ArticlePloS one2012
Sub-domains of ricin's B subunit as targets of toxin neutralizing and non-neutralizing monoclonal antibodies.
Article in PloS one, 2012. 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.
- Article
- Inflammatory Profiles Induced by Intranasal Immunization with Ricin Toxin-immune Complexes.ImmunoHorizons · 2024Article
- Article
- An intranasally administered monoclonal antibody cocktail abrogates ricin toxin-induced pulmonary tissue damage and inflammation.Human vaccines & immunotherapeutics · 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
- Review
- Evidence of Clostridium perfringens epsilon toxin associated with multiple sclerosis.Multiple sclerosis (Houndmills, Basingstoke, England) · 2019Article
- Article
- Fine-Specificity Epitope Analysis Identifies Contact Points on Ricin Toxin Recognized by Protective Monoclonal Antibodies.ImmunoHorizons · 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
- A Supercluster of Neutralizing Epitopes at the Interface of Ricin's Enzymatic (RTA) and Binding (RTB) Subunits.Toxins · 2017Article
- Spatial location of neutralizing and non-neutralizing B cell epitopes on domain 1 of ricin toxin's binding subunit.PloS one · 2017Article
- Progress and challenges associated with the development of ricin toxin subunit vaccines.Expert review of vaccines · 2016Review
- Studies of a murine monoclonal antibody directed against DARC: reappraisal of its specificity.PloS one · 2015Article
- Chimeric plantibody passively protects mice against aerosolized ricin challenge.Clinical and vaccine immunology : CVI · 2014Article
- Article
- Differential neutralizing activities of a single domain camelid antibody (VHH) specific for ricin toxin's binding subunit (RTB).PloS one · 2014Article
- Stepwise engineering of heterodimeric single domain camelid VHH antibodies that passively protect mice from ricin toxin.The Journal of biological chemistry · 2013Article
- Neutralizing monoclonal antibodies against ricin's enzymatic subunit interfere with protein disulfide isomerase-mediated reduction of ricin holotoxin in vitro.Journal of immunological methods · 2013Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The B subunit (RTB) of ricin toxin is a galactose (Gal)-/N-acetylgalactosamine (GalNac)-specific lectin that mediates attachment, entry, and intracellular trafficking of ricin in host cells. Structurally, RTB consists of two globular domains with identical folding topologies. Domains 1 and 2 are each comprised of three homologous sub-domains (α, β, γ) that likely arose by gene duplication from a primordial carbohydrate recognition domain (CRD), although only sub-domains 1α and 2γ retain functional lectin activity. As part of our ongoing effort to generate a comprehensive B cell epitope map of ricin, we report the characterization of three new RTB-specific monoclonal antibodies (mAbs). All three mAbs, JB4, B/J F9 and C/M A2, were initially identified based on their abilities to neutralize ricin in a Vero cell cytotoxicity assay and to partially (or completely) block ricin attachment to cell surfaces. However, only JB4 proved capable of neutralizing ricin in a macrophage apoptosis assay and in imparting passive immunity to mice in a model of systemic intoxication. Using a combination of techniques, including competitive ELISAs, pepscan analysis, differential reactivity by Western blot, as well as affinity enrichment of phage displayed peptides, we tentatively localized the epitopes recognized by the non-neutralizing mAbs B/J F9 and C/M A2 to sub-domains 2α and 2β, respectively. Furthermore, we propose that the epitope recognized by JB4 is within sub-domain 2γ, adjacent to RTB's high affinity Gal/GalNAc CRD. These data suggest that recognition of RTB's sub-domains 1α and 2γ are critical determinants of antibody neutralizing activity and protective immunity to ricin.
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