Purification, characterization and toxicity profile of ricin isoforms from castor beans

Sehgal, Payal; Khan, Mohsin; Kumar, Om; Vijayaraghavan, R.

doi:10.1016/j.fct.2010.08.015

Cited by 37 publications

(23 citation statements)

References 28 publications

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“…Abr4 and Abr6, which displayed cross-reactivity with ricin B-chain, did not bind abrax but bound commercial abrin, Abrus agglutinin, and all three abrin fractions with greatest affinity for abrin fraction I (data not shown for fractions II and III). Although the three abrin fractions had been reported to be immunologically indistinguishable [12], there are reports of anti-ricin antibodies that react with only one of the analogous 3 ricin fractions [42]. Thus, the preferential recognition of fraction I by Abr4 and Abr6 may represent inclusion in the epitope of sequence differences between the fractions that were not observed previously.…”

Section: Resultsmentioning

confidence: 95%

Llama-Derived Single Domain Antibodies Specific for Abrus Agglutinin

Goldman

Anderson

Zabetakis

et al. 2011

Toxins

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Llama derived single domain antibodies (sdAb), the recombinantly expressed variable heavy domains from the unique heavy-chain only antibodies of camelids, were isolated from a library derived from llamas immunized with a commercial abrin toxoid preparation. Abrin is a potent toxin similar to ricin in structure, sequence and mechanism of action. The selected sdAb were evaluated for their ability to bind to commercial abrin as well as abrax (a recombinant abrin A-chain), purified abrin fractions, Abrus agglutinin (a protein related to abrin but with lower toxicity), ricin, and unrelated proteins. Isolated sdAb were also evaluated for their ability to refold after heat denaturation and ability to be used in sandwich assays as both capture and reporter elements. The best binders were specific for the Abrus agglutinin, showing minimal binding to purified abrin fractions or unrelated proteins. These binders had sub nM affinities and regained most of their secondary structure after heating to 95 °C. They functioned well in sandwich assays. Through gel analysis and the behavior of anti-abrin monoclonal antibodies, we determined that the commercial toxoid preparation used for the original immunizations contained a high percentage of Abrus agglutinin, explaining the selection of Abrus agglutinin binders. Used in conjunction with anti-abrin monoclonal and polyclonal antibodies, these reagents can fill a role to discriminate between the highly toxic abrin and the related, but much less toxic, Abrus agglutinin and distinguish between different crude preparations.

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Section: Resultsmentioning

confidence: 95%

Llama-Derived Single Domain Antibodies Specific for Abrus Agglutinin

Goldman

Anderson

Zabetakis

et al. 2011

Toxins

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“…The full-length proteins of the ricin gene family have been shown to inhibit protein synthesis similar to ricin itself [121]. Additional heterogeneity of ricin is based on different glycosylation patterns [118], and variable toxicities of ricin isoforms have been correlated with different glycosylation levels [123,124]. …”

Section: Toxicity Of Ricin and R Communis Agglutininmentioning

confidence: 99%

Ricinus communis Intoxications in Human and Veterinary Medicine—A Summary of Real Cases

Worbs

Köhler

Pauly

et al. 2011

Toxins

186

177

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Accidental and intended Ricinus communis intoxications in humans and animals have been known for centuries but the causative agent remained elusive until 1888 when Stillmark attributed the toxicity to the lectin ricin. Ricinus communis is grown worldwide on an industrial scale for the production of castor oil. As by-product in castor oil production ricin is mass produced above 1 million tons per year. On the basis of its availability, toxicity, ease of preparation and the current lack of medical countermeasures, ricin has gained attention as potential biological warfare agent. The seeds also contain the less toxic, but highly homologous Ricinus communis agglutinin and the alkaloid ricinine, and especially the latter can be used to track intoxications. After oil extraction and detoxification, the defatted press cake is used as organic fertilizer and as low-value feed. In this context there have been sporadic reports from different countries describing animal intoxications after uptake of obviously insufficiently detoxified fertilizer. Observations in Germany over several years, however, have led us to speculate that the detoxification process is not always performed thoroughly and controlled, calling for international regulations which clearly state a ricin threshold in fertilizer. In this review we summarize knowledge on intended and unintended poisoning with ricin or castor seeds both in humans and animals, with a particular emphasis on intoxications due to improperly detoxified castor bean meal and forensic analysis.

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“…Ricin is a protoplasmic toxin that can cause aggregation and dissolution of red blood cells in addition to liver and kidney damage, hemorrhage, and necrosis [2]. Indeed, ricin has been reported to be a particularly potent agent of hemolysis [8]. In our cohort of children, both hemoglobin concentrations and red blood cell counts were increased after PE, hemoglobin concentrations significantly so.…”

Section: Discussionmentioning

confidence: 70%

Early plasma exchange for treating ricin toxicity in children after castor bean ingestion

Wang

Nie

Chen

et al. 2014

J of Clinical Apheresis

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Plasma exchange (PE) for the treatment of ricin toxicity has not been previously reported. Here we describe the use of PE to treat children who experienced ricin toxicity after ingesting castor beans. Seven children (median age: 8.1 years) who consumed castor beans (median: 5 beans) were treated with PE. All had bradycardia and sinus arrhythmia, and most had experienced episodes of vomiting and/or diarrhea. PE settings were blood flow, 50-80 mL/min; PE rate, 600-800 mL/h; volume of exchange, 1440-1950 mL. Median time from ingestion to PE was 73 h. All clinical symptoms disappeared and vital signs rapidly returned to normal after PE; no severe organ dysfunction occurred. All children were discharged and recovered uneventfully. Concentrations of all serum biochemical parameters significantly decreased immediately after PE. Some, but not all, of these parameters were also significantly decreased at 48 and 72 h after PE compared with before PE. Our findings suggest that PE can be an effective early intervention in the treatment of ricin toxicity due to castor bean ingestion.

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Purification, characterization and toxicity profile of ricin isoforms from castor beans

Cited by 37 publications

References 28 publications

Llama-Derived Single Domain Antibodies Specific for Abrus Agglutinin

Llama-Derived Single Domain Antibodies Specific for Abrus Agglutinin

Ricinus communis Intoxications in Human and Veterinary Medicine—A Summary of Real Cases

Early plasma exchange for treating ricin toxicity in children after castor bean ingestion

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