ArticleImmunology letters
Localization of non-linear neutralizing B cell epitopes on ricin toxin's enzymatic subunit (RTA).
Article in Immunology letters. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 34 citations in OpenAlex.
- Inflammatory Profiles Induced by Intranasal Immunization with Ricin Toxin-immune Complexes.ImmunoHorizons · 2024Article
- 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
- Article
- Fine-Specificity Epitope Analysis Identifies Contact Points on Ricin Toxin Recognized by Protective Monoclonal Antibodies.ImmunoHorizons · 2018Article
- High-Definition Mapping of Four Spatially Distinct Neutralizing Epitope Clusters on RiVax, a Candidate Ricin Toxin Subunit Vaccine.Clinical and vaccine immunology : CVI · 2017Article
- 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
- Protein Structure Facilitates High-Resolution Immunological Mapping.Clinical and vaccine immunology : CVI · 2017Review
- A Supercluster of Neutralizing Epitopes at the Interface of Ricin's Enzymatic (RTA) and Binding (RTB) Subunits.Toxins · 2017Article
- Using homology modeling to interrogate binding affinity in neutralization of ricin toxin by a family of single domain antibodies.Proteins · 2017Article
- Structural Analysis of Single Domain Antibodies Bound to a Second Neutralizing Hot Spot on Ricin Toxin's Enzymatic Subunit.The Journal of biological chemistry · 2017Article
- Spatial location of neutralizing and non-neutralizing B cell epitopes on domain 1 of ricin toxin's binding subunit.PloS one · 2017Article
- Humanized Monoclonal Antibody That Passively Protects Mice against Systemic and Intranasal Ricin Toxin Challenge.Clinical and vaccine immunology : CVI · 2016Article
- Progress and challenges associated with the development of ricin toxin subunit vaccines.Expert review of vaccines · 2016Review
- Structural analysis of nested neutralizing and non-neutralizing B cell epitopes on ricin toxin's enzymatic subunit.Proteins · 2016Article
- Recent advances in the development of vaccines against ricin.Human vaccines & immunotherapeutics · 2016Article
- Novel Ricin Subunit Antigens With Enhanced Capacity to Elicit Toxin-Neutralizing Antibody Responses in Mice.Journal of pharmaceutical sciences · 2016Article
- Neutralizing Monoclonal Antibodies against Disparate Epitopes on Ricin Toxin's Enzymatic Subunit Interfere with Intracellular Toxin Transport.Scientific reports · 2016Article
- Comparative Adjuvant Effects of Type II Heat-Labile Enterotoxins in Combination with Two Different Candidate Ricin Toxin Vaccine Antigens.Clinical and vaccine immunology : CVI · 2015Article
- Thermostable ricin vaccine protects rhesus macaques against aerosolized ricin: Epitope-specific neutralizing antibodies correlate with protection.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Efforts to develop a vaccine for ricin toxin are focused on identifying highly immunogenic, safe, and thermostable recombinant derivatives of ricin's enzymatic A subunit (RTA). As a means to guide vaccine design, we have embarked on an effort to generate a comprehensive neutralizing and non-neutralizing B cell epitope map of RTA. In a series of previous studies, we identified three spatially distinct linear (continuous), neutralizing epitopes on RTA, as defined by monoclonal antibodies (mAbs) PB10 (and R70), SyH7, and GD12. In this report we now describe a new collection of 19 toxin-neutralizing mAbs that bind non-linear epitopes on RTA. The most potent toxin-neutralizing mAbs in this new collection, namely WECB2, TB12, PA1, PH12 and IB2 each had nanamolar (or sub-nanomolar) affinities for ricin and were each capable of passively protecting mice against a 5-10xLD50 toxin challenge. Competitive binding assays by surface plasmon resonance revealed that WECB2 binds an epitope that overlaps with PB10 and R70; TB12, PA1, PH12 recognize epitope(s) close to or overlapping with SyH7's epitope; and GD12 and IB2 recognize epitopes that are spatially distinct from all other toxin-neutralizing mAbs. We estimate that we have now accounted for ∼75% of the predicted epitopes on the surface of RTA and that toxin-neutralizing mAbs are directed against a very limited number of these epitopes. Having this information provides a framework for further refinement of RTA mutagenesis and vaccine design.
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