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Pesquisa : D08.811.913.696.620.475 [Categoria DeCS]
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[PMID]:28437612
[Au] Autor:Ma C; Liang C; Wang Y; Pan M; Jiang Q; Shi C
[Ad] Endereço:Key Laboratory of Sensor Analysis of Tumor Marker, Ministry of Education, College of Chemistry and Molecular Engineering, Qingdao University of Science and Technology , Qingdao 266042, P.R. China.
[Ti] Título:Combinatorial Library Based on Restriction Enzyme-mediated Modular Assembly.
[So] Source:ACS Comb Sci;19(6):351-355, 2017 Jun 12.
[Is] ISSN:2156-8944
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Combinatorial approaches in directed evolution were proven to be more efficient for exploring sequence space and innovating function of protein. Here, we presented the modular assembly of secondary structures (MASS) for constructing a combinatorial library. In this approach, secondary structure elements were extracted from natural existing protein. The common linkers were flanking secondary structure elements, and then secondary structure elements were digested by Hinf I restriction endonuclease that was used in the construction of combinatorial library for the first time. The digested DNA fragments were randomly ligated in the sense orientation, then in sequence to be amplified by PCR and transformation. This approach showed that different DNA fragments without homologous sequences could be randomly assembled to create significant sequence space. With the structure analysis of recombinants, it would be beneficial to the rational design, even to the design of protein de novo, and to evolve any genetic part or circuit.
[Mh] Termos MeSH primário: Bactérias/enzimologia
Técnicas de Química Combinatória/métodos
DNA/metabolismo
Desoxirribonucleases de Sítio Específico do Tipo II/metabolismo
Evolução Molecular Direcionada/métodos
Biblioteca Gênica
[Mh] Termos MeSH secundário: Bacillus/enzimologia
Bacillus/genética
Bacillus/metabolismo
Bactérias/genética
Bactérias/metabolismo
Sequência de Bases
DNA/genética
Genes Bacterianos
Canamicina Quinase/genética
Klebsiella pneumoniae/enzimologia
Klebsiella pneumoniae/genética
Klebsiella pneumoniae/metabolismo
Nucleotidiltransferases/genética
Recombinação Genética
Staphylococcus aureus/enzimologia
Staphylococcus aureus/genética
Staphylococcus aureus/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
9007-49-2 (DNA); EC 2.7.1.95 (Kanamycin Kinase); EC 2.7.7.- (Nucleotidyltransferases); EC 2.7.7.- (kanamycin nucleotidyltransferase); EC 3.1.21.4 (Deoxyribonucleases, Type II Site-Specific); EC 3.1.21.4 (GANTC-specific type II deoxyribonucleases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170425
[St] Status:MEDLINE
[do] DOI:10.1021/acscombsci.6b00145


  2 / 997 MEDLINE  
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[PMID]:28373209
[Au] Autor:Sánchez-Carrera D; Bravo-Navas S; Cabezón E; Arechaga I; Cabezas M; Yáñez L; Pipaón C
[Ad] Endereço:Laboratorio de Hematología Molecular, Servicio de Hematología y Hemoterapia, Hospital Universitario Marqués de Valdecilla-Instituto de Investigación Marqués de Valdecilla (IDIVAL), Santander, Spain.
[Ti] Título:Fludarabine resistance mediated by aminoglycoside-3'-phosphotransferase-IIa and the structurally related eukaryotic cAMP-dependent protein kinase.
[So] Source:FASEB J;31(7):3007-3017, 2017 Jul.
[Is] ISSN:1530-6860
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:While working with G418-resistant stably transfected cells, we realized the neomycin resistance (NeoR) gene, which encodes the aminoglycoside-3'-phosphotransferase-IIa [APH(3')-IIa], also confers resistance to the nucleoside analog fludarabine. Fludarabine is a cytostatic drug widely used in the treatment of hematologic and solid tumors, as well as in the conditioning of patients before transplantation of hematopoietic progenitors. We present evidence that NeoR-transfected cells do not incorporate fludarabine, thus avoiding DNA damage caused by the drug, evidenced by a lack of FANCD2 monoubiquitination and impaired apoptosis. A screening of other nucleoside analogs revealed that APH(3')-IIa only protects against ATP purine analogs. Moreover, APH(3')-IIa ATPase activity is inhibited by fludarabine monophosphate, suggesting that APH(3')-IIa blocks fludarabine incorporation into DNA by dephosphorylating its active fludarabine triphosphate form. Furthermore, overexpression of the catalytic subunit of the eukaryotic kinase PKA, which is structurally related to APHs, also provides resistance to fludarabine, anticipating its putative utility as a response marker to the drug. Our results preclude the use of Neo marker plasmids in the study of purine analogs and unveils a new resistance mechanism against these chemotherapeuticals.-Sánchez-Carrera, D., Bravo-Navas, S., Cabezón, E., Arechaga, I., Cabezas, M., Yáñez, L., Pipaón, C. Fludarabine resistance mediated by aminoglycoside-3'-phosphotransferase-IIa and the structurally related eukaryotic cAMP-dependent protein kinase.
[Mh] Termos MeSH primário: Antineoplásicos/farmacologia
Proteínas Quinases Dependentes de AMP Cíclico/metabolismo
Resistência a Medicamentos Antineoplásicos/fisiologia
Regulação Enzimológica da Expressão Gênica/fisiologia
Canamicina Quinase/metabolismo
Vidarabina/análogos & derivados
[Mh] Termos MeSH secundário: Sítios de Ligação
Linhagem Celular Transformada
Clonagem Molecular
Proteínas Quinases Dependentes de AMP Cíclico/genética
Fibroblastos
Seres Humanos
Canamicina Quinase/genética
Estrutura Molecular
Relação Estrutura-Atividade
Vidarabina/química
Vidarabina/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); EC 2.7.1.95 (Kanamycin Kinase); EC 2.7.11.11 (Cyclic AMP-Dependent Protein Kinases); FA2DM6879K (Vidarabine); P2K93U8740 (fludarabine)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170918
[Lr] Data última revisão:
170918
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170405
[St] Status:MEDLINE
[do] DOI:10.1096/fj.201601245R


  3 / 997 MEDLINE  
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[PMID]:28260587
[Au] Autor:Carvalho I; Campo RD; Sousa M; Silva N; Carrola J; Marinho C; Santos T; Carvalho S; Nóvoa M; Quaresma M; Pereira JE; Cobo M; Igrejas G; Poeta P
[Ad] Endereço:1​Department of Veterinary Sciences, University of Trás-os-Montes and Alto Douro, Vila Real, Portugal 2​Department of Genetics and Biotechnology, Vila Real, Portugal 3​Functional Genomics and Proteomics Unit, Vila Real, Portugal.
[Ti] Título:Antimicrobial-resistant Escherichia coli and Enterococcus spp. isolated from Miranda donkey (Equus asinus): an old problem from a new source with a different approach.
[So] Source:J Med Microbiol;66(2):191-202, 2017 Mar.
[Is] ISSN:1473-5644
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:PURPOSE: The Miranda donkey (Equus asinus) is an endangeredasinine from Miranda do Douro region, located in the north east of Portugal. We studied the antimicrobial resistance and virulence genes in Escherichia coli and Enterococcus spp. isolates from these animals. METHODOLOGY: In March 2014, a total of 66 faecal samples were recovered from independent animals. Antibiotic resistance was determined by the disc diffusion method. Carriage of genes coding for antibiotic-resistant and virulent factors was analysed by PCR. RESULTS: A total of 66 E. coli and 41 enterococcal isolates were detected, with Enterococcus faecium (61 %) and Enterococcus hirae (24 %) being the most prevalent species. For enterococcal isolates, high percentages of resistance rates to tetracycline (68.3 %), quinupristin/dalfopristin (51.2 %) and ciprofloxacin (48.8 %) were observed. The genes erm(A) and/or erm(B), tet(M) and/or tet(L), vat(D) and/or vat(E) and aph(3')-IIIa were also found. The most frequent virulence gene detected was gel(E), followed by ace, cpd and hyl. Escherichia coli isolates were highly resistant to streptomycin (78 %), whereas 39 % of them exhibited resistance to aminoglycosides and tetracycline. Genes sul1 and/or sul2 were detected in 66.7 % of trimethoprim/sulfamethoxazole-resistant isolates. The virulence genes detected were fim(A) (46 %) and cnf1 (27 %). CONCLUSION: To the best of our knowledge, this is the first report showing antibiotic resistance among Escherichiacoli and Enterococcus spp. isolates from the Miranda donkey in Portugal, indicating possible antibiotic-resistant bacterial reservoirs. However, the detection of these resistances presents a low risk for other animals and human beings in that rural area.
[Mh] Termos MeSH primário: Farmacorresistência Bacteriana Múltipla
Enterococcus/genética
Equidae/microbiologia
Escherichia coli/genética
[Mh] Termos MeSH secundário: Aminoglicosídeos/farmacologia
Animais
Antibacterianos/farmacologia
Proteínas de Bactérias/genética
Ciprofloxacino/farmacologia
DNA Bacteriano/genética
Enterococcus/classificação
Enterococcus/isolamento & purificação
Escherichia coli/classificação
Escherichia coli/isolamento & purificação
Canamicina Quinase/genética
Metiltransferases/genética
Testes de Sensibilidade Microbiana
Portugal
Sulfametoxazol/farmacologia
Tetraciclina/farmacologia
Trimetoprima/farmacologia
Virginiamicina/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aminoglycosides); 0 (Anti-Bacterial Agents); 0 (Bacterial Proteins); 0 (DNA, Bacterial); 11006-76-1 (Virginiamycin); 126602-89-9 (quinupristin-dalfopristin); 5E8K9I0O4U (Ciprofloxacin); AN164J8Y0X (Trimethoprim); EC 2.1.1.- (Methyltransferases); EC 2.1.1.184 (ErmA protein, Bacteria); EC 2.7.1.95 (Kanamycin Kinase); F8VB5M810T (Tetracycline); JE42381TNV (Sulfamethoxazole)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170321
[Lr] Data última revisão:
170321
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170307
[St] Status:MEDLINE
[do] DOI:10.1099/jmm.0.000423


  4 / 997 MEDLINE  
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[PMID]:28004885
[Au] Autor:Elbehery AH; Leak DJ; Siam R
[Ad] Endereço:Graduate Program of Biotechnology, The American University in Cairo, Cairo, Egypt.
[Ti] Título:Novel thermostable antibiotic resistance enzymes from the Atlantis II Deep Red Sea brine pool.
[So] Source:Microb Biotechnol;10(1):189-202, 2017 Jan.
[Is] ISSN:1751-7915
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The advent of metagenomics has greatly facilitated the discovery of enzymes with useful biochemical characteristics for industrial and biomedical applications, from environmental niches. In this study, we used sequence-based metagenomics to identify two antibiotic resistance enzymes from the secluded, lower convective layer of Atlantis II Deep Red Sea brine pool (68°C, ~2200 m depth and 250‰ salinity). We assembled > 4 000 000 metagenomic reads, producing 43 555 contigs. Open reading frames (ORFs) called from these contigs were aligned to polypeptides from the Comprehensive Antibiotic Resistance Database using BLASTX. Two ORFs were selected for further analysis. The ORFs putatively coded for 3'-aminoglycoside phosphotransferase [APH(3')] and a class A beta-lactamase (ABL). Both genes were cloned, expressed and characterized for activity and thermal stability. Both enzymes were active in vitro, while only APH(3') was active in vivo. Interestingly, APH(3') proved to be thermostable (T  = 61.7°C and ~40% residual activity after 30 min of incubation at 65°C). On the other hand, ABL was not as thermostable, with a T  = 43.3°C. In conclusion, we have discovered two novel AR enzymes with potential application as thermophilic selection markers.
[Mh] Termos MeSH primário: Farmacorresistência Bacteriana
Canamicina Quinase/genética
Canamicina Quinase/metabolismo
Metagenoma
beta-Lactamases/genética
beta-Lactamases/metabolismo
[Mh] Termos MeSH secundário: Clonagem Molecular
Biologia Computacional
Estabilidade Enzimática
Expressão Gênica
Sedimentos Geológicos
Oceano Índico
Canamicina Quinase/química
Metagenômica
Fases de Leitura Aberta
Sais
Análise de Sequência de DNA
Homologia de Sequência
Temperatura Ambiente
beta-Lactamases/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Salts); 0 (brine); EC 2.7.1.95 (Kanamycin Kinase); EC 3.5.2.6 (beta-Lactamases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170613
[Lr] Data última revisão:
170613
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161223
[St] Status:MEDLINE
[do] DOI:10.1111/1751-7915.12468


  5 / 997 MEDLINE  
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[PMID]:27965516
[Au] Autor:Yoon EJ; Grillot-Courvalin C; Courvalin P
[Ad] Endereço:Microbiology Department, Institut Pasteur, Unité des Agents Antibactériens, Paris, France.
[Ti] Título:New aminoglycoside-modifying enzymes APH(3')-VIII and APH(3')-IX in Acinetobacter rudis and Acinetobacter gerneri.
[So] Source:J Antibiot (Tokyo);70(4):400-403, 2017 Apr.
[Is] ISSN:0021-8820
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Analysis of whole-genome sequences of 133 strains of Acinetobacter detected two genes for new types of aminoglycoside 3'-O-phosphotransferase [APH(3')], type VIII in Acinetobacter rudis and IX in A. gerneri. The enzymes were related to each other (49% identity) and to APH(3')-VI (61% and 51% identity, respectively), which is intrinsic to A. guillouiae. The cloned genes conferred kanamycin and amikacin resistance to Escherichia coli but were cryptic or expressed at low levels in the original hosts. The chromosomal location of both genes and the genetic events for acquisition of an ancestral aphA gene by A. rudis and A. gerneri, and loss by A. bereziniae were supported by the molecular phylogenetic tree of these genes. These data confirm that nonpathogenic susceptible bacterial species can be considered as potential reservoirs of resistance genes.
[Mh] Termos MeSH primário: Acinetobacter/metabolismo
Aminoglicosídeos/metabolismo
Antibacterianos/metabolismo
Canamicina Quinase/metabolismo
[Mh] Termos MeSH secundário: Acinetobacter/efeitos dos fármacos
Amicacina/farmacologia
Mapeamento Cromossômico
Cromossomos Bacterianos/genética
Clonagem Molecular
DNA Bacteriano/genética
Farmacorresistência Bacteriana/genética
Escherichia coli/efeitos dos fármacos
Escherichia coli/genética
Canamicina/farmacologia
Canamicina Quinase/química
Testes de Sensibilidade Microbiana
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aminoglycosides); 0 (Anti-Bacterial Agents); 0 (DNA, Bacterial); 59-01-8 (Kanamycin); 84319SGC3C (Amikacin); EC 2.7.1.95 (Kanamycin Kinase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170504
[Lr] Data última revisão:
170504
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161215
[St] Status:MEDLINE
[do] DOI:10.1038/ja.2016.144


  6 / 997 MEDLINE  
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[PMID]:27858324
[Au] Autor:Tabatabaei I; Ruf S; Bock R
[Ad] Endereço:Max-Planck-Institut für Molekulare Pflanzenphysiologie, Am Mühlenberg 1, 14476, Potsdam-Golm, Germany.
[Ti] Título:A bifunctional aminoglycoside acetyltransferase/phosphotransferase conferring tobramycin resistance provides an efficient selectable marker for plastid transformation.
[So] Source:Plant Mol Biol;93(3):269-281, 2017 Feb.
[Is] ISSN:1573-5028
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:KEY MESSAGE: A new selectable marker gene for stable transformation of the plastid genome was developed that is similarly efficient as the aadA, and produces no background of spontaneous resistance mutants. More than 25 years after its development for Chlamydomonas and tobacco, the transformation of the chloroplast genome still represents a challenging technology that is available only in a handful of species. The vast majority of chloroplast transformation experiments conducted thus far have relied on a single selectable marker gene, the spectinomycin resistance gene aadA. Although a few alternative markers have been reported, the aadA has remained unrivalled in efficiency and is, therefore, nearly exclusively used. The development of new marker genes for plastid transformation is of crucial importance to all efforts towards extending the species range of the technology as well as to those applications in basic research, biotechnology and synthetic biology that involve the multistep engineering of plastid genomes. Here, we have tested a bifunctional resistance gene for its suitability as a selectable marker for chloroplast transformation. The bacterial enzyme aminoglycoside acetyltransferase(6')-Ie/aminoglycoside phosphotransferase(2″)-Ia possesses an N-terminal acetyltransferase domain and a C-terminal phosphotransferase domain that can act synergistically and detoxify aminoglycoside antibiotics highly efficiently. We report that, in combination with selection for resistance to the aminoglycoside tobramycin, the aac(6')-Ie/aph(2″)-Ia gene represents an efficient marker for plastid transformation in that it produces similar numbers of transplastomic lines as the spectinomycin resistance gene aadA. Importantly, no spontaneous antibiotic resistance mutants appear under tobramycin selection.
[Mh] Termos MeSH primário: Acetiltransferases/metabolismo
Canamicina Quinase/metabolismo
Plastídeos/genética
Tobramicina/farmacologia
Transformação Genética/efeitos dos fármacos
[Mh] Termos MeSH secundário: Aminoglicosídeos/farmacologia
Antibacterianos/farmacologia
Genes de Plantas
Marcadores Genéticos
Plantas Geneticamente Modificadas
Tabaco/genética
Tabaco/crescimento & desenvolvimento
Transgenes
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aminoglycosides); 0 (Anti-Bacterial Agents); 0 (Genetic Markers); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.- (aminoglycoside acetyltransferase); EC 2.7.1.95 (Kanamycin Kinase); VZ8RRZ51VK (Tobramycin)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170227
[Lr] Data última revisão:
170227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161119
[St] Status:MEDLINE
[do] DOI:10.1007/s11103-016-0560-x


  7 / 997 MEDLINE  
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[PMID]:27599726
[Au] Autor:Wu D; Navet N; Liu Y; Uchida J; Tian M
[Ad] Endereço:Department of Plant and Environmental Protection Sciences, University of Hawaii at Manoa, 3190 Maile Way, St. John 317, Honolulu, HI, 96822, USA.
[Ti] Título:Establishment of a simple and efficient Agrobacterium-mediated transformation system for Phytophthora palmivora.
[So] Source:BMC Microbiol;16(1):204, 2016 Sep 06.
[Is] ISSN:1471-2180
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: As an agriculturally important oomycete genus, Phytophthora contains a large number of destructive plant pathogens that severely threaten agricultural production and natural ecosystems. Among them is the broad host range pathogen P. palmivora, which infects many economically important plant species. An essential way to dissect their pathogenesis mechanisms is genetic modification of candidate genes, which requires effective transformation systems. Four methods were developed for transformation of Phytophthora spp., including PEG(polyethylene glycol)/CaCl2 mediated protoplast transformation, electroporation of zoospores, microprojectile bombardment and Agrobacterium-mediated transformation (AMT). Among them, AMT has many advantages over the other methods such as easy handling and mainly generating single-copy integration in the genome. An AMT method previously reported for P. infestans and P. palmivora has barely been used in oomycete research due to low success and low reproducibility. RESULTS: In this study, we report a simple and efficient AMT system for P. palmivora. Using this system, we were able to reproducibly generate over 40 transformants using zoospores collected from culture grown in a single 100 mm-diameter petri dish. The generated GFP transformants constitutively expressed GFP readily detectable using a fluorescence microscope. All of the transformants tested using Southern blot analysis contained a single-copy T-DNA insertion. CONCLUSIONS: This system is highly effective and reproducible for transformation of P. palmivora and expected to be adaptable for transformation of additional Phytophthora spp. and other oomycetes. Its establishment will greatly accelerate their functional genomic studies.
[Mh] Termos MeSH primário: Agrobacterium/genética
Técnicas de Transferência de Genes
Biologia Molecular/métodos
Phytophthora/microbiologia
Transformação Genética/genética
[Mh] Termos MeSH secundário: Sequência de Bases
Cloreto de Cálcio
Elementos de DNA Transponíveis
DNA Bacteriano
DNA de Protozoário
Eletroporação/métodos
Regulação da Expressão Gênica
Vetores Genéticos
Proteínas de Fluorescência Verde
Canamicina Quinase
Microscopia de Fluorescência
Oomicetos/genética
Plantas/microbiologia
Plantas/parasitologia
Plasmídeos
Polietilenoglicóis
Protoplastos
Reprodutibilidade dos Testes
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA Transposable Elements); 0 (DNA, Bacterial); 0 (DNA, Protozoan); 0 (T-DNA); 147336-22-9 (Green Fluorescent Proteins); 30IQX730WE (Polyethylene Glycols); EC 2.7.1.95 (Kanamycin Kinase); M4I0D6VV5M (Calcium Chloride)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170831
[Lr] Data última revisão:
170831
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160908
[St] Status:MEDLINE
[do] DOI:10.1186/s12866-016-0825-1


  8 / 997 MEDLINE  
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[PMID]:27514959
[Au] Autor:Perumal N; Murugesan S; Krishnan P
[Ad] Endereço:Department of Microbiology, Dr. ALM PG Institute of Basic Medical Sciences, University of Madras, Chennai, India.
[Ti] Título:Distribution of genes encoding aminoglycoside-modifying enzymes among clinical isolates of methicillin-resistant staphylococci.
[So] Source:Indian J Med Microbiol;34(3):350-2, 2016 Jul-Sep.
[Is] ISSN:1998-3646
[Cp] País de publicação:India
[La] Idioma:eng
[Ab] Resumo:The objective of this study was to determine the distribution of genes encoding aminoglycoside-modifying enzymes (AMEs) and staphylococcal cassette chromosome mec (SCCmec) elements among clinical isolates of methicillin-resistant staphylococci (MRS). Antibiotic susceptibility test was done using Kirby-Bauer disk diffusion method. The presence of SCCmec types and AME genes, namely, aac (6')-Ie-aph (2''), aph (3')-IIIa and ant (4')-Ia was determined using two different multiplex polymerase chain reaction. The most encountered AME genes were aac (6')-Ie-aph (2'') (55.4%) followed by aph (3')-IIIa (32.3%) and ant (4')-Ia gene (9%). SCCmec type I (34%) was predominant in this study. In conclusion, the aac (6')-Ie-aph (2'') was the most common AME gene and SCCmec type I was most predominant among the MRS isolates.
[Mh] Termos MeSH primário: Acetiltransferases/genética
Inativação Metabólica
Canamicina Quinase/genética
Staphylococcus aureus Resistente à Meticilina/enzimologia
Staphylococcus aureus Resistente à Meticilina/genética
Nucleotidiltransferases/genética
Infecções Estafilocócicas/microbiologia
[Mh] Termos MeSH secundário: Aminoglicosídeos/metabolismo
Antibacterianos/metabolismo
Biotransformação
Testes de Sensibilidade a Antimicrobianos por Disco-Difusão
Seres Humanos
Staphylococcus aureus Resistente à Meticilina/isolamento & purificação
Reação em Cadeia da Polimerase Multiplex
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aminoglycosides); 0 (Anti-Bacterial Agents); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.- (aminoglycoside acetyltransferase); EC 2.7.1.95 (Kanamycin Kinase); EC 2.7.7.- (Nucleotidyltransferases); EC 2.7.7.46 (gentamicin 2''-nucleotidyltransferase)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160813
[St] Status:MEDLINE
[do] DOI:10.4103/0255-0857.188339


  9 / 997 MEDLINE  
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[PMID]:27387794
[Au] Autor:Ngo HX; Garneau-Tsodikova S
[Ad] Endereço:Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, 789 South Limestone Street, Lexington, KY, 40536-0596, USA.
[Ti] Título:Flipping the Switch "On" for Aminoglycoside-Resistance Enzymes: The Mechanism Is Finally Revealed!
[So] Source:Structure;24(7):1011-3, 2016 Jul 06.
[Is] ISSN:1878-4186
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In a recent issue of Structure, Caldwell et al. (2016) determined crystal structures of APH(2″)-Ia in complex with various combinations of aminoglycosides and nucleosides, which compellingly revealed that the catalytic activity of this resistance enzyme is regulated by a conformational change of the triphosphate of GTP, a mechanism previously unknown for antibiotic kinases.
[Mh] Termos MeSH primário: Aminoglicosídeos
Canamicina Quinase/química
[Mh] Termos MeSH secundário: Antibacterianos
Fosfotransferases (Aceptor do Grupo Álcool)/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aminoglycosides); 0 (Anti-Bacterial Agents); EC 2.7.1.- (Phosphotransferases (Alcohol Group Acceptor)); EC 2.7.1.95 (Kanamycin Kinase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160709
[St] Status:MEDLINE


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[PMID]:27338640
[Au] Autor:Boyko KM; Gorbacheva MA; Korzhenevskiy DA; Alekseeva MG; Mavletova DA; Zakharevich NV; Elizarov SM; Rudakova NN; Danilenko VN; Popov VO
[Ad] Endereço:Bach Institute of Biochemistry, Federal Research Centre of Biotechnology of the Russian Academy of Sciences, Leninsky Prospekt. 33, Bld. 2, 119071, Moscow, Russian Federation; National Research Center "Kurchatov Institute", Kurchatov Complex of NBICS-technologies, Akad. Kurchatova sqr., 1, Moscow, 1
[Ti] Título:Structural characterization of the novel aminoglycoside phosphotransferase AphVIII from Streptomyces rimosus with enzymatic activity modulated by phosphorylation.
[So] Source:Biochem Biophys Res Commun;477(4):595-601, 2016 09 02.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Aminoglycoside phosphotransferases represent a broad class of enzymes that promote bacterial resistance to aminoglycoside antibiotics via the phosphorylation of hydroxyl groups in the latter. Here we report the spatial structure of the 3'-aminoglycoside phosphotransferase of novel VIII class (AphVIII) solved by X-ray diffraction method with a resolution of 2.15 Å. Deep analysis of APHVIII structure and its comparison with known structures of aminoglycoside phosphotransferases of various types reveals that AphVIII has a typical two-domain fold and, however, possesses some unique characteristics that distinguish the enzyme from its known homologues. The most important difference is the presence of the activation loop with unique Ser146 residue. We demonstrate that in the apo-state of the enzyme the activation loop does not interact with other parts of the enzyme and seems to adopt catalytically competent state only after substrate binding.
[Mh] Termos MeSH primário: Canamicina Quinase/química
Streptomyces rimosus/enzimologia
[Mh] Termos MeSH secundário: Sítios de Ligação
Cristalografia por Raios X
Ativação Enzimática
Canamicina Quinase/metabolismo
Modelos Moleculares
Nucleotídeos/metabolismo
Fosforilação
Conformação Proteica
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Nucleotides); 0 (Recombinant Proteins); EC 2.7.1.95 (Kanamycin Kinase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171126
[Lr] Data última revisão:
171126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160625
[St] Status:MEDLINE



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