ArticleThe Journal of biological chemistry2011
Identification of a novel functional domain of ricin responsible for its potent toxicity.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 37 citations in OpenAlex.
- Article
- 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
- Review
- 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
- High-Definition Mapping of Four Spatially Distinct Neutralizing Epitope Clusters on RiVax, a Candidate Ricin Toxin Subunit Vaccine.Clinical and vaccine immunology : CVI · 2017Article
- Using homology modeling to interrogate binding affinity in neutralization of ricin toxin by a family of single domain antibodies.Proteins · 2017Article
- Unraveling the Roots of Selectivity of Peptide Affinity Reagents for Structurally Similar Ribosomal Inactivating Protein Derivatives.Molecules (Basel, Switzerland) · 2016Article
- Toxicity of ricin A chain is reduced in mammalian cells by inhibiting its interaction with the ribosome.Toxicology and applied pharmacology · 2016Article
- Structural analysis of nested neutralizing and non-neutralizing B cell epitopes on ricin toxin's enzymatic subunit.Proteins · 2016Article
- Neutralizing Monoclonal Antibodies against Disparate Epitopes on Ricin Toxin's Enzymatic Subunit Interfere with Intracellular Toxin Transport.Scientific reports · 2016Article
- Potential therapeutic applications of plant toxin-ricin in cancer: challenges and advances.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2015Review
- Characterization and epitope mapping of the polyclonal antibody repertoire elicited by ricin holotoxin-based vaccination.Clinical and vaccine immunology : CVI · 2014Article
- Crystal structures of ricin toxin's enzymatic subunit (RTA) in complex with neutralizing and non-neutralizing single-chain antibodies.Journal of molecular biology · 2014Article
- Article
- Arginine residues on the opposite side of the active site stimulate the catalysis of ribosome depurination by ricin A chain by interacting with the P-protein stalk.The Journal of biological chemistry · 2013Article
- Structural insights into the neutralization mechanism of monoclonal antibody 6C2 against ricin.The Journal of biological chemistry · 2013Article
- A relatively low level of ribosome depurination by mutant forms of ricin toxin A chain can trigger protein synthesis inhibition, cell signaling and apoptosis in mammalian cells.The international journal of biochemistry & cell biology · 2012Article
- Resolution of two overlapping neutralizing B cell epitopes within a solvent exposed, immunodominant α-helix in ricin toxin's enzymatic subunit.Toxicon : official journal of the International Society on Toxinology · 2012Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ribosome-inactivating proteins (RIPs) are toxic N-glycosidases that depurinate the universally conserved α-sarcin loop of large rRNAs. They have received attention in biological and biomedical research because of their unique biological activities toward animals and human cells as cell-killing agents. A better understanding of the depurination mechanism of RIPs could allow us to develop potent neutralizing antibodies and to design efficient immunotoxins for clinical use. Among these RIPs, ricin exhibited remarkable efficacy in depurination activity and highly conserved tertiary structure with other RIPs. It can be considered as a prototype to investigate the depurination mechanism of RIPs. In the present study, we successfully identified a novel functional domain responsible for controlling the depurination activity of ricin, which is located far from the enzymatic active site reported previously. Our study indicated that ricin A-chain mAbs binding to this domain (an α-helix comprising the residues 99-106) exhibited an unusual potent neutralizing ability against ricin in vivo. To further investigate the potential role of the α-helix in regulating the catalytic activity of ricin, ricin A-chain variants with different flexibility of the α-helix were rationally designed. Our data clearly demonstrated that the flexibility of the α-helix is responsible for controlling the depurination activity of ricin and determining the extent of protein synthesis inhibition, suggesting that the conserved α-helix might be considered as a potential target for the prevention and treatment of RIP poisoning.
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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.