Phylogenetic Analysis of Proteolytic Acinetobacter Strains Based on the Sequence of Genes Encoding Aminoglycoside 6′-N-Acetyltransferases

Rudant, E.; Bouvet, Philippe; Courvalin, Patrice; Lambert, Thierry

doi:10.1016/s0723-2020(99)80028-9

Cited by 17 publications

(14 citation statements)

References 32 publications

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“…At the same time, the Acinetobacter genus has diverged significantly from other gammaproteobacteria, as highlighted by a phylogenetic tree based on the highly conserved sequences of 16S rRNA genes ( Fig. 1) (116,188,213,222,265,266). As such, Acinetobacter sp.…”

Section: Introductionmentioning

confidence: 99%

Essential Biological Processes of an Emerging Pathogen: DNA Replication, Transcription, and Cell Division in Acinetobacter spp

Robinson

Brzoska

Turner

et al. 2010

Microbiol Mol Biol Rev

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SUMMARY Within the last 15 years, members of the bacterial genus Acinetobacter have risen from relative obscurity to be among the most important sources of hospital-acquired infections. The driving force for this has been the remarkable ability of these organisms to acquire antibiotic resistance determinants, with some strains now showing resistance to every antibiotic in clinical use. There is an urgent need for new antibacterial compounds to combat the threat imposed by Acinetobacter spp. and other intractable bacterial pathogens. The essential processes of chromosomal DNA replication, transcription, and cell division are attractive targets for the rational design of antimicrobial drugs. The goal of this review is to examine the wealth of genome sequence and gene knockout data now available for Acinetobacter spp., highlighting those aspects of essential systems that are most suitable as drug targets. Acinetobacter spp. show several key differences from other pathogenic gammaproteobacteria, particularly in global stress response pathways. The involvement of these pathways in short- and long-term antibiotic survival suggests that Acinetobacter spp. cope with antibiotic-induced stress differently from other microorganisms.

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Section: Introductionmentioning

confidence: 99%

Essential Biological Processes of an Emerging Pathogen: DNA Replication, Transcription, and Cell Division in Acinetobacter spp

Robinson

Brzoska

Turner

et al. 2010

Microbiol Mol Biol Rev

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“…Three classes of aminoglycoside-inactivating enzymes (acetyltransferases, phosphotransferases, and adenylyltransferases) have been identified in Acinetobacter (15). Acinetobacter haemolyticus and related species are intrinsically resistant to aminoglycosides by synthesis of a chromosomally encoded specific N-acetyltransferase [AAC(6Ј)] (14,30). In contrast, aminoglycoside-resistant A. baumannii isolates usually result from the acquisition of genes encoding modifying enzymes (15,33).…”

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confidence: 99%

Resistance-Nodulation-Cell Division-Type Efflux Pump Involved in Aminoglycoside Resistance in Acinetobacter baumannii Strain BM4454

Magnet

Courvalin

Lambert

2001

Antimicrob Agents Chemother

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523

453

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Multidrug-resistant strain Acinetobacter baumannii BM4454 was isolated from a patient with a urinary tract infection. The adeB gene, which encodes a resistance-nodulation-cell division (RND) protein, was detected in this strain by PCR with two degenerate oligodeoxynucleotides. Insertional inactivation of adeB in BM4454, which generated BM4454-1, showed that the corresponding protein was responsible for aminoglycoside resistance and was involved in the level of susceptibility to other drugs including fluoroquinolones, tetracyclines, chloramphenicol, erythromycin, trimethoprim, and ethidium bromide. Study of ethidium bromide accumulation in BM4454 and BM4454-1, in the presence or in the absence of carbonyl cyanide m-chlorophenylhydrazone, demonstrated that AdeB was responsible for the decrease in intracellular ethidium bromide levels in a proton motive force-dependent manner. The adeB gene was part of a cluster that included adeA and adeC which encodes proteins homologous to membrane fusion and outer membrane proteins of RND-type three-component efflux systems, respectively. The products of two upstream open reading frames encoding a putative twocomponent regulatory system might be involved in the regulation of expression of the adeABC gene cluster.

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“…Three different types of enzymatic modification of the drug include O-phosphorylation, O-nucleotidylation, and N-acetylation. Expression of genes encoding these enzymes is either by acquisition of foreign DNA (plasmid-borne) or by overexpression of a housekeeping gene with modifying activity (13)(14)(15). Aminoglycoside N-acetyltransferases (AACs) 1 use acetyl-coenzyme A (acetyl-CoA) as the acetyl group donor and are grouped into four classes: AAC(1), AAC(2Ј), AAC (3), and AAC(6Ј) based on the site of their regioselective acetylation of the aminoglycoside.…”

mentioning

confidence: 99%

Overexpression and Mechanistic Analysis of Chromosomally Encoded Aminoglycoside 2′-N-Acetyltransferase (AAC(2′)-Ic) fromMycobacterium tuberculosis

Hegde

Javid-Majd²,

Blanchard

2001

Journal of Biological Chemistry

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Phylogenetic Analysis of Proteolytic Acinetobacter Strains Based on the Sequence of Genes Encoding Aminoglycoside 6′-N-Acetyltransferases

Cited by 17 publications

References 32 publications

Essential Biological Processes of an Emerging Pathogen: DNA Replication, Transcription, and Cell Division in Acinetobacter spp

Essential Biological Processes of an Emerging Pathogen: DNA Replication, Transcription, and Cell Division in Acinetobacter spp

Resistance-Nodulation-Cell Division-Type Efflux Pump Involved in Aminoglycoside Resistance in Acinetobacter baumannii Strain BM4454

Overexpression and Mechanistic Analysis of Chromosomally Encoded Aminoglycoside 2′-N-Acetyltransferase (AAC(2′)-Ic) fromMycobacterium tuberculosis

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