ArticleMolecular pharmaceutics2012
The role of individual carbohydrate-binding sites in the function of the potent anti-HIV lectin griffithsin.
Article in Molecular pharmaceutics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 46 citations in OpenAlex.
- Tunable multivalent Fe(II)-based glycoassemblies as mimetics for native high-mannose glycans.bioRxiv : the preprint server for biology · 2025Article
- The Antiviral Activity of the Lectin Griffithsin against SARS-CoV-2 Is Enhanced by the Presence of Structural Proteins.Viruses · 2023Article
- Sustained Delivery of the Antiviral Protein Griffithsin and Its Adhesion to a Biological Surface by a Silk Fibroin Scaffold.Materials (Basel, Switzerland) · 2023Article
- Article
- Lectins and lectibodies: potential promising antiviral agents.Cellular & molecular biology letters · 2022Review
- Structure and Carbohydrate Recognition by the Nonmitogenic Lectin Horcolin.Biochemistry · 2022Article
- Algal and Cyanobacterial Lectins and Their Antimicrobial Properties.Marine drugs · 2021Review
- Efficacy of silk fibroin biomaterial vehicle for in vivo mucosal delivery of Griffithsin and protection against HIV and SHIV infection ex vivo.Journal of the International AIDS Society · 2020Article
- The Potential of Algal Biotechnology to Produce Antiviral Compounds and Biopharmaceuticals.Molecules (Basel, Switzerland) · 2020Review
- The High Content of Fructose in Human Semen Competitively Inhibits Broad and Potent Antivirals That Target High-Mannose Glycans.Journal of virology · 2020Article
- The Need for Ocular Protection for Health Care Workers During SARS-CoV-2 Outbreak and a Hypothesis for a Potential Personal Protective Equipment.Frontiers in public health · 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
- Novel Antiretroviral Structures from Marine Organisms.Molecules (Basel, Switzerland) · 2019Review
- Mannose-Specific Lectins from Marine Algae: Diverse Structural Scaffolds Associated to Common Virucidal and Anti-Cancer Properties.Marine drugs · 2019Review
- Structure-function characterization of an insecticidal protein GNIP1Aa, a member of an MACPF and β-tripod families.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Characterization of the hypersensitive response-like cell death phenomenon induced by targeting antiviral lectin griffithsin to the secretory pathway.Plant biotechnology journal · 2018Article
- Pharmaceutical Approaches to HIV Treatment and Prevention.Advanced therapeutics · 2018Article
- Surface-displayed porcine reproductive and respiratory syndrome virus from cell culture onto gram-positive enhancer matrix particles.Journal of industrial microbiology & biotechnology · 2018Article
- Chemical and Biophysical Approaches for Complete Characterization of Lectin-Carbohydrate Interactions.Methods in enzymology · 2018Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
Abstract
Griffithsin (GRFT) is a lectin that has been shown to inhibit HIV infection by binding to high mannose glycan structures on the surface of gp120, and it is among the most potent HIV entry inhibitors reported so far. However, important biochemical details on the antiviral mechanism of GRFT action remain unexplored. In order to understand the role of the three individual carbohydrate-binding sites (CBS) in GRFT, mutations were made at each site (D30A, D70A, and D112A), and the resulting mutants were investigated. NMR studies revealed that each GRFT variant was folded but showed significant peak movement on the carbohydrate-binding face of the protein. The wild-type and each point mutant protein appeared as tight dimers with a K(d) below 4.2 μM. Mutation of any individual CBS on GRFT reduced binding of the protein to mannose, and ELISA assays revealed a partial loss of ability of each GRFT point mutant to bind gp120, with a near-complete loss of binding by the triple mutant D30A/D70A/D112A GRFT. A more quantitative surface plasmon resonance (SPR) examination showed a rather small loss of binding to gp120 for the individual GRFT point mutants (K(D): 123 to 245 pM range versus 73 pM for wild-type GRFT), but dramatic loss of the triple mutant to bind gp120 derived from R5 and X4 strains (K(D) > 12 nM). In contrast to the 2- to 3-fold loss of binding to gp120, the single CBS point mutants of GRFT were significantly less able to inhibit viral infection, exhibiting a 26- to 1900-fold loss of potency, while the triple mutant was at least 875-fold less effective against HIV-1 infection. The disparity between HIV-1 gp120 binding ability and HIV inhibitory potency for these GRFT variants indicates that gp120 binding and virus neutralization do not necessarily correlate, and suggests a mechanism that is not based on simple gp120 binding.
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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.