Legionella pneumophila is an opportunistic pathogen and the causative agent of Legionnaires' disease. Despite being exposed to many chemical compounds in its natural and man-made habitats (natural aquatic biotopes and man-made water systems), L. pneumophila is able to adapt and survive in these environments. The molecular mechanisms by which this bacterium detoxifies these chemicals remain poorly understood. In particular, the expression and functions of XMEs (xenobiotic-metabolizing enzymes) that could contribute to chemical detoxification in L. pneumophila have been poorly documented at the molecular and functional levels. In the present paper we report the identification and biochemical and functional characterization of a unique acetyltransferase that metabolizes aromatic amine chemicals in three characterized clinical strains of L. pneumophila (Paris, Lens and Philadelphia). Strain-specific sequence variations in this enzyme, an atypical member of the arylamine N-acetyltransferase family (EC 2.3.1.5), produce enzymatic variants with different structural and catalytic properties. Functional inactivation and complementation experiments showed that this acetyltransferase allows L. pneumophila to detoxify aromatic amine chemicals and grow in their presence. The present study provides a new enzymatic mechanism by which the opportunistic pathogen L. pneumophila biotransforms and detoxifies toxic aromatic chemicals. These data also emphasize the role of XMEs in the environmental adaptation of certain prokaryotes.
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Research Article|
June 27 2012
Characterization of an acetyltransferase that detoxifies aromatic chemicals in Legionella pneumophila
Xavier Kubiak;
Xavier Kubiak
*Université Paris Diderot, Sorbonne Paris Cité, Unité de Biologie Fonctionnelle et Adaptative, CNRS EAC4413, 75013, Paris, France
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Delphine Dervins-Ravault;
Delphine Dervins-Ravault
†Institut Pasteur, Biologie des Bactéries Intracellulaires, 28, Rue du Dr Roux, Paris, France
‡CNRS UMR 3525, 28, Rue du Dr Roux, Paris, France
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Benjamin Pluvinage;
Benjamin Pluvinage
1
*Université Paris Diderot, Sorbonne Paris Cité, Unité de Biologie Fonctionnelle et Adaptative, CNRS EAC4413, 75013, Paris, France
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Alain F. Chaffotte;
Alain F. Chaffotte
§Institut Pasteur, Unité de Résonance Magnétique Nucléaire des Biomolécules, Paris, France
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Laura Gomez-Valero;
Laura Gomez-Valero
†Institut Pasteur, Biologie des Bactéries Intracellulaires, 28, Rue du Dr Roux, Paris, France
‡CNRS UMR 3525, 28, Rue du Dr Roux, Paris, France
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Julien Dairou;
Julien Dairou
*Université Paris Diderot, Sorbonne Paris Cité, Unité de Biologie Fonctionnelle et Adaptative, CNRS EAC4413, 75013, Paris, France
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Florent Busi;
Florent Busi
*Université Paris Diderot, Sorbonne Paris Cité, Unité de Biologie Fonctionnelle et Adaptative, CNRS EAC4413, 75013, Paris, France
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Jean-Marie Dupret;
Jean-Marie Dupret
*Université Paris Diderot, Sorbonne Paris Cité, Unité de Biologie Fonctionnelle et Adaptative, CNRS EAC4413, 75013, Paris, France
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Carmen Buchrieser;
Carmen Buchrieser
†Institut Pasteur, Biologie des Bactéries Intracellulaires, 28, Rue du Dr Roux, Paris, France
‡CNRS UMR 3525, 28, Rue du Dr Roux, Paris, France
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Fernando Rodrigues-Lima
Fernando Rodrigues-Lima
2
*Université Paris Diderot, Sorbonne Paris Cité, Unité de Biologie Fonctionnelle et Adaptative, CNRS EAC4413, 75013, Paris, France
2To whom correspondence should be addressed (email fernando.rodrigues-lima@univ-paris-diderot.fr).
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Publisher: Portland Press Ltd
Received:
March 27 2012
Revision Received:
April 27 2012
Accepted:
April 30 2012
Accepted Manuscript online:
April 30 2012
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2012 Biochemical Society
2012
Biochem J (2012) 445 (2): 219–228.
Article history
Received:
March 27 2012
Revision Received:
April 27 2012
Accepted:
April 30 2012
Accepted Manuscript online:
April 30 2012
Citation
Xavier Kubiak, Delphine Dervins-Ravault, Benjamin Pluvinage, Alain F. Chaffotte, Laura Gomez-Valero, Julien Dairou, Florent Busi, Jean-Marie Dupret, Carmen Buchrieser, Fernando Rodrigues-Lima; Characterization of an acetyltransferase that detoxifies aromatic chemicals in Legionella pneumophila. Biochem J 15 July 2012; 445 (2): 219–228. doi: https://doi.org/10.1042/BJ20120528
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