ArticleVaccine2010
Folding domains within the ricin toxin A subunit as targets of protective antibodies.
Article in Vaccine, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
56 citing papers in PubMed, 77 citations in OpenAlex.
- Article
- Inflammatory Profiles Induced by Intranasal Immunization with Ricin Toxin-immune Complexes.ImmunoHorizons · 2024Article
- Targeting the Inside of Cells with Biologicals: Toxin Routes in a Therapeutic Context.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2023Review
- Article
- Sensitivity of Kupffer cells and liver sinusoidal endothelial cells to ricin toxin and ricin toxin-Ab complexes.Journal of leukocyte biology · 2019Article
- Leucine 232 and hydrophobic residues at the ribosomal P stalk binding site are critical for biological activity of ricin.Bioscience reports · 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
- 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
- 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
- Evaluation of lumazine synthase from Bacillus anthracis as a presentation platform for polyvalent antigen display.Protein science : a publication of the Protein Society · 2017Article
- Ricin uses arginine 235 as an anchor residue to bind to P-proteins of the ribosomal stalk.Scientific reports · 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
- Progress and challenges associated with the development of ricin toxin subunit vaccines.Expert review of vaccines · 2016Review
- Humanized Monoclonal Antibody That Passively Protects Mice against Systemic and Intranasal Ricin Toxin Challenge.Clinical and vaccine immunology : CVI · 2016Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Efforts to develop an effective vaccine against ricin are focused on the engineering of attenuated and stable recombinant forms of the toxin's enzymatic A subunit (RTA). While several candidate antigens are in development, vaccine design and efficacy studies are being undertaken in the absence of a fundamental understanding of those regions of RTA that are critical in eliciting protective immunity. In this present study, we produced and characterized a collection of monoclonal antibodies (MAbs) directed against five distinct immunodominant regions on RTA, and used these MAbs to identify several key neutralizing epitopes on the toxin. Protective MAbs were directed against α-helices located in RTA folding domains 1 and 2, whereas non-neutralizing antibodies recognized random coils and loops that were primarily confined to folding domain 3. These data offer insights into the immunodominant and structural determinants on RTA that give rise to protective immunity, and for the first time provide an immunological rationale for ricin vaccine design.
Indexed as
Identifiers
What OpenQuestion holds
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.