New ribosome-inactivating proteins and other proteins with protein synthesis – inhibiting activities

Jack Ho Wong , Hui Bao , Tzi Bun Ng , Helen Hei Ling Chan , Charlene Cheuk Wing Ng , Gene Chi Wai Man , Hexiang Wang , Suzhen Guan , Shuang Zhao , Evandro Fei Fang , Krzysztof Rolka , Qin Liu , Chunman Li , Ou Sha , Lixin Xia

Abstract

Ribosome-inactivating proteins (RIPs) consist of three varieties. Type 1 RIPs are single-chained and approximately 30-kDa in molecular weight. Type 2 RIPs are double-chained and composed of a type 1 RIP chain and a lectin chain. Type III RIPs, such as maize b-32 barley and JIP60 which are produced as single-domain proenzymes, possess an N-terminal domain corresponding to the A domain of RIPs and fused to a C-terminal domain. In addition to the aforementioned three types of RIPs originating from flowering plants, there are recently discovered proteins and peptides with ribosome-inactivating and protein synthesis inhibitory activities but which are endowed with characteristics such as molecular weights distinctive from those of the regular RIPs. These new/unusual RIPs discussed in the present review encompass metazoan RIPs from Anopheles and Culex mosquitos, antimicro- bial peptides derived from RIP of the pokeweed Phytolacca dioica, maize RIP (a type III RIP derived from a precursor form), RIPs from the garden pea and the kelp. In addition, RIPs with a molecular weight smaller than those of regular type 1 RIPs are produced by plants in the Cucurbitaceae family including the bitter gourd, bottle gourd, sponge gourd, ridge gourd, wax gourd, hairy gourd, pumpkin, and Chinese cucumber. A small type II RIP from camphor tree (Cinnamomum camphora) seeds and a snake gourd type II RIP with its catalytic chain cleaved into two have been reported. RIPs produced from mushrooms including the golden needle mushroom, king tuber mushroom, straw mushroom, and puffball mushroom are also discussed in addition to a type II RIP from the mushroom Polyporus umbellatus. Bacterial (Spiroplasma) RIPs associated with the fruitfly, Shiga toxin, and Streptomyces coelicolor RIP are also dealt with. The aforementioned proteins display a diversity of molecular weights, amino acid sequences, and mechanisms of action. Some of them are endowed with exploitable antipathogenic activities.
Publication typeIn press (online first, early view)
Author Jack Ho Wong
Jack Ho Wong,,
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, Hui Bao
Hui Bao,,
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, Tzi Bun Ng
Tzi Bun Ng,,
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, Helen Hei Ling Chan
Helen Hei Ling Chan,,
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, Charlene Cheuk Wing Ng
Charlene Cheuk Wing Ng,,
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, Gene Chi Wai Man
Gene Chi Wai Man,,
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, Hexiang Wang
Hexiang Wang,,
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, Suzhen Guan
Suzhen Guan,,
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, Shuang Zhao
Shuang Zhao,,
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, Evandro Fei Fang
Evandro Fei Fang,,
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et al.`
Journal seriesApplied Microbiology and Biotechnology, ISSN 0175-7598, e-ISSN 1432-0614, (N/A 100 pkt)
Issue year2020
Noonline first
Pages1-16
Publication size in sheets0.75
Keywords in PolishBiałka aktywujące rybosomy, rybotoksyny, roślinne, glony, algi, grzyby, bakteryjne, grzybowe
Keywords in EnglishRibosome-inactivating proteins, ribotoxins, plant, algal, mushroom, bacterial, fungal
ASJC Classification2700 General Medicine; 1305 Biotechnology; 2402 Applied Microbiology and Biotechnology
Abstract in PolishW pracy przedstawiono charakterystykę białek aktywujących rybosomy.
DOIDOI:10.1007/s00253-020-10457-7
URL https://doi.org/10.1007/s00253-020-10457-7
Languageen angielski
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Wong_Ho-Jack_New_ribosome_inactivating_protein_2020.pdf 525,79 KB
Score (nominal)100
Score sourcejournalList
ScoreMinisterial score = 100.0, 29-05-2020, ArticleFromJournal
Publication indicators WoS Citations = 0.000; Scopus SNIP (Source Normalised Impact per Paper): 2018 = 1.236; WoS Impact Factor: 2018 = 3.670 (2) - 2018=3.889 (5)
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