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

Toxins

Martin Göttle¹  Stefan Dove² 

[1] Department of Neurology, Emory University School of Medicine, 6302 Woodruff Memorial Research Building, 101 Woodruff Circle, Atlanta, GA 30322, USADepartment of Medicinal/Pharmaceutical Chemistry II, University of Regensburg, D-93040 Regensburg, Germany;

关键词: adenylyl cyclase toxin;    anthrax;    Bacillus anthracis;    edema factor;    edema toxin;   

DOI  :  10.3390/toxins4070505

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2012 by the authors; licensee MDPI, Basel, Switzerland.