiviral activity of NICTABA and Urtica dioica agglutinin (UDA). Surface plasmon resonance (SPR) studies were performed to study the sugar specificity and the interactions of both lectins with the envelope glycoproteins of HIV-1.
resultsThe N-acetyl-d-glucosamine (GlcNAc)-binding lectins exhibited broad-spectrum activity against several families of enveloped viruses including influenza A/B, Dengue virus type 2, herpes simplex virus types 1 and 2 and HIV-1/2. The IC50 of NICTABA for various HIV-1 strains, clinical isolates and HIV-2 assessed in PBMCs ranged from 5 to 30 nM. Furthermore, NICTABA inhibited syncytium formation between persistently HIV-1-infected T cells and uninfected CD4+ T lymphocytes and prevented DC-SIGN-mediated HIV-1 transmission to CD4+ target T lymphocytes. However, unlike many other antiviral carbohydrate-binding agents (CBAs) described so far, NICTABA did not block HIV-1 capture to DC-SIGN+ cells and it did not interfere with the binding of the human monoclonal antibody 2G12 to gp120. SPR studies with HIV-1 envelope glycoproteins showed that the affinity of NICTABA for gp120 and gp41 was in the low nanomolar range. The specific binding of NICTABA to gp120 could be prevented in the presence of a GlcNAc trimer, but not in the presence of mannose trimers. NICTABA displayed no antiviral activity against non-enveloped viruses.
conclusionsSince CBAs possess a high genetic barrier for the development of viral resistance and NICTABA shows a broad antiviral activity profile, this CBA may qualify as a potential antiviral candidate with a pleiotropic mode of action aimed at targeting the entry of enveloped viruses.
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