Membrane Depolarization Prevents Cell Invasion by Bordetella pertussis Adenylate Cyclase Toxin

Adenylate cyclase toxin from Bordetella pertussis is a 177-kDa calmodulin-activated enzyme that has the ability to enter eukaryotic cells and convert endogenous ATP into cAMP. Little is known, however, about the mechanism of cell entry. We now demonstrate that intoxication of cardiac myocytes by ade...

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Bibliographic Details
Published inThe Journal of biological chemistry Vol. 270; no. 17; pp. 9695 - 9697
Main Authors Otero, A S, Yi, X B, Gray, M C, Szabo, G, Hewlett, E L
Format Journal Article
LanguageEnglish
Published United States American Society for Biochemistry and Molecular Biology 28.04.1995
Subjects
Adenylate Cyclase Toxin
Animals
Atrial Function
Bordetella pertussis
Bordetella pertussis - enzymology
Heart Atria - cytology
Heart Atria - drug effects
In Vitro Techniques
Membrane Potentials - physiology
Rana catesbeiana
Virulence Factors, Bordetella - toxicity
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Summary:Adenylate cyclase toxin from Bordetella pertussis is a 177-kDa calmodulin-activated enzyme that has the ability to enter eukaryotic cells and convert endogenous ATP into cAMP. Little is known, however, about the mechanism of cell entry. We now demonstrate that intoxication of cardiac myocytes by adenylate cyclase toxin is driven and controlled by the electrical potential across the plasma membrane. The steepness of the voltage dependence of intoxication is comparable with that previously observed for the activation of K and Na channels of excitable membranes. The voltage-sensitive process is downstream from toxin binding to the cell surface and appears to correspond to the translocation of the catalytic domain across the membrane.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.270.17.9695