Base de dados : LILACS
Pesquisa : D08.811.913.696.445 [Categoria DeCS]
Referências encontradas : 4 [refinar]
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Id: lil-769825
Autor: Cavalcanti, Felipe Lira de Sá; Mirones, Cristina Rodríguez; Paucar, Elena Román; Montes, Laura Álvarez; Leal-Balbino, Tereza Cristina; Morais, Marcia Maria Camargo de; Martínez-Martínez, Luis; Ocampo-Sosa, Alain Antonio.
Título: Mutational and acquired carbapenem resistance mechanisms in multidrug resistant Pseudomonas aeruginosa clinical isolates from Recife, Brazil
Fonte: Mem. Inst. Oswaldo Cruz;110(8):1003-1009, Dec. 2015. tab, graf.
Idioma: en.
Projeto: REIPI; . SNS Miguel Servet.
Resumo: An investigation was carried out into the genetic mechanisms responsible for multidrug resistance in nine carbapenem-resistant Pseudomonas aeruginosaisolates from different hospitals in Recife, Brazil. Susceptibility to antimicrobial agents was determined by broth microdilution. Polymerase chain reaction (PCR) was employed to detect the presence of genes encoding β-lactamases, aminoglycoside-modifying enzymes (AMEs), 16S rRNA methylases, integron-related genes and OprD. Expression of genes coding for efflux pumps and AmpC cephalosporinase were assessed by quantitative PCR. The outer membrane proteins were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The blaSPM-1, blaKPC-2 and blaGES-1 genes were detected in P. aeruginosaisolates in addition to different AME genes. The loss of OprD in nine isolates was mainly due to frameshift mutations, premature stop codons and point mutations. An association of loss of OprD with the overexpression of MexAB-OprM and MexXY-OprM was observed in most isolates. Hyper-production of AmpC was also observed in three isolates. Clonal relationship of the isolates was determined by repetitive element palindromic-PCR and multilocus sequence typing. Our results show that the loss of OprD along with overexpression of efflux pumps and β-lactamase production were responsible for the multidrug resistance in the isolates analysed.
Descritores: Carbapenêmicos/metabolismo
Farmacorresistência Bacteriana Múltipla/genética
Mutação
Pseudomonas aeruginosa/efeitos dos fármacos
Pseudomonas aeruginosa/genética
Resistência beta-Lactâmica/genética
beta-Lactamases/metabolismo
-Aminoglicosídeos/metabolismo
Anfotericina B/análogos & derivados
Anfotericina B/metabolismo
Antifúngicos/metabolismo
Brasil
Cefalosporinase/classificação
Cefalosporinase/metabolismo
Códon sem Sentido/metabolismo
Ativação Enzimática/genética
Mutação da Fase de Leitura/genética
Regulação Bacteriana da Expressão Gênica/genética
Proteínas de Membrana Transportadoras/metabolismo
Metiltransferases/metabolismo
Nucleotidiltransferases/metabolismo
Mutação Puntual/genética
Porinas/metabolismo
Pseudomonas aeruginosa/enzimologia
Pseudomonas aeruginosa/isolamento & purificação
Sequências Repetitivas de Ácido Nucleico
beta-Lactamases/genética
Limites: Seres Humanos
Tipo de Publ: Research Support, Non-U.S. Gov't
Responsável: BR1.1 - BIREME


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Id: lil-604286
Autor: Vaziri, Farzam; Peerayeh, Shahin Najar; Nejad, Qorban Behzadian; Farhadian, Abbas.
Título: The prevalence of aminoglycoside-modifying enzyme genes (aac (6')-I, aac (6')-II, ant (2")-I, aph (3')-VI) in Pseudomonas aeruginosa
Fonte: Clinics;66(9):1519-1522, 2011. ilus, tab.
Idioma: en.
Resumo: INTRODUCTION: Pseudomonas aeruginosa (P. aeruginosa) is one of the primary opportunistic pathogens responsible for nosocomial infections. Aminoglycosides are an import ant component of antipseudomonal chemotherapy. The inactivation of drugs by modifying enzymes is the most common mechanism of aminoglycoside resistance. OBJECTIVES: The inactivation of aminoglycosides by modifying enzymes is the primary resistance mechanism employed by P. aeruginosa. The aim of the present study was to investigate the occurrence of aminoglycoside resistance and the prevalence of four import ant modifying enzyme genes (aac (6')-I, aac (6')-II, ant (2")-I, aph (3')-VI) in P. aeruginosa in Iran. METHODS: A total of 250 clinical isolates of P. aeruginosa were collected from several hospitals in seven cities in Iran. Antimicrobial susceptibility tests (using the disk diffusion method and E-tests) were performed for all 250 isolates. In addition, all isolates were screened for the presence of modifying enzyme genes by polymerase chain reaction. RESULTS: The resistance rates, as determined by the disk diffusion method, were as follows: gentamicin 43 percent, tobramycin 38 percent, and amikacin 24 percent. Of the genes examined, aac (6')-II (36 percent) was the most frequently identified gene in phenotypic resist ant isolates, followed by ant (2")-I, aph (3')-VI, and aac (6')-I. CONCLUSIONS: Aminoglycoside resistance in P. aeruginosa remains a signific ant problem in Iran. Therefore, there is considerable local surveillance of aminoglycoside resistance.
Descritores: Acetiltransferases/genética
Aminoglicosídeos/farmacologia
Antibacterianos/farmacologia
Farmacorresistência Bacteriana/genética
Canamicina Quinase/genética
Nucleotidiltransferases/genética
Pseudomonas aeruginosa/genética
-Aminoglicosídeos/metabolismo
Antibacterianos/metabolismo
DNA Bacteriano/genética
Farmacorresistência Bacteriana/efeitos dos fármacos
Irã (Geográfico)
Pseudomonas aeruginosa/efeitos dos fármacos
Limites: Feminino
Seres Humanos
Masculino
Tipo de Publ: Research Support, Non-U.S. Gov't
Responsável: BR1.1 - BIREME


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Id: lil-479679
Autor: Araújo, L. M; Huergo, L. F; Invitti, A. L; Gimenes, C. I; Bonatto, A. C; Monteiro, R. A; Souza, E. M; Pedrosa, F. O; Chubatsu, L. S.
Título: Different responses of the GlnB and GlnZ proteins upon in vitro uridylylation by the Azospirillum brasilense GlnD protein
Fonte: Braz. j. med. biol. res = Rev. bras. pesqui. méd. biol;41(4):289-294, Apr. 2008. ilus.
Idioma: en.
Resumo: Azospirillum brasilense is a diazotroph found in association with important agricultural crops. In this organism, the regulation of nitrogen fixation by ammonium ions involves several proteins including the uridylyltransferase/uridylyl-removing enzyme, GlnD, which reversibly uridylylates the two PII proteins, GlnB and GlnZ, in response to the concentration of ammonium ions. In the present study, the uridylylation/deuridylylation cycle of A. brasilense GlnB and GlnZ proteins by GlnD was reconstituted in vitro using the purified proteins. The uridylylation assay was analyzed using non-denaturing polyacrylamide gel electrophoresis and fluorescent protein detection. Our results show that the purified A. brasilense GlnB and GlnZ proteins were uridylylated by the purified A. brasilense GlnD protein in a process dependent on ATP and 2-oxoglutarate. The dependence on ATP for uridylylation was similar for both proteins. On the other hand, at micromolar concentration of 2-oxoglutarate (up to 100 µM), GlnB uridylylation was almost twice that of GlnZ, an effect that was not observed at higher concentrations of 2-oxoglutarate (up to 10 mM). Glutamine inhibited uridylylation and stimulated deuridylylation of both GlnB and GlnZ. However, glutamine seemed to inhibit GlnZ uridylylation more efficiently. Our results suggest that the differences in the uridylylation pattern of GlnB and GlnZ might be important for fine-tuning of the signaling pathway of cellular nitrogen status in A. brasilense.
Descritores: Azospirillum brasilense/metabolismo
Proteínas de Bactérias/metabolismo
-Azospirillum brasilense/genética
Proteínas de Bactérias/genética
Eletroforese em Gel de Poliacrilamida
Escherichia coli/genética
Escherichia coli/metabolismo
Nucleotidiltransferases
Proteínas PII Reguladoras de Nitrogênio/genética
Proteínas PII Reguladoras de Nitrogênio/metabolismo
Plasmídeos/genética
Transdução de Sinais
Limites: Seres Humanos
Tipo de Publ: Research Support, Non-U.S. Gov't
Responsável: BR1.1 - BIREME


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Id: lil-29121
Autor: Broussain, Maria Teresa; Pinto, María Eugenia; Cona, Erna.
Título: Resistencia de bacilos Gram negativos frente a seis aminoglicósidos / Resistance of Gram-negative bacilli to 6 aminoglycosides
Fonte: Rev. méd. Chile;113(12):1210-6, dic. 1985. tab.
Idioma: es.
Descritores: Antibacterianos/farmacologia
Bactérias Gram-Negativas/efeitos dos fármacos
Resistência Microbiana a Medicamentos
-Acetiltransferases/metabolismo
Aminoglicosídeos/farmacologia
Bactérias Gram-Negativas/enzimologia
Nucleotidiltransferases/metabolismo
Fosfotransferases/metabolismo
Plasmídeos
Responsável: BR1.1 - BIREME



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