ArticleClinical and vaccine immunology : CVI2017
High-Definition Mapping of Four Spatially Distinct Neutralizing Epitope Clusters on RiVax, a Candidate Ricin Toxin Subunit Vaccine.
Article in Clinical and vaccine immunology : CVI, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 42 citations in OpenAlex.
- Ricin as a Biothreat Agent: From Molecular Mechanisms to Clinical Toxicology, Forensic Aspects, and Risk Mitigation.BioMed research international · 2026Review
- A clinical approach to an unidentified aerosolized bioterrorism agent: a narrative review for emergency providers.Clinical and experimental emergency medicine · 2023Article
- Hydrogen Deuterium Exchange and other Mass Spectrometry-based Approaches for Epitope Mapping.Frontiers in analytical science · 2023Article
- Serum antibody profiling identifies vaccine-induced correlates of protection against aerosolized ricin toxin in rhesus macaques.NPJ vaccines · 2022Article
- Durable Immunity to Ricin Toxin Elicited by a Thermostable, Lyophilized Subunit Vaccine.mSphere · 2021Article
- Mechanism of Thimerosal-Induced Structural Destabilization of a Recombinant Rotavirus P[4] Protein Antigen Formulated as a Multi-Dose Vaccine.Journal of pharmaceutical sciences · 2021Article
- An intranasally administered monoclonal antibody cocktail abrogates ricin toxin-induced pulmonary tissue damage and inflammation.Human vaccines & immunotherapeutics · 2020Article
- Article
- Intracellular Neutralization of Ricin Toxin by Single-domain Antibodies Targeting the Active Site.Journal of molecular biology · 2020Article
- Passive immunization with an extended half-life monoclonal antibody protects Rhesus macaques against aerosolized ricin toxin.NPJ vaccines · 2020Article
- Sites of vulnerability on ricin B chain revealed through epitope mapping of toxin-neutralizing monoclonal antibodies.PloS one · 2020Article
- Sensitivity of Kupffer cells and liver sinusoidal endothelial cells to ricin toxin and ricin toxin-Ab complexes.Journal of leukocyte biology · 2019Article
- Ricin and Ricinus communis in pharmacology and toxicology-from ancient use and "Papyrus Ebers" to modern perspectives and "poisonous plant of the year 2018".Naunyn-Schmiedeberg's archives of pharmacology · 2019Review
- A Collection of Single-Domain Antibodies that Crowd Ricin Toxin's Active Site.Antibodies (Basel, Switzerland) · 2018Article
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- Article
- 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
- Investigating the dynamics and polyanion binding sites of fibroblast growth factor-1 using hydrogen-deuterium exchange mass spectrometry.Protein science : a publication of the Protein Society · 2018Article
- 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
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
Abstract
RiVax is a promising recombinant ricin toxin A subunit (RTA) vaccine antigen that has been shown to be safe and immunogenic in humans and effective at protecting rhesus macaques against lethal-dose aerosolized toxin exposure. We previously used a panel of RTA-specific monoclonal antibodies (MAbs) to demonstrate, by competition enzyme-linked immunosorbent assay (ELISA), that RiVax elicits similar serum antibody profiles in humans and macaques. However, the MAb binding sites on RiVax have yet to be defined. In this study, we employed hydrogen exchange-mass spectrometry (HX-MS) to localize the epitopes on RiVax recognized by nine toxin-neutralizing MAbs and one nonneutralizing MAb. Based on strong protection from hydrogen exchange, the nine MAbs grouped into four spatially distinct epitope clusters (namely, clusters I to IV). Cluster I MAbs protected RiVax's α-helix B (residues 94 to 107), a protruding immunodominant secondary structure element known to be a target of potent toxin-neutralizing antibodies. Cluster II consisted of two subclusters located on the "back side" (relative to the active site pocket) of RiVax. One subcluster involved α-helix A (residues 14 to 24) and α-helices F-G (residues 184 to 207); the other encompassed β-strand d (residues 62 to 69) and parts of α-helices D-E (154 to 164) and the intervening loop. Cluster III involved α-helices C and G on the front side of RiVax, while cluster IV formed a sash from the front to back of RiVax, spanning strands b, c, and d (residues 35 to 59). Having a high-resolution B cell epitope map of RiVax will enable the development and optimization of competitive serum profiling assays to examine vaccine-induced antibody responses across species.
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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.