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Published in Paul Pumpens, Single-Stranded RNA Phages, 2020
The MS2 RNA was used as a model by the characterization of the depurination activity of saporin (Barbieri et al. 1994), a ribosome-inactivating protein that appeared as a representative of the multigene family of proteins in various parts of the Saponaria officinalis plant. Interest in the ribosome-inactivating proteins (RIPs), which were produced in fact not only by plants, but also by bacteria and fungi, grew recently in connection with their potent anti-HIV activity (Yadav and Batra 2015).
Microalgae and Cyanobacteria as a Potential Source of Anticancer Compounds
Published in Gokare A. Ravishankar, Ranga Rao Ambati, Handbook of Algal Technologies and Phytochemicals, 2019
An exciting area of development is the use of algal chloroplast as a synthetic biology platform for production of therapeutics (Dyo and Purton 2018). Using this approach, transgenes can be inserted at precise and predetermined locations within the chloroplast genome to allow for stable synthesis of a desired recombinant protein. Among the microalgal species, Chlamydomonas reinhardtii is one of the most advanced microalgal platforms for chloroplast transformation. The chloroplast genetic system of this microalga is well suited for synthetic biology as its genome is small (205 kb) and of low complexity (99 genes) (Maul et al. 2002). Recombinant proteins including anticancer immunotoxins have been successfully produced using this microalgal platform. For instance, Tran et al. (2013) successfully developed Chlamyomonas reinhardtii as a platform to produce a series of chimeric proteins. The recombinant protein consists of a single chain antibody (scFV) targeting the B-cell surface antigen CD22, genetically fused to the eukaryotic ribosome inactivating protein, gelonin, from Gelonium multiform. The antibody-toxin chimeric protein is useful as an immunotoxin that acts as a cytotoxic agent against B-cell lymphomas.
Plant Lectins in Cancer Treatment: The Case of Viscum album L.
Published in Spyridon E. Kintzios, Maria G. Barberaki, Evangelia A. Flampouri, Plants That Fight Cancer, 2019
A number of in vivo studies against animal models are conducted regarding plant-derived lectins and their potential anticancer properties. Abrin was administered to nude mice, bearing three different human tumors. The treatment caused the delay of tumor growth in the case of Lewis lung carcinoma and increased life expectancy in mice inoculated with Ehrlich ascites carcinoma and B16 melanoma (Fodstad et al. 1977). Similar results presented in other assays where abrin isoforms exhibited inhibition of tumor growth in mice with sarcoma 180 (Lin et al. 1982), tumor reduction in mice bearing Dalton’s lymphoma ascites, and increased animal life span (Ramnath et al. 2002). WGA was found to control tumor growth on lymphoma (Ganguly and Das 1994), and a wheat germ extract inhibits colon cancer in F-344 rats (Zalatnai et al. 2001). Peanut agglutinin (PNA) against mice bearing Dalton’s lymphoma caused the reduction of lymphoma proliferation and activation of autophagic and apoptotic procedures (Mukhopadhyay et al. 2014). Momordica charantia lectin (MCL), a type II ribosome inactivating protein, exhibited antitumor activity towards athymic nude mice xenograft inoculated by nasopharyngeal carcinoma cell line CNE2 (Fang et al. 2012).
Screening and characterisation of a novel efficient tumour cell-targeting peptide derived from insulin-like growth factor binding proteins
Published in Journal of Drug Targeting, 2023
Min-Lin He, Jin Lei, Xue-Wei Cao, Jian Zhao, Fu-Jun Wang
Trichosanthin (TCS) is a macromolecular active protein extracted from the root tuber of Trichosanthes kirilowii and has long been used in traditional Chinese medicine as an abortifacient [36]. As a type I ribosome inactivating protein (RIP), TCS is widely used in antitumor research [36–39]. However, unlike type II RIP, TCS has a low transmembrane entry efficiency, which affects its intracellular pharmacological effects. In this study, we analysed and selected a highly homologous 18 amino acid consensus sequences from the C-terminal domain HBD of IGFBPs, named as IHP (IGFBP-HBD-CPP), which was fused with the enhanced green fluorescent protein (EGFP) to test its transmembrane activity by fluorescence microscopy and flow cytometry. The pattern of its differential binding to tumour cells were screened. Subsequently, a fusion protein of TCS and IHP5 was expressed to investigate the toxicity of recombinant protein to various tumour cells.
An Overview of Hepatocellular Carcinoma with Emphasis on Dietary Products and Herbal Remedies
Published in Nutrition and Cancer, 2022
Deepa S. Mandlik, Satish K. Mandlik
Momordica charantia lectin (MCL) is a type II ribosome-inactivating protein obtained from bitter gourd, a vegetable used commonly. In Vitro and In Vivo, MCL treatment significantly reduced HCC cell growth by inducing G2/M phase arrest, autophagy and apoptosis (70). Furthermore, in cultured Hep G2 cells, MAP30 (type I ribosome-inactivating protein) isolated from bitter gourd, showed both cytostatic and cytotoxic impact. The activities were due to the induction of S phase cell cycle arrest and activation of extrinsic and intrinsic caspase apoptosis.MAP30’s anti-tumor activity has also been revealed In Vivo. RNase MC2 is a ribonuclease found in M. charantia that has been shown to increase apoptosis in both in-vivo and In Vitro studies (71). The antioxidant functions of total phenolic content, chlorogenic acid and anthocyanin content and in-vitro anticancer ability of potato. The highest antioxidant activity was found in Solanum pinnatisectum, which also had the best antiproliferative effects against liver cancer cells (72). The glycoalkaloids contained in potatoes were thought to have anti-tumor properties. In the range of 0.1–10 g/mL, treatment with potato glycoalkaloids (α-chaconine), subdued HepG2 cell progress with lower cytotoxicity to normal liver cells (73).
Immunotoxins and nanobody-based immunotoxins: review and update
Published in Journal of Drug Targeting, 2021
Mohammad Reza Khirehgesh, Jafar Sharifi, Fatemeh Safari, Bahman Akbari
RT is a heterodimer glycoprotein in the seeds of the Ricinus communis that isolated first by Peter Hermann Stillmark [92]. RT (∼64 kDa) belongs to the type II ribosome-inactivating proteins (RIP II) family that consists of A chain, enzymatically active subunit (RTA), and B chains, cell binding subunit (RTB). RTA composes of 267 amino acids (∼32 kDa) with irreversible RNA N-glycosidase activity. RTA has been used in IT construction as a cytotoxic moiety [93–95]. The subunit prevents the binding of eEF2 to the ribosome by depurination of adenine 4324 at the specific alpha-sarcin/ricin loop in 28 s ribosomal RNA (rRNA). Subsequently, protein synthesis ceases at the translocation step and the cells die apoptotically [96,97]. RTB is a galactose-binding lectin (GBL) that comprises 262 amino acids. RTA and RTB connect with interchain disulphide bonds in Cys-259 of RTA and Cys-4 of RTB (∼34 kDa) [98,99]. The binding of RTB to β1-4-linked galactose on the eukaryotic cells surface leads to clathrin-mediated endocytosis or clathrin-independent endocytosis of the toxin [100,101]. After processing in the endosome and Golgi network, RT enters the ER lumen. In the ER lumen, PDI reduces the disulphide bond between RTA and RTB, leads to the separation of the two subunits. Finally, RTA transfers to the cytoplasm and inhibits protein synthesis by inactivating ribosomes, so leads to cell death [102] (Figure 4).