Involvement of OsRIP1, a ribosome-inactivating protein from rice, in plant defense against Nilaparvata lugens

Zaeytijd, Jeroen De; Chen, Pengyu; Scheys, Freja; Subramanyam, Kondeti; Dubiel, Malgorzata; Schutter, Kristof De; Smagghe, Guy; Damme, Els J.M. Van

doi:10.1016/j.phytochem.2019.112190

Cited by 8 publications

(5 citation statements)

References 18 publications

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“…Different hypotheses on the role of RIPs in plants are under discussion. RIPs possess antiviral, antifungal, antibacterial and insecticidal activities, which may contribute in the protection against plant pests and predators [ 18 , 19 ]. In addition, RIP activity is increased in senescent and stressed leaves, suggesting that RIPs play an important role in regulating the death of plant cells.…”

Section: Introductionmentioning

confidence: 99%

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Sapovaccarin-S1 and -S2, Two Type I RIP Isoforms from the Seeds of Saponaria vaccaria L.

Schlaak

Weise

Kuropka

et al. 2022

Toxins

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Type I ribosome-inactivating proteins (RIPs) are plant toxins that inhibit protein synthesis by exerting rRNA N-glycosylase activity (EC 3.2.2.22). Due to the lack of a cell-binding domain, type I RIPs are not target cell-specific. However once linked to antibodies, so called immunotoxins, they are promising candidates for targeted anti-cancer therapy. In this study, sapovaccarin-S1 and -S2, two newly identified type I RIP isoforms differing in only one amino acid, were isolated from the seeds of Saponaria vaccaria L. Sapovaccarin-S1 and -S2 were purified using ammonium sulfate precipitation and subsequent cation exchange chromatography. The determined molecular masses of 28,763 Da and 28,793 Da are in the mass range typical for type I RIPs and the identified amino acid sequences are homologous to known type I RIPs such as dianthin 30 and saporin-S6 (79% sequence identity each). Sapovaccarin-S1 and -S2 showed adenine-releasing activity and induced cell death in Huh-7 cells. In comparison to other type I RIPs, sapovaccarin-S1 and -S2 exhibited a higher thermostability as shown by nano-differential scanning calorimetry. These results suggest that sapovaccarin-S1 and -S2 would be optimal candidates for targeted anti-cancer therapy.

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Section: Introductionmentioning

confidence: 99%

“…The RIP plant extract can either be directly applied to the plant surface or, alternatively, a virus-resistant transgenic plant may be constructed [ 23 , 24 ]. In terms of crop protection, the antiviral activity of RIPs is complemented by insecticidal effects [ 19 , 25 ].…”

Section: Introductionmentioning

confidence: 99%

Sapovaccarin-S1 and -S2, Two Type I RIP Isoforms from the Seeds of Saponaria vaccaria L.

Schlaak

Weise

Kuropka

et al. 2022

Toxins

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show abstract

“…A study highlighting the effect of a pest infestation, Nilaparvata lugens (brown plant hopper) in rice and its role in inducing transcription of OsRIP1 has established the defensive property of OsRIP1 against said pest under in vitro conditions. It was observed that OsRIP1 scuttled the protein translation of insect ribosomes 75 . Another study has demonstrated the dose‐dependent entomotoxic effect of type‐1 RIPs in inducing mortality in insects attacking the plants.…”

Section: Role Of Rips In Defence Against Insect/pest Infestationsmentioning

confidence: 99%

“…It was observed that OsRIP1 scuttled the protein translation of insect ribosomes. 75 Another study has demonstrated the dose-dependent entomotoxic effect of type-1 RIPs in inducing mortality in insects attacking the plants. The study observed the effects of lychnin, momordin, gelonin, PAP-S and Saporin S-6 on larvae of Spodoptera frugiperda and Anticarsia gemmatalis.…”

Section: Role Of Rips In Defence Against Insect/pest Infestationsmentioning

confidence: 99%

Expanding role of ribosome‐inactivating proteins: From toxins to therapeutics

et al. 2022

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Ribosome-inactivating proteins (RIPs) are toxic proteins with N-glycosidase activity. RIPs exert their action by removing a specific purine from 28S rRNA, thereby, irreversibly inhibiting the process of protein synthesis. RIPs can target both prokaryotic and eukaryotic cells. In bacteria, the production of RIPs aid in the process of pathogenesis whereas, in plants, the production of these toxins has been attributed to bolster defense against insects, viral, bacterial and fungal pathogens. In recent years, RIPs have been engineered to target a particular cell type, this has fueled various experiments testing the potential role of RIPs in many biomedical applications like anti-viral and anti-tumor therapies in animals as well as anti-pest agents in engineered plants. In this review, we present a comprehensive study of various RIPs, their mode of action, their significance in various fields involving plants and animals. Their potential as treatment options for plant infections and animal diseases is also discussed.

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“…The heterologously expressed RIPs in tobacco plants result in enhanced resistance to Spodoptera exigua with low toxicity to the plant cells [ 9 ]. Based on these research facts, RIPs have been shown to confer broad-spectrum resistance to a variety of plant diseases and insect pests, especially in the agricultural field [ 9 , 10 , 11 ]. Furthermore, a formulation of RIPs combined with antibodies was used to treat cancer, indicating that RIPs have anticancer activity and potential promising applications in the cancer medicine field [ 5 , 12 , 13 , 14 ].…”

Section: Introductionmentioning

confidence: 99%

Ribosome-Inactivating Proteins of Bougainvillea glabra Uncovered Polymorphism and Active Site Divergence

Lin

et al. 2021

Toxins

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Ribosome-inactivating proteins (RIPs) are toxic proteins that can inhibit protein synthesis. RIPs purified from Bougainvillea have low nonspecific toxicity, showing promise for processing applications in the agricultural and medical fields. However, systematic research on the polymorphism of Bougainvillea RIPs is lacking, and it is worth exploring whether different isoforms differ in their active characteristics. The transcriptional and translational expression of type I RIPs in Bougainvillea glabra leaves was investigated in this study. Seven RIPs exhibited seasonal variation at both the mRNA and protein levels. The isoforms BI4 and BI6 showed the highest transcriptional expression in both the summer and autumn samples. Interestingly, BI6 was not detected in the protein level in any of the samples. However, the bioinformatics analysis showed that RIPs derived from the same species were gathered in a different cluster, and that the active sites changed among the isoforms during evolution. The significant discrepancy in Bougainvillea RIPs mainly locates at both termini of the amino acid sequence, particularly at the C terminus. Post-translational modifications may also exist in Bougainvillea RIPs. It is concluded that the reason for the polymorphism of Bougainvillea RIPs may be that these proteins are encoded by multiple genes due to genetic processes such as gene duplication and mutation. According to the results of sequence analysis, the possible functional differences of B. glabra RIP isoforms are discussed with regard to the observed discrepancy in both active sites and structures.

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Involvement of OsRIP1, a ribosome-inactivating protein from rice, in plant defense against Nilaparvata lugens

Cited by 8 publications

References 18 publications

Sapovaccarin-S1 and -S2, Two Type I RIP Isoforms from the Seeds of Saponaria vaccaria L.

Sapovaccarin-S1 and -S2, Two Type I RIP Isoforms from the Seeds of Saponaria vaccaria L.

Expanding role of ribosome‐inactivating proteins: From toxins to therapeutics

Ribosome-Inactivating Proteins of Bougainvillea glabra Uncovered Polymorphism and Active Site Divergence

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