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Toxins (Basel). 2012 Jul;4(7):505-35. doi: 10.3390/toxins4070505. Epub 2012 Jul 6.

Bacillus anthracis edema factor substrate specificity: evidence for new modes of action.

Author information

1
Department of Neurology, Emory University School of Medicine, Atlanta, GA 30322, USA. Mgoettl@emory.edu

Abstract

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.

KEYWORDS:

Bacillus anthracis; adenylyl cyclase toxin; anthrax; edema factor; edema toxin

PMID:
22852066
PMCID:
PMC3407890
DOI:
10.3390/toxins4070505
[Indexed for MEDLINE]
Free PMC Article
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