ArticleRetrovirology2011
Differences in the mannose oligomer specificities of the closely related lectins from Galanthus nivalis and Zea mays strongly determine their eventual anti-HIV activity.
Article in Retrovirology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 26 citations in OpenAlex.
- A Useful Guide to Lectin Binding: Machine-Learning Directed Annotation of 57 Unique Lectin Specificities.ACS chemical biology · 2022Article
- Legume Lectins with Different Specificities as Potential Glycan Probes for Pathogenic Enveloped Viruses.Cells · 2022Review
- 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
- Overview of the Structure⁻Function Relationships of Mannose-Specific Lectins from Plants, Algae and Fungi.International journal of molecular sciences · 2019Review
- Lectin microarray and mass spectrometric analysis of hepatitis C proteins reveals N-linked glycosylation.Medicine · 2018Article
- Inhibition of H9N2 Virus Invasion into Dendritic Cells by the S-Layer Protein fromFrontiers in cellular and infection microbiology · 2016Article
- HIV-1 gp120 as a therapeutic target: navigating a moving labyrinth.Expert opinion on therapeutic targets · 2015Review
- Targeting strategies for delivery of anti-HIV drugs.Journal of controlled release : official journal of the Controlled Release Society · 2014Review
- Bitter-sweet symphony: glycan-lectin interactions in virus biology.FEMS microbiology reviews · 2014Review
- 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.Molecular pharmaceutics · 2013Article
- The griffithsin dimer is required for high-potency inhibition of HIV-1: evidence for manipulation of the structure of gp120 as part of the griffithsin dimer mechanism.Antimicrobial agents and chemotherapy · 2013Article
- Structural determinants for activity and specificity of the bacterial toxin LlpA.PLoS pathogens · 2013Article
- Article
- The role of individual carbohydrate-binding sites in the function of the potent anti-HIV lectin griffithsin.Molecular pharmaceutics · 2012Article
- S-layer proteins of Lactobacillus acidophilus inhibits JUNV infection.Biochemical and biophysical research communications · 2012Article
- Photogenerated lectin sensors produced by thiol-ene/yne photo-click chemistry in aqueous solution.Biosensors & bioelectronics · 2012Article
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundIn a recent report, the carbohydrate-binding specificities of the plant lectins Galanthus nivalis (GNA) and the closely related lectin from Zea mays (GNAmaize) were determined by glycan array analysis and indicated that GNAmaize recognizes complex-type N-glycans whereas GNA has specificity towards high-mannose-type glycans. Both lectins are tetrameric proteins sharing 64% sequence similarity.
resultsGNAmaize appeared to be ~20- to 100-fold less inhibitory than GNA against HIV infection, syncytia formation between persistently HIV-1-infected HuT-78 cells and uninfected CD4+ T-lymphocyte SupT1 cells, HIV-1 capture by DC-SIGN and subsequent transmission of DC-SIGN-captured virions to uninfected CD4+ T-lymphocyte cells. In contrast to GNA, which preferentially selects for virus strains with deleted high-mannose-type glycans on gp120, prolonged exposure of HIV-1 to dose-escalating concentrations of GNAmaize selected for mutant virus strains in which one complex-type glycan of gp120 was deleted. Surface Plasmon Resonance (SPR) analysis revealed that GNA and GNAmaize interact with HIV IIIB gp120 with affinity constants (KD) of 0.33 nM and 34 nM, respectively. Whereas immobilized GNA specifically binds mannose oligomers, GNAmaize selectively binds complex-type GlcNAcβ1,2Man oligomers. Also, epitope mapping experiments revealed that GNA and the mannose-specific mAb 2G12 can independently bind from GNAmaize to gp120, whereas GNAmaize cannot efficiently bind to gp120 that contained prebound PHA-E (GlcNAcβ1,2man specific) or SNA (NeuAcα2,6X specific).
conclusionThe markedly reduced anti-HIV activity of GNAmaize compared to GNA can be explained by the profound shift in glycan recognition and the disappearance of carbohydrate-binding sites in GNAmaize that have high affinity for mannose oligomers. These findings underscore the need for mannose oligomer recognition of therapeutics to be endowed with anti-HIV activity and that mannose, but not complex-type glycan binding of chemotherapeutics to gp120, may result in a pronounced neutralizing activity against the virus.
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