<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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Format: | Article |
Language: | English |
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MDPI AG
2012-07-01
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Series: | Toxins |
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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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format | Article |
id | doaj.art-8dd829414ced41c398182c5e0433e480 |
institution | Directory Open Access Journal |
issn | 2072-6651 |
language | English |
last_indexed | 2024-04-12T19:24:09Z |
publishDate | 2012-07-01 |
publisher | MDPI AG |
record_format | Article |
series | Toxins |
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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