Ribosome-inactivating proteins (RIPs) and their important health promoting property

Wang, Shuzhen; Li, Zhiliang; Li, Shiming; Di, Rong; Ho, Chi‐Tang; Yang, Guliang

doi:10.1039/c6ra02946a

Cited by 16 publications

(12 citation statements)

References 133 publications

(98 reference statements)

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“…Type II RIPs are heterodimeric proteins with an enzymatically active A chain of about 30 kDa, which is structurally similar to type I RIPs, and a slightly bigger B chain of about 35 kDa that possesses lectin properties. A type III RIPs category comprising maize b-32 and barley JIP60 have also been proposed by some authors (Choudhary et al, 2020;Wang et al, 2016;Zhu et al, 2018). Type III RIPs contain a single A-chain related to RIP activity with an additional peptide which, in the case of JIP60, functions in activating resistance to biotic and abiotic stresses (Rustgi et al, 2014).…”

Section: Introductionmentioning

confidence: 99%

Plant-derived ribosome-inactivating proteins involved in defense against plant viruses

2021

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Section: Introductionmentioning

confidence: 99%

Plant-derived ribosome-inactivating proteins involved in defense against plant viruses

2021

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“…Charantins, a mixture of steroidal saponins found in the fruits of M. charantia exhibit hypoglycaemic activity 6,7 . Many proteins and peptides which possess RNA N-glycosidase, DNase-like, antitumor, immunosuppressive, and antimicrobial activities have also been isolated, such as ribosome-inactivating proteins (RIPs), momordica anti-HIV protein of 30 kDa (MAP30), and momorcharins (MMC) 8 . These compounds are of interest to researchers and have been studied to confirm their pharmacological activities.…”

Section: Introductionmentioning

confidence: 99%

“…In addition to RNA N-glycosidase activity, RIPs also exhibit adenosine glycosidase, RNase, DNase-like, superoxide dismutase, anti-HIV, and antimicrobial activities [10][11][12][13][14][15] . RIPs can be categorised into three types: RIPs with a single polypeptide (enzymatic subunit, chain A) are classified as type I, the structure with chain A binding to a lectin-like subunit (chain B) with a disulphide bond is classified as type II, and the synthesised precursor or inactive form with a domain similar to type I is classified as type III 8,[16][17] .…”

Section: Introductionmentioning

confidence: 99%

“…Bitter melon proteins have been found in many parts of the plant, especially fruits and seeds. These proteins have been reported to act as N-glycosidases, which were identified as RIPs 8,36 . Thai bitter melon protein (MRK29) with a molecular weight of 28.6 kDa was reported to have anti-HIV reverse transcriptase activity, which exhibited a significant reduction in viral core protein p24 expression in HIV-infected cells 24 .…”

Section: Introductionmentioning

confidence: 99%

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Investigation of genes coding for anti-HIV proteins MAP30 and MRK29 from Thai bitter melon (Momordica charantia L.)

Mekloy¹,

Sakchaisri²,

Jiratchariyakul³

et al. 2022

Pharm Sci Asia

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Thai bitter melon, or Ma-Ra-Khee-Nok, is an M. charantia L. variety that is widely cultivated in Thailand. Thai bitter melon exhibits various pharmacological activities, including antidiabetic and antiviral. Many phytochemicals are found in various parts of this plant, notably ribosome-inactivating proteins (RIPs) in fruits and seeds. MAP30 is a well-known type I RIP isolated from seeds of the Chinese bitter melon. MAP30 exhibits various pharmacological activities, such as cytotoxicity and anti-HIV activity. However, there are no reports on MAP30 sequence information in Thai bitter melons. There have been only reported on MRK29 protein which exhibits anti-HIV reverse transcriptase activity, but only 20 amino acid sequences from the N-terminal were identified. In this study, we obtained 17 sequences with a high nucleotide sequence identity (>99%) with MAP30. Of these, one sequence (McRIP001) had double substitutions at the leading sequence, twelve partial (mature) sequences had an identity of 100%, and two sequences ( McRIP002) had a single substitution (silent mutation) at the same position. Moreover, two sequences, McRIP003 and McRIP004, had a single substitution at different positions. Phylogenetic analysis of amino acid sequences demonstrated a close relationship between the obtained sequences and MAP30. Homology modelling revealed that the mutation points did not involve RNA Nglycosidase active sites. The cloning of MRK29 was unsuccessful due to the limit of available information. The present study provides a valuable reference for further research and quality control of healthcare products from Thai bitter melon.

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“…It belongs to the toxic type II ribosome-inactivating proteins, which exhibit affinity for galactose (Voss et al, 2006b). Toxic type II RIPs such as ricin, abrin and viscum lectin I are dimeric proteins with the A-chain linked to the B-chain (lectin-like) by a disulfide bond (Marshall et al, 2011;Schrot et al, 2015;Wang et al, 2016). As found for other type II RIPs, the toxicity of Rpx in tumor cells results from the inhibition of protein synthesis following translational arrest by the A-chain.…”

Section: Introductionmentioning

confidence: 99%

Riproximin Exhibits Diversity in Sugar Binding, and Modulates some Metastasis-Related Proteins with Lectin like Properties in Pancreatic Ductal Adenocarcinoma

et al. 2020

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Riproximin (Rpx) is a type II ribosome-inactivating protein with specific anti-proliferative activity. It was purified from Ximenia americana by affinity chromatography using a resin coupled with lactosyl residues. The same technique facilitated isolation of proteins with lectin-like properties from human Suit2-007 and rat ASML pancreatic cancer cells, which were termed lactosyl-sepharose binding proteins (LSBPs). The role of these proteins in cancer progression was investigated at mRNA level using chip array data of Suit2-007 and ASML cells re-isolated from nude rats. These data compared significant mRNA expression changes when relating primary (pancreas) and metastatic (liver) sites following orthotopic and intraportal implantation of Pancreatic Ductal Adenocarcinoma (PDAC) cells, respectively. The affinity of Rpx to 13 simple sugar structures was modeled by docking experiments, the ranking of which was principally confirmed by NMR-spectroscopy. In addition, Rpx and LSBPs were evaluated for anti-proliferative activity and their cellular uptake was assessed by fluorescence microscopy. From 13 monosaccharides evaluated, open-chain rhamnose, β-d-galactose, and α-l-galactopyranose showed the highest affinities for site 1 of Rpx’s B-chain. NMR evaluation yielded a similar ranking, as galactose was among the best binders. Both, Rpx and LSBPs reduced cell proliferation in vitro, but their anti-proliferative effects were decreased by 15–20% in the presence of galactose. The program “Ingenuity Pathway Analysis” identified 2,415 genes showing significantly modulated mRNA expression following exposure of Suit2-007 cells to Rpx in vitro. These genes were then matched to those 1,639 genes, which were significantly modulated in the rat model when comparing primary and metastatic growth of Suit2-007 cells. In this overlap analysis, LSBP genes were considered separately. The potential suitability of Rpx for treating metastatic Suit2-007 PDAC cells was reflected by those genes, which were modulated by Rpx in a way opposite to that observed in cancer progression. Remarkably, these were 14% of all genes modulated during cancer progression, but 71% of the respective LSBP gene subgroup. Based on these findings, we predict that Rpx has the potential to treat PDAC metastasis by modulating genes involved in metastatic progression, especially by targeting LSBPs.

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Ribosome-inactivating proteins (RIPs) and their important health promoting property

Abstract: Ribosome-inactivating proteins (RIPs), widely present in plants, certain fungi and bacteria, can inhibit protein synthesis by removing one or more specific adenine residues from the large subunit of ribosomal RNAs (rRNAs).

Cited by 16 publications

References 133 publications

Plant-derived ribosome-inactivating proteins involved in defense against plant viruses

Plant-derived ribosome-inactivating proteins involved in defense against plant viruses

Investigation of genes coding for anti-HIV proteins MAP30 and MRK29 from Thai bitter melon (Momordica charantia L.)

Riproximin Exhibits Diversity in Sugar Binding, and Modulates some Metastasis-Related Proteins with Lectin like Properties in Pancreatic Ductal Adenocarcinoma

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