Nucleotide sequence analysis of a gene encoding a streptomycin/spectinomycin adenyltransferase

Hollingshead, Susan K.; Vapnek, Daniel

doi:10.1016/0147-619x(85)90052-6

Cited by 198 publications

(151 citation statements)

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“…The ant(3')-Ia and ant(6)-Ia genes encode streptomycin resistance [42,53]. The ant(3')-Ia gene (ANT(3')-I) is commonly found in Gram-negative bacterial species, whereas the ant(6)-Ia gene (ANT(6)-I) has mainly been found in staphylococci [25,42,53]. The sat4 gene encoding resistance to streptothricins has been observed in C. coli of different animal and clinical sources in Germany [6,8].…”

Section: Aminoglycoside Resistancementioning

confidence: 99%

Antimicrobial resistance of thermophilic Campylobacter

Aarestrup¹,

2001

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-Campylobacter has become the leading cause of zoonotic enteric infections in developed and developing countries world-wide. Antimicrobial resistance has emerged among Campylobacter mainly as a consequence of the use of antimicrobial agents in food animal production. Resistance to drugs of choice for the treatment of infections, macrolides and fluoroquinolones has emerged as a clinical problem and interventions to reduce this are recommended. Resistance to fluoroquinolones and macrolides is mediated by chromosomal mutations. Resistance to other relevant antimicrobial agents, mediated by acquired resistance genes, has not become widespread so far. However, resistance genes originating from both Gram-positive and Gram-negative bacterial species have been found, showing the potential for acquired resistance to emerge in Campylobacter.Campylobacter / resistance / susceptibility testing / trends / gene Résumé -Résistance aux antimicrobiens chez Campylobacter thermophile. Campylobacter est devenu la cause principale de zoonoses entériques infectieuses dans les pays développés et en voie de développement à travers le monde. La résistance aux antibiotiques a émergé chez Campylobacter, principalement à cause de l'utilisation d'antibiotiques chez les animaux entrant dans la chaîne alimentaire. La résistance aux antibiotiques principalement utilisés dans le traitement des infections, les macrolides et les fluoroquinolones, a émergé en tant que problème clinique, et les interventions visant à réduire cette résistance sont recommandées. La résistance aux fluoroquinolones et aux macrolides est due à des mutations chromosomiques. La résistance aux autres antibiotiques utilisables, qui est due à l'acquisition de gènes de résistance, ne s'est jusqu'à maintenant pas propagée. Cependant, le fait qu'il ait été trouvé des gènes de résistance ayant pour origine des espèces bactériennes à Gram-positif et à Gram-négatif, montre la possibilité d'émergence de résistance acquise chez Campylobacter.Campylobacter / résistance / test de sensibilité / tendance / gène Vet. Res. 32 (2001) 311-321 311

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Section: Aminoglycoside Resistancementioning

confidence: 99%

Antimicrobial resistance of thermophilic Campylobacter

Aarestrup¹,

2001

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“…It is difficult to explain the formation of these elements by the same mechanisms as class I compound elements (Schmitt et al, 1985). DNA sequencing (Zolg and Hanggi, 1981;Swift et al, 1981;Dale et al, 1985;Hollingshead and Vapnek, 1985;Tait et al, 1985;Cameron et al, 1986;Hall and Vockler, 1987 Tenover et al, 1988) showed that new Abr genes are inserted in either one of two specific DNA sites, which act as recombination hot-spots (RHSs) and are located at both ends of the aadA gene. We determined that Tn2J codes for a site-specific integration system which may allow the acquisition of new Abr genes .…”

Section: Introductionmentioning

confidence: 99%

Genetic elements involved in Tn21 site-specific integration, a novel mechanism for the dissemination of antibiotic resistance genes.

1990

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Transposon Tn2l codes for a site-specific integration system, which is probably a novel recombination mechanism, responsible for the acquisition of resistance genes in this widespread family of transposons. Using insertion and deletion mutagenesis we have identified the genetic loci of the various recombination hot-spots (RHS) and of the gene product (the integrase) that catalyses the reaction. The site of recombination has been localized in two of the RHSs to the DNA sequence GTTAG, which is present at the 3' terminm of a loosely conserved palindromic sequence of -59 bp. This 59 bp sequence, which flanks the inserted genes in a number of naturally occurring transposons, is the only element required in cis for the recombination reaction.

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“…Two enzyme families that confer this resistance are distributed in both Gram-negative and Gram-positive organisms. The enzyme ANT(3Љ,9) is distributed among the Enterobacteriaceae and confers resistance to both Spec and streptomycin (7), whereas ANT(9)-Ia and -Ib are exclusive Spec adenylyltransferases found in Staphylococcus aureus (8) and Enterococcus faecalis (9), respectively. Recently, another Spec kinase gene, spcN, was cloned from the Spec producing organism Streptomyces flavopersicus (10).…”

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confidence: 99%

Spectinomycin Kinase from Legionella pneumophila

Thompson

Hughes

Cianciotto

et al. 1998

Journal of Biological Chemistry

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The bacterium Legionella pneumophila is the responsible agent for Legionnaires' disease and has recently been shown to harbor a gene encoding a kinase that confers resistance to the aminoglycoside antibiotic spectinomycin (Suter, T. M., Viswanathan, V. K., and Cianciotto, N. P. (1997) Antimicrob. Agents Chemother. 41, 1385-1388). We report the overproduction, purification, and characterization of this spectinomycin kinase from an expressing system in Escherichia coli. The purified protein shows stringent substrate specificity for spectinomycin with K m ‫؍‬ 21.5 M and k cat ‫؍‬ 24.2 s ؊1 and does not bind other aminoglycosides including kanamycin, amikacin, neomycin, butirosin, streptomycin, or apramycin. Purification of spectinomycin phosphate followed by characterization by mass spectrometry and 1 H, 13 C, and 31 P NMR established the site of phosphorylation to be at the hydroxyl group at position 9. Thus this enzyme is designated APH(9)-Ia (where APH is aminoglycoside kinase). The enzyme was inactivated by the electrophilic ATP analogue 5-[p-(fluorosulfonyl)benzoyl]adenosine, consistent with a nucleophilic residue such as Lys lining the nucleotide binding pocket. Sitedirected mutagenesis of Lys-52 and Asp-212 to Ala confirmed that these residues were important for catalysis, with Lys-52 playing a potential role in ATP binding and Asp-212 in phosphoryl transfer. Thio and solvent isotope effect experiments in the presence of either Mg 2؉ or Mn 2؉ were consistent with a kinetic mechanism in which phosphate transfer does not contribute significantly to the rate-limiting step. These results establish that APH(9)-Ia is a highly specific antibiotic resistance kinase and provides the requisite mechanistic information for future structural studies.

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Nucleotide sequence analysis of a gene encoding a streptomycin/spectinomycin adenyltransferase

Cited by 198 publications

References 50 publications

Antimicrobial resistance of thermophilic Campylobacter

Antimicrobial resistance of thermophilic Campylobacter

Genetic elements involved in Tn21 site-specific integration, a novel mechanism for the dissemination of antibiotic resistance genes.

Spectinomycin Kinase from Legionella pneumophila

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