ArticleThe Journal of biological chemistry2015
Mechanisms of Ricin Toxin Neutralization Revealed through Engineered Homodimeric and Heterodimeric Camelid Antibodies.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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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.
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Who cites it
27 citing papers in PubMed, 37 citations in OpenAlex.
- Antibody Screening and Binding Prediction Analysis Targeting Stx2.Antibodies (Basel, Switzerland) · 2026Article
- Article
- A Biparatopic Intrabody Renders Vero Cells Impervious to Ricin Intoxication.bioRxiv : the preprint server for biology · 2024Article
- Single domain antibodies from camelids in the treatment of microbial infections.Frontiers in immunology · 2024Review
- Article
- Structure-guided design of a potentFrontiers in microbiology · 2023Article
- A novel single-domain antibody multimer that potently neutralizes tetanus neurotoxin.Vaccine: X · 2021Article
- An Inside Job: Applications of Intracellular Single Domain Antibodies.Biomolecules · 2020Review
- An intranasally administered monoclonal antibody cocktail abrogates ricin toxin-induced pulmonary tissue damage and inflammation.Human vaccines & immunotherapeutics · 2020Article
- Structural Insights into Rational Design of Single-Domain Antibody-Based Antitoxins against Botulinum Neurotoxins.Cell reports · 2020Article
- High Expression Achievement of Active and Robust Anti-β2 microglobulin Nanobodies viaMolecules (Basel, Switzerland) · 2019Article
- mRNA: A Novel Avenue to Antibody Therapy?Molecular therapy : the journal of the American Society of Gene Therapy · 2019Review
- Article
- 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
- Article
- 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
- Article
- Genetically engineered red cells expressing single domain camelid antibodies confer long-term protection against botulinum neurotoxin.Nature communications · 2017Article
- Pairing Alpaca and Llama-Derived Single Domain Antibodies to Enhance Immunoassays for Ricin.Antibodies (Basel, Switzerland) · 2017Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Novel antibody constructs consisting of two or more different camelid heavy-chain only antibodies (VHHs) joined via peptide linkers have proven to have potent toxin-neutralizing activity in vivo against Shiga, botulinum, Clostridium difficile, anthrax, and ricin toxins. However, the mechanisms by which these so-called bispecific VHH heterodimers promote toxin neutralization remain poorly understood. In the current study we produced a new collection of ricin-specific VHH heterodimers, as well as VHH homodimers, and characterized them for their ability neutralize ricin in vitro and in vivo. We demonstrate that the VHH heterodimers, but not homodimers were able to completely protect mice against ricin challenge, even though the two classes of antibodies (heterodimers and homodimers) had virtually identical affinities for ricin holotoxin and similar IC50 values in a Vero cell cytotoxicity assay. The VHH heterodimers did differ from the homodimers in their ability to promote toxin aggregation in solution, as revealed through analytical ultracentrifugation. Moreover, the VHH heterodimers that were most effective at promoting ricin aggregation in solution were also the most effective at blocking ricin attachment to cell surfaces. Collectively, these data suggest that heterodimeric VHH-based neutralizing agents may function through the formation of antibody-toxin complexes that are impaired in their ability to access host cell receptors.
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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.