Non‐toxic Type 2 Ribosome‐inactivating Proteins

Jiménez, Pilar; Gayoso, Manuel J.; Girbés, Tomás

doi:10.1002/9781118847237.ch5

Cited by 5 publications

(5 citation statements)

References 67 publications

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“…The protein translation inhibition activity of SNLRP and SNA-V was significantly higher than that of SNA-I in the in vitro cell-free system. The IC50 values for SNA-I and SNA-V correspond well with earlier estimations derived from studies using rabbit reticulocyte lysates [ 11 ]. Barbieri et al reported that the translation inhibition activity in a cell-free system was considerably higher for the reduced protein compared to the non-reduced type 2 RIPs (e.g.…”

Section: Discussionsupporting

confidence: 87%

“…nigra proteins (SNLRP > SNA-V > SNA-I > SNA-II > SNA-IV) did not mirror their cytotoxicity towards HeLa cells (SNA-V > SNA-II > SNA-I > SNLRP > SNA-IV). In line with this, it was shown that SNLRP exhibits at least 250-fold lower RIP activity in cellula than in vitro [ 52 ], while for ricin, RIP activity is in a comparable range in cellula and in vitro [ 11 ]. The lectin SNA-II proved to be even more cytotoxic than some of the RIPs, despite the absence of a RIP domain.…”

Section: Discussionmentioning

confidence: 87%

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The Cytotoxicity of Elderberry Ribosome-Inactivating Proteins Is Not Solely Determined by Their Protein Translation Inhibition Activity

et al. 2015

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Although the protein translation inhibition activity of ribosome inactivating proteins (RIPs) is well documented, little is known about the contribution of the lectin chain to the biological activity of these proteins. In this study, we compared the in vitro and intracellular activity of several S. nigra (elderberry) RIPs and non-RIP lectins. Our data demonstrate that RIPs from elderberry are much more toxic to HeLa cells than to primary fibroblasts. Differences in the cytotoxicity between the elderberry proteins correlated with differences in glycan specificity of their lectin domain, cellular uptake efficiency and intracellular destination. Despite the fact that the bulk of the RIPs accumulated in the lysosomes and partly in the Golgi apparatus, we could demonstrate effective inhibition of protein synthesis in cellula. As we also observed cytotoxicity for non-RIP lectins, it is clear that the lectin chain triggers additional pathways heralding cell death. Our data suggest that one of these pathways involves the induction of autophagy.

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Section: Discussionsupporting

confidence: 87%

Section: Discussionmentioning

confidence: 87%

The Cytotoxicity of Elderberry Ribosome-Inactivating Proteins Is Not Solely Determined by Their Protein Translation Inhibition Activity

et al. 2015

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“…Regarding the selectivity, from the side of the decrease in Rd12, the selectivity of ricin to RCA120, abrin, and AAG was 3.2, 13.4, and 22.1; and from the increase of adenine, the according selectivity was 3.3, 4.8, and 9.6 to the other three RIP-IIs. It should be noted that the selectivity toward other RIP-II proteins such as Sambucus nigra , kirkiin, stenodactylin, and volkensin, 31 is unknown and needs to be further explored.…”

Section: Resultsmentioning

confidence: 99%

SCX-tip-aided LC-MS detection of active ricinviaoligonucleotide substrates for depurination kinetics

Yang

Wang

Xiao

et al. 2023

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“…Although the classical RIPs such as ricin and abrin are very toxic proteins, a few type-2 RIPs such as ebulin 1 show little or no toxicity. The cytotoxicity of ebulin 1 for HeLa cells is much lower than that of ricin, with an IC 50 value of 6 Â 10 À8 M compared to 10 À12 M for ricin (Jiménez et al, 2014).…”

Section: Ribosome-inactivating Proteinsmentioning

confidence: 91%

Toxic proteins in plants

2015

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Plants have evolved to synthesize a variety of noxious compounds to cope with unfavorable circumstances, among which a large group of toxic proteins that play a critical role in plant defense against predators and microbes. Up to now, a wide range of harmful proteins have been discovered in different plants, including lectins, ribosome-inactivating proteins, protease inhibitors, ureases, arcelins, antimicrobial peptides and pore-forming toxins. To fulfill their role in plant defense, these proteins exhibit various degrees of toxicity towards animals, insects, bacteria or fungi. Numerous studies have been carried out to investigate the toxic effects and mode of action of these plant proteins in order to explore their possible applications. Indeed, because of their biological activities, toxic plant proteins are also considered as potentially useful tools in crop protection and in biomedical applications, such as cancer treatment. Genes encoding toxic plant proteins have been introduced into crop genomes using genetic engineering technology in order to increase the plant's resistance against pathogens and diseases. Despite the availability of ample information on toxic plant proteins, very few publications have attempted to summarize the research progress made during the last decades. This review focuses on the diversity of toxic plant proteins in view of their toxicity as well as their mode of action. Furthermore, an outlook towards the biological role(s) of these proteins and their potential applications is discussed.

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Non‐toxic Type 2 Ribosome‐inactivating Proteins

Cited by 5 publications

References 67 publications

The Cytotoxicity of Elderberry Ribosome-Inactivating Proteins Is Not Solely Determined by Their Protein Translation Inhibition Activity

The Cytotoxicity of Elderberry Ribosome-Inactivating Proteins Is Not Solely Determined by Their Protein Translation Inhibition Activity

SCX-tip-aided LC-MS detection of active ricinviaoligonucleotide substrates for depurination kinetics

Toxic proteins in plants

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