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Bordetella pertussis adenylate cyclase: a toxin with multiple talents
Trends in Microbiology, 1999Bordetella pertussis secretes a calmodulin-activated adenylate cyclase toxin (CyaA) that is able to deliver its amino-terminal catalytic domain into the cytosol of eukaryotic cells. The novelty of the structural organization and conformational flexibility of the CyaA catalytic domain has opened up the way for exploiting this protein as a tool for ...
D, Ladant, A, Ullmann
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Critical Reviews in Microbiology, 2004
Cyclic AMP is a ubiquitous messenger that integrates many processes of the cell. Diverse families of adenylate cyclases and phosphodiesterases stringently regulate the intracellular concentration of cAMP. Any alteration in the cytosolic concentration of cAMP has a profound effect on the various processes of the cell.
Nidhi, Ahuja +2 more
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Cyclic AMP is a ubiquitous messenger that integrates many processes of the cell. Diverse families of adenylate cyclases and phosphodiesterases stringently regulate the intracellular concentration of cAMP. Any alteration in the cytosolic concentration of cAMP has a profound effect on the various processes of the cell.
Nidhi, Ahuja +2 more
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Bordetella Adenylate Cyclase Toxin
Journal of Toxicology: Toxin Reviews, 1987AbstractA major virulence factor of the genus Bordetella is a unique toxin, a secreted adenylate cyclase, which penetrates membranes of mammalian cells resulting in unregulated generation of adenosine 3′:5′-monophosphate (CAMP). In human infections caused by Bordetella pertussis, this toxin, Bordetella Adenylate Cyclase Toxin (BACT), and a second ...
Erica M. Tenbroek, Dennis L. Confer
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Stimulation of Intestinal Adenyl Cyclase by Cholera Toxin
Nature, 1971THE molecular mechanism by which cholera toxin produces a massive loss of water and electrolytes is unknown, but it is clear that an increase in net secretion of approximately isotonic fluid occurs throughout the length of the small intestine1,2. The relative contributions of increased active ion secretion and decreased active ion reabsorption to this ...
G W, Sharp, S, Hynie
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Cholera Toxin and the Adenylate Cyclase-Activating Signal
Journal of Infectious Diseases, 1976Studies with chemically modified cholera toxin derivatives showed that all treatments that decreased the ability of toxin to bind to mouse thymus cells or to polystyrene-coupled GM1 ganglioside caused a concomitant reduction in the toxin's ability to increase adenosine 3':5'-cyclic phosphate (cyclic AMP) in thymus cells and skin vascular permeability ...
J, Holmgren, I, Lönnroth
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Adenylate cyclase toxin (Bordetella sp.)
1997Abstract Adenylate cyclase toxin (ACT or CyaA) is a key virulence factor produced by the human whooping cough agents, 8ordetella pertussis and parapertussis and by the related animal pathogens 8. bronchiseptica and 8. avium (Weiss and Hewlett 1986; Hanski and Coote 1991; Mock and Ullmann 1993).
P Sebo, A Ullmann
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Invasive adenylate cyclase toxin of Bordetella pertussis
Trends in Biochemical Sciences, 1989Bordetella pertussis produces an adenylate cyclase which is a toxin. The enzyme penetrates eukaryotic cells and, upon activation by host calmodulin, generates high levels of intracellular cAMP; as a result bactericidal functions of immune effector cells are considerably impaired.
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Bordetella pertussis adenylate cyclase toxin: a versatile screening tool
Toxicon, 2002The calmodulin-activated adenylate cyclase (AC) toxin is an essential virulence factor of Bordetella pertussis, the causative agent of whooping cough. This toxin has been exploited to devise screening techniques for investigating diverse biological processes. This mini-review describes several such applications.
Dautin, Nathalie +2 more
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Bordetella pertussis Adenylate Cyclase: A Toxin with Multiple Talents
Zentralblatt für Bakteriologie, 1993The adenylate cyclase toxin of Bordetella pertussis is a secreted multifunctional protein, endowed with calmodulin-activated catalytic, haemolytic and cytotoxic activities. Residues and domains involved in different functions have been localized and several permissive sites, able to accommodate insertion of peptides without impairing the different ...
S, Goyard +4 more
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