Highly toxic type Ⅱ ribosome-inactivating proteins ricin and abrin and their detection methods: a review

Liang, Long-Hui; Xia, Junmei; Liu, Chang-Cai; Liu, Shilei

doi:10.3724/sp.j.1123.2020.10001

Cited by 3 publications

(4 citation statements)

References 63 publications

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“…The A-chain has N -glycosidase activity that leads to irreversible depurination of adenine from 28S ribosomal RNA and thus terminates protein synthesis. This synergism of the A and B chains inactivates the ribosome and leads to high cytotoxicity after oral administration or inhalation (Liang et al 2021 ).…”

Section: Mode Of Toxic Actionmentioning

confidence: 99%

“…Owing to its easy availability and high toxicity, Ricinus communis L. was awarded the dubious title “poisonous plant of the year 2018” in Germany (Franke et al 2019 ). The toxicity of ricin is estimated to be approximately 380-fold higher than that of the nerve agent VX (Liang et al 2021 ). A number of recent reviews cover different aspects of ricin, its preparation from castor seeds and its potential use as a biological weapon (Griffiths 2011 ; Olsnes and Kozlov 2001 ; Poelchen and Wirkner 2003 ; Spivak and Hendrickson 2005 ; Polito et al 2019 ).…”

mentioning

confidence: 99%

“…A number of recent reviews cover different aspects of ricin, its preparation from castor seeds and its potential use as a biological weapon (Griffiths 2011 ; Olsnes and Kozlov 2001 ; Poelchen and Wirkner 2003 ; Spivak and Hendrickson 2005 ; Polito et al 2019 ). Owing to its ease of preparation, wide availability, and potential use as a bioterrorism agent, ricin is listed as a prohibited substance under schedule 1A of the Chemical Weapons Convention (CWC, Liang et al 2021 ). Ricin research is now focused on the following aspects.…”

mentioning

confidence: 99%

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Ricin: an ancient toxicant, but still an evergreen

Bolt

Hengstler

2023

Arch Toxicol

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Section: Mode Of Toxic Actionmentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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Ricin: an ancient toxicant, but still an evergreen

Bolt

Hengstler

2023

Arch Toxicol

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“…These two chains are connected by a single interchain disulfide bond [ 7 ]. Pokeweed antiviral protein (PAP) and trichosanthin (TCS) belong to the subfamily of type I RIP, but abrin and RT are typical type II RIPs [ 8 ]. Ricin has attracted interest mainly due to its cytotoxicity to mammalian cells and potential applications as biological weapons, which makes it to be considered a moderate threat by the US Center for Disease Control and Prevention (CDC) [ 6 ]; moreover, ricin also can be used as a research tool to study its intracellular transport and therapeutic effect on tumors [ 9 , 10 ] and AIDS (acquired immune deficiency syndrome) [ 10 , 11 ].…”

Section: Introductionmentioning

confidence: 99%

Integrated Transcriptome and Proteome Analysis Provides Insight into the Ribosome Inactivating Proteins in Plukenetia volubilis Seeds

Yan

Shang

et al. 2022

IJMS

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Plukenetia volubilis is a highly promising plant with high nutritional and economic values. In our previous studies, the expression levels of ricin encoded transcripts were the highest in the maturation stage of P. volubilis seeds. The present study investigated the transcriptome and proteome profiles of seeds at two developmental stages (Pv-1 and Pv-2) using RNA-Seq and iTRAQ technologies. A total of 53,224 unigenes and 6026 proteins were identified, with functional enrichment analyses, including GO, KEGG, and KOG annotations. At two development stages of P. volubilis seeds, 8815 unique differentially expressed genes (DEGs) and 4983 unique differentially abundant proteins (DAPs) were identified. Omics-based association analysis showed that ribosome-inactivating protein (RIP) transcripts had the highest expression and abundance levels in Pv-2, and those DEGs/DAPs of RIPs in the GO category were involved in hydrolase activity. Furthermore, 21 RIP genes and their corresponding amino acid sequences were obtained from libraries produced with transcriptome analysis. The analysis of physicochemical properties showed that 21 RIPs of P. volubilis contained ricin, the ricin_B_lectin domain, or RIP domains and could be divided into three subfamilies, with the largest number for type II RIPs. The expression patterns of 10 RIP genes indicated that they were mostly highly expressed in Pv-2 and 4 transcripts encoding ricin_B_like lectins had very low expression levels during the seed development of P. volubilis. This finding would represent valuable evidence for the safety of oil production from P. volubilis for human consumption. It is also notable that the expression level of the Unigene0030485 encoding type I RIP was the highest in roots, which would be related to the antiviral activity of RIPs. This study provides a comprehensive analysis of the physicochemical properties and expression patterns of RIPs in different organs of P. volubilis and lays a theoretical foundation for further research and utilization of RIPs in P. volubilis.

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A Novel Humanized Anti-Abrin A Chain Antibody Inhibits Abrin Toxicity In Vitro and In Vivo

Peng

Shi

et al. 2022

Front. Immunol.

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Abrin, a type-II ribosome inactivating protein from the seed of Abrus precatorius, is classified as a Category B bioterrorism warfare agent. Due to its high toxicity, ingestion by animals or humans will lead to death from multiple organ failure. Currently, no effective agents have been reported to treat abrin poisoning. In this study, a novel anti-abrin neutralizing antibody (S008) was humanized using computer-aided design, which possessed lower immunogenicity. Similar to the parent antibody, a mouse anti-abrin monoclonal antibody, S008 possessed high affinity and showed a protective effect against abrin both in vitro and in vivo, and protected mice that S008 was administered 6 hours after abrin. S008 was found that it did not inhibit entry of abrin into cells, suggesting an intracellular blockade capacity against the toxin. In conclusion, this work demonstrates that S008 is a high affinity anti-abrin antibody with both a neutralizing and protective effect and may be an excellent candidate for clinical treatment of abrin poisoning.

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Highly toxic type Ⅱ ribosome-inactivating proteins ricin and abrin and their detection methods: a review

Cited by 3 publications

References 63 publications

Ricin: an ancient toxicant, but still an evergreen

Ricin: an ancient toxicant, but still an evergreen

Integrated Transcriptome and Proteome Analysis Provides Insight into the Ribosome Inactivating Proteins in Plukenetia volubilis Seeds

A Novel Humanized Anti-Abrin A Chain Antibody Inhibits Abrin Toxicity In Vitro and In Vivo

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