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Bacillus anthracis Edema Factor Substrate Specificity: Evidence for New Modes of Action

Since the isolation of Bacillus anthracis exotoxins in the 1960s, the detrimental activity of edema factor (EF) was considered as adenylyl cyclase activity only. Yet the catalytic site of EF was recently shown to accomplish cyclization of cytidine 5′-triphosphate, uridine 5′-triphosphate and inosine...

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Detalles Bibliográficos
Autores principales: Göttle, Martin, Dove, Stefan, Seifert, Roland
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3407890/
https://www.ncbi.nlm.nih.gov/pubmed/22852066
http://dx.doi.org/10.3390/toxins4070505
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author Göttle, Martin
Dove, Stefan
Seifert, Roland
author_facet Göttle, Martin
Dove, Stefan
Seifert, Roland
author_sort Göttle, Martin
collection PubMed
description Since the isolation of Bacillus anthracis exotoxins in the 1960s, the detrimental activity of edema factor (EF) was considered as adenylyl cyclase activity only. Yet the catalytic site of EF was recently shown to accomplish cyclization of cytidine 5′-triphosphate, uridine 5′-triphosphate and inosine 5′-triphosphate, in addition to adenosine 5′-triphosphate. This review discusses the broad EF substrate specificity and possible implications of intracellular accumulation of cyclic cytidine 3′:5′-monophosphate, cyclic uridine 3′:5′-monophosphate and cyclic inosine 3′:5′-monophosphate on cellular functions vital for host defense. In particular, cAMP-independent mechanisms of action of EF on host cell signaling via protein kinase A, protein kinase G, phosphodiesterases and CNG channels are discussed.
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spelling pubmed-34078902012-07-31 Bacillus anthracis Edema Factor Substrate Specificity: Evidence for New Modes of Action Göttle, Martin Dove, Stefan Seifert, Roland Toxins (Basel) Review Since the isolation of Bacillus anthracis exotoxins in the 1960s, the detrimental activity of edema factor (EF) was considered as adenylyl cyclase activity only. Yet the catalytic site of EF was recently shown to accomplish cyclization of cytidine 5′-triphosphate, uridine 5′-triphosphate and inosine 5′-triphosphate, in addition to adenosine 5′-triphosphate. This review discusses the broad EF substrate specificity and possible implications of intracellular accumulation of cyclic cytidine 3′:5′-monophosphate, cyclic uridine 3′:5′-monophosphate and cyclic inosine 3′:5′-monophosphate on cellular functions vital for host defense. In particular, cAMP-independent mechanisms of action of EF on host cell signaling via protein kinase A, protein kinase G, phosphodiesterases and CNG channels are discussed. MDPI 2012-07-06 /pmc/articles/PMC3407890/ /pubmed/22852066 http://dx.doi.org/10.3390/toxins4070505 Text en © 2012 by the authors; licensee MDPI, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0/ This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Review
Göttle, Martin
Dove, Stefan
Seifert, Roland
Bacillus anthracis Edema Factor Substrate Specificity: Evidence for New Modes of Action
title Bacillus anthracis Edema Factor Substrate Specificity: Evidence for New Modes of Action
title_full Bacillus anthracis Edema Factor Substrate Specificity: Evidence for New Modes of Action
title_fullStr Bacillus anthracis Edema Factor Substrate Specificity: Evidence for New Modes of Action
title_full_unstemmed Bacillus anthracis Edema Factor Substrate Specificity: Evidence for New Modes of Action
title_short Bacillus anthracis Edema Factor Substrate Specificity: Evidence for New Modes of Action
title_sort bacillus anthracis edema factor substrate specificity: evidence for new modes of action
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3407890/
https://www.ncbi.nlm.nih.gov/pubmed/22852066
http://dx.doi.org/10.3390/toxins4070505
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