ArticleJournal of molecular biology2014
Crystal structures of ricin toxin's enzymatic subunit (RTA) in complex with neutralizing and non-neutralizing single-chain antibodies.
Article in Journal of molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
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Who cites it
31 citing papers in PubMed, 43 citations in OpenAlex.
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- Applications of nanobodies in plant science and biotechnology.Plant molecular biology · 2021Review
- Intracellular Neutralization of Ricin Toxin by Single-domain Antibodies Targeting the Active Site.Journal of molecular biology · 2020Article
- Sensitivity of Kupffer cells and liver sinusoidal endothelial cells to ricin toxin and ricin toxin-Ab complexes.Journal of leukocyte biology · 2019Article
- A Collection of Single-Domain Antibodies that Crowd Ricin Toxin's Active Site.Antibodies (Basel, Switzerland) · 2018Article
- Enzymatic Transition States and Drug Design.Chemical reviews · 2018Review
- Fine-Specificity Epitope Analysis Identifies Contact Points on Ricin Toxin Recognized by Protective Monoclonal Antibodies.ImmunoHorizons · 2018Article
- Contribution of an unusual CDR2 element of a single domain antibody in ricin toxin binding affinity and neutralizing activity.Protein engineering, design & selection : PEDS · 2018Article
- In planta expression of nanobody-based designer chicken antibodies targeting Campylobacter.PloS one · 2018Article
- Protein Structure Facilitates High-Resolution Immunological Mapping.Clinical and vaccine immunology : CVI · 2017Review
- High-Resolution Epitope Positioning of a Large Collection of Neutralizing and Nonneutralizing Single-Domain Antibodies on the Enzymatic and Binding Subunits of Ricin Toxin.Clinical and vaccine immunology : CVI · 2017Article
- High-Definition Mapping of Four Spatially Distinct Neutralizing Epitope Clusters on RiVax, a Candidate Ricin Toxin Subunit Vaccine.Clinical and vaccine immunology : CVI · 2017Article
- Using homology modeling to interrogate binding affinity in neutralization of ricin toxin by a family of single domain antibodies.Proteins · 2017Article
- Selective cytotoxicity of a novel immunotoxin based on pulchellin A chain for cells expressing HIV envelope.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 1 country.
Funding
Abstract
Ricin is a select agent toxin and a member of the RNA N-glycosidase family of medically important plant and bacterial ribosome-inactivating proteins. In this study, we determined X-ray crystal structures of the enzymatic subunit of ricin (RTA) in complex with the antigen binding domains (VHH) of five unique single-chain monoclonal antibodies that differ in their respective toxin-neutralizing activities. None of the VHHs made direct contact with residues involved in RTA's RNA N-glycosidase activity or induced notable allosteric changes in the toxin's subunit. Rather, the five VHHs had overlapping structural epitopes on the surface of the toxin and differed in the degree to which they made contact with prominent structural elements in two folding domains of the RTA. In general, RTA interactions were influenced most by the VHH CDR3 (CDR, complementarity-determining region) elements, with the most potent neutralizing antibody having the shortest and most conformationally constrained CDR3. These structures provide unique insights into the mechanisms underlying toxin neutralization and provide critically important information required for the rational design of ricin toxin subunit vaccines.
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