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

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 a...

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Published inApplied microbiology and biotechnology Vol. 104; no. 10; pp. 4211 - 4226
Main Authors Wong, Jack Ho, Bao, Hui, Ng, Tzi Bun, Chan, Helen Hei Ling, Ng, Charlene Cheuk Wing, Man, Gene Chi Wai, Wang, Hexiang, Guan, Suzhen, Zhao, Shuang, Fang, Evandro Fei, Rolka, Krzysztof, Liu, Qin, Li, Chunman, Sha, Ou, Xia, Lixin
Format Journal Article
LanguageEnglish
Published Berlin/Heidelberg Springer Berlin Heidelberg 01.05.2020
Springer
Springer Nature B.V
Subjects
Amino Acid Sequence
amino acid sequences
Amino acids
Animals
Anopheles
Antimicrobial peptides
Bacteria
barley
Benincasa hispida
Biomedical and Life Sciences
Biotechnology
Camphor
catalytic activity
Chains
Cinnamomum camphora
Corn
cucumbers
Cucurbita
Culex
Culicidae - chemistry
Deactivation
Domains
Flowering
Flowering plants
Fruit flies
Gourds
Insect Proteins - metabolism
Lagenaria siceraria
Lectins
Life Sciences
Luffa acutangula
Luffa aegyptiaca
macroalgae
mechanism of action
Medical colleges
Microbial Genetics and Genomics
Microbiology
Mini-Review
Molecular weight
Momordica charantia
Mosquitoes
Mushrooms
Peptides
Phytolacca
Pine needles
Pisum sativum subsp. sativum var. sativum
Plant Proteins - metabolism
Plants (botany)
Pleurotus tuber-regium
Polyporus umbellatus
Proenzymes
Protein biosynthesis
Protein Biosynthesis - drug effects
Protein synthesis
Proteins
pumpkins
Ribonucleic acid
Ribosome Inactivating Proteins - classification
Ribosome Inactivating Proteins - metabolism
Ribosome Inactivating Proteins - pharmacology
ribosomes
RNA
Seeds
Seeds - chemistry
Shiga toxin
Snakes
Spiroplasma
Streptomyces coelicolor
Toxins
Trichosanthes cucumerina var. anguina
tubers
Volvariella volvacea
zymogens
Canada
Japan
China
Ribotoxins
Ribosome-inactivating proteins
Algal
Bacterial
Plant
Fungal
Mushroom
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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, antimicrobial 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.
AbstractList 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, antimicrobial 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.
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, antimicrobial 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.
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, antimicrobial 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.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, antimicrobial 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.
Audience Academic
Author Zhao, Shuang
Liu, Qin
Li, Chunman
Wang, Hexiang
Fang, Evandro Fei
Ng, Tzi Bun
Guan, Suzhen
Xia, Lixin
Man, Gene Chi Wai
Sha, Ou
Rolka, Krzysztof
Bao, Hui
Chan, Helen Hei Ling
Wong, Jack Ho
Ng, Charlene Cheuk Wing
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  organization: Department of Anatomy, Histology and Embryology, School of Basic Medical Sciences, Shenzhen University, State Key Laboratory of Respiratory Disease for Allergy, School of Medicine, Shenzhen University
– sequence: 2
  givenname: Hui
  surname: Bao
  fullname: Bao, Hui
  organization: State Key Laboratory of Respiratory Disease for Allergy, School of Medicine, Shenzhen University
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  givenname: Tzi Bun
  orcidid: 0000-0001-7951-8838
  surname: Ng
  fullname: Ng, Tzi Bun
  email: tzibunng@cuhk.edu.hk
  organization: School of Biomedical Sciences, Faculty of Medicine, The Chinese University of Hong Kong
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  givenname: Helen Hei Ling
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  fullname: Chan, Helen Hei Ling
  email: helen.chan@vitagreen.com
  organization: Vita Green Pharmaceuticals (Hong Kong) Limited
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  fullname: Ng, Charlene Cheuk Wing
  organization: School of Medicine, King’s College London
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  organization: Department of Orthopedics and Traumatology, The Chinese University of Hong Kong
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  givenname: Hexiang
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  organization: Department of Microbiology, China Agricultural University
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  givenname: Suzhen
  surname: Guan
  fullname: Guan, Suzhen
  organization: Department of Social Medicine, College of Public Health, Xinjiang Medical University
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  givenname: Shuang
  surname: Zhao
  fullname: Zhao, Shuang
  organization: Institute of Plant and Environment Protection, Beijing Academy of Agriculture and Forestry Sciences, and Beijing Key Laboratory of Fruits and Vegetable Storage and Processing, Key Laboratory of Vegetable Postharvest Processing, Ministry of Agriculture
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  givenname: Evandro Fei
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  organization: Institute of Plant Nutrition, Agricultural Resources and Environmental Science, Henan Academy of Agricultural Sciences
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  organization: Department of Anatomy, Histology and Embryology, School of Basic Medical Sciences, Shenzhen University
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  organization: State Key Laboratory of Respiratory Disease for Allergy, School of Medicine, Shenzhen University
BackLink https://www.ncbi.nlm.nih.gov/pubmed/32193575$$D View this record in MEDLINE/PubMed
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Copyright Springer Nature B.V. May 2020
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Wed Aug 13 06:20:12 EDT 2025
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Tue Jun 10 20:53:13 EDT 2025
Fri Jun 27 05:04:20 EDT 2025
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Issue 10
Keywords Ribotoxins
Ribosome-inactivating proteins
Algal
Bacterial
Plant
Fungal
Mushroom
Language English
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Snippet 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...
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SubjectTerms Amino Acid Sequence
amino acid sequences
Amino acids
Animals
Anopheles
Antimicrobial peptides
Bacteria
barley
Benincasa hispida
Biomedical and Life Sciences
Biotechnology
Camphor
catalytic activity
Chains
Cinnamomum camphora
Corn
cucumbers
Cucurbita
Culex
Culicidae - chemistry
Deactivation
Domains
Flowering
Flowering plants
Fruit flies
Gourds
Insect Proteins - metabolism
Lagenaria siceraria
Lectins
Life Sciences
Luffa acutangula
Luffa aegyptiaca
macroalgae
mechanism of action
Medical colleges
Microbial Genetics and Genomics
Microbiology
Mini-Review
Molecular weight
Momordica charantia
Mosquitoes
Mushrooms
Peptides
Phytolacca
Pine needles
Pisum sativum subsp. sativum var. sativum
Plant Proteins - metabolism
Plants (botany)
Pleurotus tuber-regium
Polyporus umbellatus
Proenzymes
Protein biosynthesis
Protein Biosynthesis - drug effects
Protein synthesis
Proteins
pumpkins
Ribonucleic acid
Ribosome Inactivating Proteins - classification
Ribosome Inactivating Proteins - metabolism
Ribosome Inactivating Proteins - pharmacology
ribosomes
RNA
Seeds
Seeds - chemistry
Shiga toxin
Snakes
Spiroplasma
Streptomyces coelicolor
Toxins
Trichosanthes cucumerina var. anguina
tubers
Volvariella volvacea
zymogens
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Title New ribosome-inactivating proteins and other proteins with protein synthesis–inhibiting activities
URI https://link.springer.com/article/10.1007/s00253-020-10457-7
https://www.ncbi.nlm.nih.gov/pubmed/32193575
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http://hdl.handle.net/10852/85328
Volume 104
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