Characterization of an acetyltransferase that detoxifies aromatic chemicals in Legionella pneumophila

Xavier Jean Philippe Kubiak; Delphine Dervins-Ravault; Benjamin Pluvinage; Alain F Chaffotte; Laura Gomez-Valero; Julien Dairou; Florent Busi; Jean-Marie Dupret; Carmen Buchrieser; Fernando Rodrigues-Lima

doi:10.1042/bj20120528

Characterization of an acetyltransferase that detoxifies aromatic chemicals in Legionella pneumophila

Xavier Jean Philippe Kubiak, Delphine Dervins-Ravault, Benjamin Pluvinage, Alain F Chaffotte, Laura Gomez-Valero, Julien Dairou, Florent Busi, Jean-Marie Dupret, Carmen Buchrieser, Fernando Rodrigues-Lima

Department of Neuroscience

11 Citations (Scopus)

Abstract

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.

Original language	English
Journal	Biochemical Journal
Volume	445
Issue number	2
Pages (from-to)	219-28
Number of pages	10
ISSN	0264-6021
DOIs	https://doi.org/10.1042/bj20120528
Publication status	Published - 15 Jul 2012

Keywords

Amines
Arylamine N-Acetyltransferase
Blotting, Western
Circular Dichroism
Genetic Complementation Test
Genetic Variation
Hydrocarbons, Aromatic
Legionella pneumophila
Legionnaires' Disease
Metabolic Detoxication, Drug
Phylogeny
Protein Folding
Recombinant Proteins

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10.1042/bj20120528

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title = "Characterization of an acetyltransferase that detoxifies aromatic chemicals in Legionella pneumophila",

abstract = "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.",

keywords = "Amines, Arylamine N-Acetyltransferase, Blotting, Western, Circular Dichroism, Genetic Complementation Test, Genetic Variation, Hydrocarbons, Aromatic, Legionella pneumophila, Legionnaires' Disease, Metabolic Detoxication, Drug, Phylogeny, Protein Folding, Recombinant Proteins",

author = "Kubiak, {Xavier Jean Philippe} and Delphine Dervins-Ravault and Benjamin Pluvinage and Chaffotte, {Alain F} and Laura Gomez-Valero and Julien Dairou and Florent Busi and Jean-Marie Dupret and Carmen Buchrieser and Fernando Rodrigues-Lima",

year = "2012",

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T1 - Characterization of an acetyltransferase that detoxifies aromatic chemicals in Legionella pneumophila

AU - Kubiak, Xavier Jean Philippe

AU - Dervins-Ravault, Delphine

AU - Pluvinage, Benjamin

AU - Chaffotte, Alain F

AU - Gomez-Valero, Laura

AU - Dairou, Julien

AU - Busi, Florent

AU - Dupret, Jean-Marie

AU - Buchrieser, Carmen

AU - Rodrigues-Lima, Fernando

PY - 2012/7/15

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N2 - 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.

AB - 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.

KW - Amines

KW - Arylamine N-Acetyltransferase

KW - Blotting, Western

KW - Circular Dichroism

KW - Genetic Complementation Test

KW - Genetic Variation

KW - Hydrocarbons, Aromatic

KW - Legionella pneumophila

KW - Legionnaires' Disease

KW - Metabolic Detoxication, Drug

KW - Phylogeny

KW - Protein Folding

KW - Recombinant Proteins

U2 - 10.1042/bj20120528

DO - 10.1042/bj20120528

M3 - Journal article

C2 - 22545684

SN - 0264-6021

VL - 445

SP - 219

EP - 228

JO - Biochemical Journal

JF - Biochemical Journal

IS - 2

ER -

Characterization of an acetyltransferase that detoxifies aromatic chemicals in Legionella pneumophila

Abstract

Keywords

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