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1.
J Antimicrob Chemother ; 77(7): 1838-1846, 2022 06 29.
Artigo em Inglês | MEDLINE | ID: mdl-35425984

RESUMO

BACKGROUND: Resistance to linezolid has become a worldwide concern since it is one of the last-resort antibiotics to treat multidrug-resistant staphylococcal and enterococcal infections. OBJECTIVES: We investigated staphylococcal infections caused by 16 cfr-positive linezolid-resistant Staphylococcus epidermidis and Staphylococcus aureus isolates in a French university hospital from 2015 to 2018. METHODS: Antimicrobial susceptibility of isolates was tested by broth microdilution and gradient strips. Genetic determinants of linezolid resistance (including cfr gene and 23S rRNA mutations) were assessed by PCR and WGS; the latter was also used to characterize the cfr-carrying plasmids in S. epidermidis and S. aureus, and to explore the clonal relationship of isolates. RESULTS: All linezolid-resistant staphylococcal isolates harboured the same cfr-carrying plasmid, sharing 99% identity with the previously described pSA737. The three S. aureus isolates belonged to different STs (ST8, ST72, ST2416); the 13 methicillin-resistant S. epidermidis (MRSE) belonged to ST2 and harboured both cfr and mutations in genes encoding 23S rRNA and ribosomal proteins. Phylogenetic analysis grouped the MRSE isolates into two clusters, one of which (n = 12 isolates) belonged to the recently reported multidrug-resistant worldwide-disseminated S. epidermidis lineages. CONCLUSIONS: The results presented herein highlight the persistence and efficient spread of a cfr-carrying plasmid in a hospital related both to the dissemination of a multidrug-resistant S. epidermidis clone and the in vivo interspecies transfer of cfr between S. epidermidis and S. aureus. The emergence of linezolid-resistant strains should be closely monitored, and the mechanisms involved systematically explored in order to limit the spread of plasmid-mediated resistance.


Assuntos
Staphylococcus aureus Resistente à Meticilina , Infecções Estafilocócicas , Antibacterianos/farmacologia , Células Clonais , Hospitais , Humanos , Linezolida/farmacologia , Resistência a Meticilina , Testes de Sensibilidade Microbiana , Filogenia , RNA Ribossômico 23S/genética , Staphylococcus , Staphylococcus aureus , Staphylococcus epidermidis
2.
Antimicrob Agents Chemother ; 51(6): 2179-84, 2007 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-17420213

RESUMO

By studying the beta-lactamase content of several Acinetobacter spp. isolates from Argentina, producing the expanded-spectrum beta-lactamases (ESBL) VEB-1a or PER-2, a novel Ambler class A beta-lactamase gene was identified. It encoded the narrow-spectrum beta-lactamase SCO-1, whose activity was inhibited by clavulanic acid. SCO-1 hydrolyzes penicillins at a high level and cephalosporins and carbapenems at a very low level. beta-Lactamase SCO-1 was identified from unrelated VEB-1a-positive or PER-2-positive Acinetobacter spp. isolates recovered from three hospitals. The bla(SCO-1) gene was apparently located on a plasmid of ca. 150 kb from all cases but was not associated with any ESBL-encoding gene. The G+C content of the bla(SCO) gene was 52%, a value that does not correspond to that of the A. baumannii genome (39%). beta-Lactamase SCO-1 shares 47% amino acid identity with CARB-5 and ca. 40% with the enzymes TEM, SHV, and CTX-M. A gene encoding a putative resolvase was identified downstream of the bla(SCO-1) gene, but its precise way of acquisition remains to be determined.


Assuntos
Acinetobacter/efeitos dos fármacos , Acinetobacter/enzimologia , Antibacterianos/farmacologia , Resistência beta-Lactâmica , beta-Lactamases , beta-Lactamas/farmacologia , Acinetobacter/classificação , Acinetobacter/genética , Infecções por Acinetobacter/microbiologia , Sequência de Aminoácidos , Argentina , Ácido Clavulânico/metabolismo , Ácido Clavulânico/farmacologia , Clonagem Molecular , Humanos , Testes de Sensibilidade Microbiana , Dados de Sequência Molecular , Análise de Sequência de DNA , beta-Lactamases/química , beta-Lactamases/genética , beta-Lactamases/isolamento & purificação , beta-Lactamases/metabolismo
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