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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...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2012
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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. |
format | Online Article Text |
id | pubmed-3407890 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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