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Journal of Bacteriology, November 2005, p. 7579-7588, Vol. 187, No. 22
0021-9193/05/$08.00+0     doi:10.1128/JB.187.22.7579-7588.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Adenylate Cyclase Toxin (ACT) from Bordetella hinzii: Characterization and Differences from ACT of Bordetella pertussis

Gina M. Donato, Hung-Lun J. Hsia, Candace S. Green, and Erik L. Hewlett*

Division of Infectious Diseases and International Health, Departments of Medicine and Pharmacology, University of Virginia School of Medicine, Charlottesville, Virginia 22908

Received 6 May 2005/ Accepted 6 September 2005

Bordetella hinzii is a commensal respiratory microorganism in poultry but is increasingly being recognized as an opportunistic pathogen in immunocompromised humans. Although associated with a variety of disease states, practically nothing is known about the mechanisms employed by this bacterium. In this study, we show by DNA sequencing and reverse transcription-PCR that both commensal and clinical strains of B. hinzii possess and transcriptionally express cyaA, the gene encoding adenylate cyclase toxin (ACT) in other pathogenic Bordetella species. By Western blotting, we also found that B. hinzii produces full-length ACT protein in quantities that are comparable to those made by B. pertussis. In contrast to B. pertussis ACT, however, ACT from B. hinzii is less extractable from whole bacteria, nonhemolytic, has a 50-fold reduction in adenylate cyclase activity, and is unable to elevate cyclic AMP levels in host macrophages (nontoxic). The decrease in enzymatic activity is attributable, at least in part, to a decreased binding affinity of B. hinzii ACT for calmodulin, the eukaryotic activator of B. pertussis ACT. In addition, we demonstrate that the lack of intoxication by B. hinzii ACT may be due to the absence of expression of cyaC, the gene encoding the accessory protein required for the acylation of B. pertussis ACT. These results demonstrate the expression of ACT by B. hinzii and represent the first characterization of a potential virulence factor of this organism.

* Corresponding author, Mailing address: Box 800419, University of Virginia School of Medicine, Charlottesville, VA 22908. Phone: (434) 924-5945. Fax: (434) 982-3830. E-mail: eh2v{at}virginia.edu.

Journal of Bacteriology, November 2005, p. 7579-7588, Vol. 187, No. 22
0021-9193/05/$08.00+0     doi:10.1128/JB.187.22.7579-7588.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.





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