Mechanisms of resistance to aminoglycoside antibiotics: overview and perspectives
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TLDR
By far the most widespread mechanism of resistance to AGs is the inactivation of these antibiotics by AG-modifying enzymes, and an overview of these mechanisms is provided.Abstract:
Aminoglycoside (AG) antibiotics are used to treat many Gram-negative and some Gram-positive infections and, importantly, multidrug-resistant tuberculosis. Among various bacterial species, resistance to AGs arises through a variety of intrinsic and acquired mechanisms. The bacterial cell wall serves as a natural barrier for small molecules such as AGs and may be further fortified via acquired mutations. Efflux pumps work to expel AGs from bacterial cells, and modifications here too may cause further resistance to AGs. Mutations in the ribosomal target of AGs, while rare, also contribute to resistance. Of growing clinical prominence is resistance caused by ribosome methyltransferases. By far the most widespread mechanism of resistance to AGs is the inactivation of these antibiotics by AG-modifying enzymes. We provide here an overview of these mechanisms by which bacteria become resistant to AGs and discuss their prevalence and potential for clinical relevance.read more
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References
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Journal Article
Accumulation of plasmid-mediated fluoroquinolone resistance genes, qepA and qnrS1, in Enterobacter aerogenes co-producing RmtB and class A beta-lactamase LAP-1.
TL;DR: Although the prevalence of qepA is currently low, considering the presence of ISCR3C and the possibility of co-selection and co-transferability of plasmids, more active surveillance for these multi-drug resistant bacteria and prudent use of antimicrobials are needed.
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Aminoglycoside resistance 16S rRNA methyltransferases block endogenous methylation, affect translation efficiency and fitness of the host
Virginia S. Lioy,Sylvie Goussard,Vincent Guérineau,Eun-Jeong Yoon,Patrice Courvalin,Marc Galimand,Catherine Grillot-Courvalin +6 more
TL;DR: Compared ArmA and NpmA in isogenic Escherichia coli harboring the corresponding structural genes and their inactive point mutants cloned under the control of their native constitutive promoter in the stable plasmid pGB2 indicate that resistance methyltransferases impair endogenous methylation with different consequences on cell fitness.
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Outbreak of Salmonella enterica serotype Infantis producing ArmA 16S RNA methylase and CTX-M-15 extended-spectrum β-lactamase in a neonatology ward in Constantine, Algeria
Thierry Naas,Chafia Bentchouala,Gaelle Cuzon,Sanàa Yaou,Abdesselam Lezzar,Farida Smati,Patrice Nordmann +6 more
TL;DR: Spread of 16S RNA methylase determinants at the same level as bla(CTX-M) genes in Enterobacteriaceae may seriously compromise the efficacy of aminoglycosides for treating Gram-negative infections.
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Effects of Altering Aminoglycoside Structures on Bacterial Resistance Enzyme Activities
TL;DR: It is demonstrated that the bifunctional enzyme AAC(3-Ib/AAC(6′)-Ib′ can diacetylate gentamicin, suggesting that two modifications likely provide more-robust inactivation in vivo.
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Structural insights into the function of aminoglycoside-resistance A1408 16S rRNA methyltransferases from antibiotic-producing and human pathogenic bacteria
TL;DR: It is proposed that a dynamic extended loop structure that is positioned adjacent to both the bound SAM and a functionally critical structural motif may mediate concerted conformational changes in rRNA and protein that underpin the specificity of target selection and activation of methyltransferase activity.