Ribosome Inactivating Proteins: From Plant Defense to Treatments against Human Misuse or Diseases

Barbier, Julien; Gillet, Daniel

doi:10.3390/toxins10040160

Cited by 8 publications

(3 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This result confirms that kirkiin ability to inhibit protein synthesis is related to the N-glycosylase activity on mammalian ribosomes. As several evidences suggest that rRNA N-glycosylase activity might play a role in plant defense [ 32 ], for example against fungi, the effect of kirkiin was assayed on ribosomes from Saccharomyces cerevisiae , which might be homologous to ribosomes from putative plant pathogens. Kirkiin displayed rRNA N-glycosylase activity on yeast ribosomes, as indicated by the release of the diagnostic fragment [ 33 ] upon treatment with aniline acetate.…”

Section: Discussionmentioning

confidence: 99%

Kirkiin: A New Toxic Type 2 Ribosome-Inactivating Protein from the Caudex of Adenia kirkii

Bortolotti

Maiello

Ferreras

et al. 2021

Toxins

View full text Add to dashboard Cite

Ribosome-inactivating proteins (RIPs) are plant toxins that irreversibly damage ribosomes and other substrates, thus causing cell death. RIPs are classified in type 1 RIPs, single-chain enzymatic proteins, and type 2 RIPs, consisting of active A chains, similar to type 1 RIPs, linked to lectin B chains, which enable the rapid internalization of the toxin into the cell. For this reason, many type 2 RIPs are very cytotoxic, ricin, volkensin and stenodactylin being the most toxic ones. From the caudex of Adenia kirkii (Mast.) Engl., a new type 2 RIP, named kirkiin, was purified by affinity chromatography on acid-treated Sepharose CL-6B and gel filtration. The lectin, with molecular weight of about 58 kDa, agglutinated erythrocytes and inhibited protein synthesis in a cell-free system at very low concentrations. Moreover, kirkiin was able to depurinate mammalian and yeast ribosomes, but it showed little or no activity on other nucleotide substrates. In neuroblastoma cells, kirkiin inhibited protein synthesis and induced apoptosis at doses in the pM range. The biological characteristics of kirkiin make this protein a potential candidate for several experimental pharmacological applications both alone for local treatments and as component of immunoconjugates for systemic targeting in neurodegenerative studies and cancer therapy.

show abstract

Section: Discussionmentioning

confidence: 99%

Kirkiin: A New Toxic Type 2 Ribosome-Inactivating Protein from the Caudex of Adenia kirkii

Bortolotti

Maiello

Ferreras

et al. 2021

Toxins

View full text Add to dashboard Cite

show abstract

“…Type I RIPs consist only of the N-glycosylase domain, whereas type II RIPs such as ricin from Ricinus communis L. additionally contain a lectin domain which binds with high affinity to galactose molecules on the cell surface. The physiological role of type I RIPs in the plant cell is not completely understood, however they have been reported to provide protection against herbivores 7 , 8 and viruses 9 .…”

Section: Introductionmentioning

confidence: 99%

An unusual type I ribosome-inactivating protein from Agrostemma githago L.

Weise

Schrot

Wuerger

et al. 2020

Sci Rep

View full text Add to dashboard Cite

Agrostemma githago L. (corn cockle) is an herbaceous plant mainly growing in Europe. The seeds of the corn cockle are toxic and poisonings were widespread in the past by consuming contaminated flour. The toxic principle of Agrostemma seeds was attributed to triterpenoid secondary metabolites. Indeed, this is in part true. However Agrostemma githago L. is also a producer of ribosome-inactivating proteins (RIPs). RIPs are N-glycosylases that inactivate the ribosomal RNA, a process leading to an irreversible inhibition of protein synthesis and subsequent cell death. A widely known RIP is ricin from Ricinus communis L., which was used as a bioweapon in the past. In this study we isolated agrostin, a 27 kDa RIP from the seeds of Agrostemma githago L., and determined its full sequence. The toxicity of native agrostin was investigated by impedance-based live cell imaging. By RNAseq we identified 7 additional RIPs (agrostins) in the transcriptome of the corn cockle. Agrostin was recombinantly expressed in E. coli and characterized by MALDI-TOF–MS and adenine releasing assay. This study provides for the first time a comprehensive analysis of ribosome-inactivating proteins in the corn cockle and complements the current knowledge about the toxic principles of the plant.

show abstract

“…Among them, RIPs are a type of RNase that can specifically modify the ribonucleic acid rRNA on the large subunit of the ribosome by destroying the structural integrity of the ribosome and inhibiting protein biosynthesis [30,31]. RIPs are divided into two types according to their primary structure and enzymatic mechanism of action: type I RIPs and type II RIPs.…”

Section: Discussionmentioning

confidence: 99%

Beauveria bassiana Ribotoxin (BbRib) Induces Silkworm Cell Apoptosis via Activating Ros Stress Response

Taha

et al. 2021

Processes

View full text Add to dashboard Cite

The BbRib gene participates in the infection process of Beauveria bassiana (B. bassiana). It also helps pathogenic fungi to escape and defeat the insect host immune defense system by regulating the innate immune response. However, model insects are rarely used to study the mechanism of fungal ribosomal toxin protein. In this study, BbRib protein was produced by prokaryotic expression and injected into silkworm (Bombyx mori) larvae. The physiological and biochemical indexes of silkworm were monitored, and the pathological effects of BbRib protein on immune tissues of silkworm were examined by Hematoxylin and Eosin (HE) staining. BbRib protein can significantly affect the growth and development of the silkworm, causing poisoning, destroying the midgut and fat body and producing physiological changes. The ROS stress response in the adipose tissue and cells of the silkworm was activated to induce apoptosis. These results indicated that the BbRib gene not only participates in the infection process of B. bassiana, it also helps the pathogenic fungi escape the immune system by regulating the innate immune system of the silkworm, allowing it to break through the silkworm’s immune defense. This study reveals the potential molecular mechanism of BbRib protein to insect toxicity, and provides a theoretical basis and material basis for the development and use of novel insecticidal toxins.

show abstract

Ribosome Inactivating Proteins: From Plant Defense to Treatments against Human Misuse or Diseases

Cited by 8 publications

References 18 publications

Kirkiin: A New Toxic Type 2 Ribosome-Inactivating Protein from the Caudex of Adenia kirkii

Kirkiin: A New Toxic Type 2 Ribosome-Inactivating Protein from the Caudex of Adenia kirkii

An unusual type I ribosome-inactivating protein from Agrostemma githago L.

Beauveria bassiana Ribotoxin (BbRib) Induces Silkworm Cell Apoptosis via Activating Ros Stress Response

Contact Info

Product

Resources

About