<em>Bacillus anthracis</em> Edema Factor Substrate Specificity: Evidence for New Modes of Action

Since the isolation of <em>Bacillus anthracis</em> 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...

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Main Authors: Roland Seifert, Stefan Dove, Martin Göttle
Format: Article
Language:English
Published: MDPI AG 2012-07-01
Series:Toxins
Subjects:
Online Access:http://www.mdpi.com/2072-6651/4/7/505
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author Roland Seifert
Stefan Dove
Martin Göttle
author_facet Roland Seifert
Stefan Dove
Martin Göttle
author_sort Roland Seifert
collection DOAJ
description Since the isolation of <em>Bacillus anthracis</em> 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 doaj.art-8dd829414ced41c398182c5e0433e4802022-12-22T03:19:31ZengMDPI AGToxins2072-66512012-07-014750553510.3390/toxins4070505<em>Bacillus anthracis</em> Edema Factor Substrate Specificity: Evidence for New Modes of ActionRoland SeifertStefan DoveMartin GöttleSince the isolation of <em>Bacillus anthracis</em> 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.http://www.mdpi.com/2072-6651/4/7/505adenylyl cyclase toxinanthrax<em>Bacillus anthracis</em><em> </em>edema factor<em> </em>edema toxin
spellingShingle Roland Seifert
Stefan Dove
Martin Göttle
<em>Bacillus anthracis</em> Edema Factor Substrate Specificity: Evidence for New Modes of Action
Toxins
adenylyl cyclase toxin
anthrax
<em>Bacillus anthracis</em>
<em> </em>edema factor
<em> </em>edema toxin
title <em>Bacillus anthracis</em> Edema Factor Substrate Specificity: Evidence for New Modes of Action
title_full <em>Bacillus anthracis</em> Edema Factor Substrate Specificity: Evidence for New Modes of Action
title_fullStr <em>Bacillus anthracis</em> Edema Factor Substrate Specificity: Evidence for New Modes of Action
title_full_unstemmed <em>Bacillus anthracis</em> Edema Factor Substrate Specificity: Evidence for New Modes of Action
title_short <em>Bacillus anthracis</em> Edema Factor Substrate Specificity: Evidence for New Modes of Action
title_sort lt em gt bacillus anthracis lt em gt edema factor substrate specificity evidence for new modes of action
topic adenylyl cyclase toxin
anthrax
<em>Bacillus anthracis</em>
<em> </em>edema factor
<em> </em>edema toxin
url http://www.mdpi.com/2072-6651/4/7/505
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AT stefandove ltemgtbacillusanthracisltemgtedemafactorsubstratespecificityevidencefornewmodesofaction
AT martingottle ltemgtbacillusanthracisltemgtedemafactorsubstratespecificityevidencefornewmodesofaction