Base de dados : MEDLINE
Pesquisa : D04.345.566.802.500 [Categoria DeCS]
Referências encontradas : 4 [refinar]
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[Au] Autor:Kadlec K; Pomba CF; Couto N; Schwarz S
[Ti] Título:Small plasmids carrying vga(A) or vga(C) genes mediate resistance to lincosamides, pleuromutilins and streptogramin A antibiotics in methicillin-resistant Staphylococcus aureus ST398 from swine.
[So] Source:J Antimicrob Chemother;65(12):2692-3, 2010 Dec.
[Is] ISSN:1460-2091
[Cp] País de publicação:England
[La] Idioma:eng
[Mh] Termos MeSH primário: Transportadores de Cassetes de Ligação de ATP/genética
Proteínas de Bactérias/genética
Farmacorresistência Bacteriana Múltipla/genética
Staphylococcus aureus Resistente à Meticilina/efeitos dos fármacos
Doenças dos Suínos/microbiologia
[Mh] Termos MeSH secundário: Animais
Staphylococcus aureus Resistente à Meticilina/genética
Testes de Sensibilidade Microbiana
Recombinação Genética
Infecções Estafilocócicas/microbiologia
Infecções Estafilocócicas/veterinária
Estreptogramina Grupo A/farmacologia
[Pt] Tipo de publicação:LETTER
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Bacterial Proteins); 0 (Diterpenes); 0 (Lincosamides); 0 (Streptogramin Group A); 125-65-5 (pleuromutilin); 147995-39-9 (VgA protein, Staphylococcus aureus)
[Em] Mês de entrada:1103
[Cu] Atualização por classe:101110
[Lr] Data última revisão:
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100930
[St] Status:MEDLINE
[do] DOI:10.1093/jac/dkq365

  2 / 4 MEDLINE  
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[Au] Autor:Wang GF; Huang N; Meng ZH; Liu QH
[Ad] Endereço:Shanghai Institute of Pharmaceutical Industry, Shanghai 200437, China.
[Ti] Título:Identification of novel inhibitors of the streptogramin group A acetyltransferase via virtual screening.
[So] Source:Yao Xue Xue Bao;42(1):47-53, 2007 Jan.
[Is] ISSN:0513-4870
[Cp] País de publicação:China
[La] Idioma:eng
[Ab] Resumo:Virginiamycin acetyltransferase D (VatD) plays a vital rule in streptogramins resistance by chemically inactivating streptogramin A. Therefore, it is desirable to discover novel small molecular weight inhibitors of VatD via state-of-the-art virtual screening techniques. This "cocktail" strategy by combining VatD inhibitor with streptogramins may provide new therapeutic opportunity for resistant bacteria infections. Structure-based virtual screening method (molecular docking) was applied to rank and score a chemical database containing 300 000 commercially available compounds against the VatD substrate binding site. Twenty six out of the 200 top scored compounds from the docking calculation were selected and submitted to the VatD enzymatic inhibition assay. The plasmid pRSET B/vatD was constructed and transformed into E. coli (trxB) host cells for over-expression, and VatD enzyme was purified and validated by showing acetyltransferase activity to Virginiamycin M1. Three out of these 26 tested compounds showed enzymatic inhibition on VatD with IC50 168.6, 91.0 and 55.2 micromol x L(-1), separately. Other compounds could not be dissolved in the system and/or had little effect on the enzyme (IC50 > 200 micromol x L(-1)). To our knowledge, it is first time that small molecular weight organic compounds were identified as VatD inhibitors. It is expected that the VatD inhibitors identified at present study could serve as lead compounds for the further development of the novel therapeutic agents to overcome streptogramins resistance.
[Mh] Termos MeSH primário: Acetiltransferases/antagonistas & inibidores
Inibidores Enzimáticos/farmacologia
Estreptogramina Grupo A/farmacologia
[Mh] Termos MeSH secundário: Acetiltransferases/genética
Catálise/efeitos dos fármacos
Desenho de Drogas
Farmacorresistência Bacteriana
Inibidores Enzimáticos/química
Inibidores Enzimáticos/metabolismo
Escherichia coli/genética
Vetores Genéticos
Estrutura Molecular
Estreptogramina Grupo A/química
Estreptogramina Grupo A/metabolismo
Transformação Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Streptogramin Group A); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.- (virginiamycin acetyltransferase D)
[Em] Mês de entrada:0805
[Cu] Atualização por classe:070524
[Lr] Data última revisão:
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:070525
[St] Status:MEDLINE

  3 / 4 MEDLINE  
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[Au] Autor:Johnston NJ; Mukhtar TA; Wright GD
[Ad] Endereço:Antimicrobial Research Centre, Department of Biochemistry, McMaster University, ON, Canada.
[Ti] Título:Streptogramin antibiotics: mode of action and resistance.
[So] Source:Curr Drug Targets;3(4):335-44, 2002 Aug.
[Is] ISSN:1389-4501
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The streptogramin antibiotics were discovered over 40 years ago but are only now emerging as important therapeutic agents for the treatment of infection caused by a variety of bacteria. The streptogramins consist of mixtures of two structurally distinct compounds, type A and type B, which are separately bacteriostatic, but bactericidal in appropriate ratios. These antibiotics act at the level of inhibition of translation through binding to the bacterial ribosome. Resistance to streptogramins occurs through a number of mechanisms including target modification, efflux, and enzyme catalyzed antibiotic modification. This review describes the current understanding of streptogramin function and resistance with emphasis on molecular mechanism and epidemiology.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
[Mh] Termos MeSH secundário: Antibacterianos/química
Bactérias/efeitos dos fármacos
Infecções Bacterianas/tratamento farmacológico
Resistência a Medicamentos/genética
Farmacorresistência Bacteriana/genética
Seres Humanos
Estrutura Molecular
Estreptogramina Grupo A/química
Estreptogramina Grupo A/farmacologia
Estreptogramina Grupo B/química
Estreptogramina Grupo B/farmacologia
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Streptogramin Group A); 0 (Streptogramin Group B); 0 (Streptogramins)
[Em] Mês de entrada:0302
[Cu] Atualização por classe:061115
[Lr] Data última revisão:
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:020710
[St] Status:MEDLINE

  4 / 4 MEDLINE  
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[Au] Autor:Sugantino M; Roderick SL
[Ad] Endereço:Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, New York 10461, USA.
[Ti] Título:Crystal structure of Vat(D): an acetyltransferase that inactivates streptogramin group A antibiotics.
[So] Source:Biochemistry;41(7):2209-16, 2002 Feb 19.
[Is] ISSN:0006-2960
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The streptogramin class of antibiotics act to inhibit bacterial protein synthesis, and their semisynthetic derivatives, such as dalfopristin-quinupristin (Synercid), are used to treat serious or life-threatening infections due to multiply antibiotic resistant bacteria. Acquired resistance of the nosocomial pathogen Enterococcus faecium to the group A component of natural and semisynthetic streptogramin mixtures is a prerequisite for the streptogramin resistance phenotype and is mediated by a streptogramin acetyltransferase. The crystal structure of Vat(D), a streptogramin acetyltransferase from a human urinary isolate of E. faecium, has been determined as an apoenzyme and in complex with either acetyl-CoA or virginiamycin M1 and CoA. These structures illustrate the location and arrangement of residues at the active site, and point to His 82 as a residue that may function as a general base. The structural similarity of Vat(D) to the xenobiotic acetyltransferase from Pseudomonas aeruginosa indicates similarities in the catalytic mechanism for these enzymes as well as several shared and distinctive antibiotic binding interactions between these enzymes and their respective substrates. These results reveal the molecular basis for a reaction by which Gram-positive cocci acquire resistance to a last resort antibiotic.
[Mh] Termos MeSH primário: Acetiltransferases/química
Proteínas de Bactérias
Enterococcus faecium/enzimologia
Estreptogramina Grupo A/antagonistas & inibidores
Estreptogramina Grupo A/metabolismo
[Mh] Termos MeSH secundário: Acetiltransferases/metabolismo
Sequência de Aminoácidos
Sítios de Ligação
Cloranfenicol O-Acetiltransferase/química
Cristalografia por Raios X
Seres Humanos
Dados de Sequência Molecular
Dobramento de Proteína
Estrutura Secundária de Proteína
Pseudomonas aeruginosa/enzimologia
[Nm] Nome de substância:
0 (Apoenzymes); 0 (Bacterial Proteins); 0 (Streptogramin Group A); 0 (Xenobiotics); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.- (Vat protein, Bacteria); EC (Chloramphenicol O-Acetyltransferase)
[Em] Mês de entrada:0203
[Cu] Atualização por classe:071114
[Lr] Data última revisão:
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:020214
[St] Status:MEDLINE

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