Ribosome-inactivating proteins Potent poisons and molecular tools

Ribosome-inactivating proteins (RIPs) were first isolated over a century ago and have been shown to be catalytic toxins that irreversibly inactivate protein synthesis. Elucidation of atomic structures and molecular mechanism has revealed these proteins to be a diverse group subdivided into two class...

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Published inVirulence Vol. 4; no. 8; pp. 774 - 784
Main Authors Walsh, Matthew J, Dodd, Jennifer E, Hautbergue, Guillaume M
Format Journal Article
LanguageEnglish
Published United States Taylor & Francis 15.11.2013
Landes Bioscience
Subjects
abrin
analytical and therapeutic applications
Bacterial Toxins - metabolism
biological weapon
BLF1
BPSL1549
eukaryotic protein synthesis inhibition
Humans
Poisons - toxicity
Protein Synthesis Inhibitors - toxicity
Ribosome Inactivating Proteins - toxicity
ricin
RNA, Ribosomal, 28S - metabolism
saporin
Shiga toxins
Special Focus Review
α-sarcin
abrin
biological weapon
ricin
BPSL1549
analytical and therapeutic applications
α-sarcin
BLF1
Shiga toxins
saporin
eukaryotic protein synthesis inhibition
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Abstract Ribosome-inactivating proteins (RIPs) were first isolated over a century ago and have been shown to be catalytic toxins that irreversibly inactivate protein synthesis. Elucidation of atomic structures and molecular mechanism has revealed these proteins to be a diverse group subdivided into two classes. RIPs have been shown to exhibit RNA N-glycosidase activity and depurinate the 28S rRNA of the eukaryotic 60S ribosomal subunit. In this review, we compare archetypal RIP family members with other potent toxins that abolish protein synthesis: the fungal ribotoxins which directly cleave the 28S rRNA and the newly discovered Burkholderia lethal factor 1 (BLF1). BLF1 presents additional challenges to the current classification system since, like the ribotoxins, it does not possess RNA N-glycosidase activity but does irreversibly inactivate ribosomes. We further discuss whether the RIP classification should be broadened to include toxins achieving irreversible ribosome inactivation with similar turnovers to RIPs, but through different enzymatic mechanisms.
AbstractList Ribosome-inactivating proteins (RIPs) were first isolated over a century ago and have been shown to be catalytic toxins that irreversibly inactivate protein synthesis. Elucidation of atomic structures and molecular mechanism has revealed these proteins to be a diverse group subdivided into two classes. RIPs have been shown to exhibit RNA N -glycosidase activity and depurinate the 28S rRNA of the eukaryotic 60S ribosomal subunit. In this review, we compare archetypal RIP family members with other potent toxins that abolish protein synthesis: the fungal ribotoxins which directly cleave the 28S rRNA and the newly discovered Burkholderia lethal factor 1 (BLF1). BLF1 presents additional challenges to the current classification system since, like the ribotoxins, it does not possess RNA N -glycosidase activity but does irreversibly inactivate ribosomes. We further discuss whether the RIP classification should be broadened to include toxins achieving irreversible ribosome inactivation with similar turnovers to RIPs, but through different enzymatic mechanisms.
Ribosome-inactivating proteins (RIPs) were first isolated over a century ago and have been shown to be catalytic toxins that irreversibly inactivate protein synthesis. Elucidation of atomic structures and molecular mechanism has revealed these proteins to be a diverse group subdivided into two classes. RIPs have been shown to exhibit RNA N-glycosidase activity and depurinate the 28S rRNA of the eukaryotic 60S ribosomal subunit. In this review, we compare archetypal RIP family members with other potent toxins that abolish protein synthesis: the fungal ribotoxins which directly cleave the 28S rRNA and the newly discovered Burkholderia lethal factor 1 (BLF1). BLF1 presents additional challenges to the current classification system since, like the ribotoxins, it does not possess RNA N-glycosidase activity but does irreversibly inactivate ribosomes. We further discuss whether the RIP classification should be broadened to include toxins achieving irreversible ribosome inactivation with similar turnovers to RIPs, but through different enzymatic mechanisms.
Author Hautbergue, Guillaume M
Dodd, Jennifer E
Walsh, Matthew J
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Issue 8
Keywords abrin
biological weapon
ricin
BPSL1549
analytical and therapeutic applications
α-sarcin
BLF1
Shiga toxins
saporin
eukaryotic protein synthesis inhibition
Language English
License open-access: http://creativecommons.org/licenses/by-nc/3.0/: This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.
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Snippet Ribosome-inactivating proteins (RIPs) were first isolated over a century ago and have been shown to be catalytic toxins that irreversibly inactivate protein...
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pubmed
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Publisher
StartPage 774
SubjectTerms abrin
analytical and therapeutic applications
Bacterial Toxins - metabolism
biological weapon
BLF1
BPSL1549
eukaryotic protein synthesis inhibition
Humans
Poisons - toxicity
Protein Synthesis Inhibitors - toxicity
Ribosome Inactivating Proteins - toxicity
ricin
RNA, Ribosomal, 28S - metabolism
saporin
Shiga toxins
Special Focus Review
α-sarcin
Subtitle Potent poisons and molecular tools
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Title Ribosome-inactivating proteins
URI https://www.tandfonline.com/doi/abs/10.4161/viru.26399
https://www.ncbi.nlm.nih.gov/pubmed/24071927
https://pubmed.ncbi.nlm.nih.gov/PMC3925711
Volume 4
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