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[PMID]:29458684
[Au] Autor:Wise MG; Horvath E; Young K; Sahm DF; Kazmierczak KM
[Ad] Endereço:1​International Health Management Associates, Schaumburg, Illinois, USA.
[Ti] Título:Global survey of Klebsiella pneumoniae major porins from ertapenem non-susceptible isolates lacking carbapenemases.
[So] Source:J Med Microbiol;67(3):289-295, 2018 Mar.
[Is] ISSN:1473-5644
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:PURPOSE: To understand the diversity of porin disruption in Klebsiella pneumoniae, the major outer membrane protein (OMP) porins, OmpK35 and OmpK36, were examined in a set of isolates that did not harbour traditional carbapenem-hydrolysing enzymes, but nevertheless tested non-susceptible to ertapenem. METHODS: A world-wide collection of Klebsiella pneumoniae isolates that were part of the Study for Monitoring Antimicrobial Resistance Trends (SMART) surveillance project over the years 2008-2014 were characterised with regard to their ß-lactamase gene carriage and potential permeability defects. Four hundred and eighty-seven isolates that did not carry carbapenemase genes, but were non-susceptible to ertapenem, were investigated by sequence analysis of the genes encoding OmpK35 and OmpK36. Isolates without obvious genetic lesions in either major porin gene were further examined by outer membrane protein SDS-PAGE. RESULTS: The majority of isolates, 83.0 % (404/487), exhibited clear genetic disruption in either or both of the ompK35 and ompK36 genes. Among the proportion of the collection with the highest ertapenem MIC value (>4 mg l ), 60.5 % (115/190) showed mutation in both porin genes. Isolates without obvious genetic mutations were examined by SDS-PAGE, and 90.4 % (75/83) were found to lack or show altered expression of at least one of the major OMPs when compared to an ertapenem sensitive control strain. CONCLUSION: This study illustrates that porin deficiency in Klebsiella pneumoniae is a widespread phenomenon, and in combination with ESBLs and/or AmpC enzymes, likely accounts for the elevated ertapenem MICs observed in this study.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Proteínas de Bactérias/genética
Klebsiella pneumoniae/genética
Porinas/genética
beta-Lactamas/farmacologia
[Mh] Termos MeSH secundário: Proteínas de Bactérias/metabolismo
Carbapenêmicos/farmacologia
DNA Bacteriano/genética
Eletroforese em Gel de Poliacrilamida
Seres Humanos
Infecções por Klebsiella/epidemiologia
Infecções por Klebsiella/microbiologia
Klebsiella pneumoniae/efeitos dos fármacos
Klebsiella pneumoniae/isolamento & purificação
Klebsiella pneumoniae/metabolismo
Testes de Sensibilidade Microbiana
Mutação
beta-Lactamases/genética
beta-Lactamases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Bacterial Proteins); 0 (Carbapenems); 0 (DNA, Bacterial); 0 (OmpK35 porin, Klebsiella pneumoniae); 0 (OmpK36 protein, Klebsiella pneumoniae); 0 (Porins); 0 (beta-Lactams); EC 3.5.2.6 (beta-Lactamases); EC 3.5.2.6 (carbapenemase); G32F6EID2H (ertapenem)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180221
[St] Status:MEDLINE
[do] DOI:10.1099/jmm.0.000691


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[PMID]:29458539
[Au] Autor:Ma ST; Ding GJ; Huang XW; Wang ZW; Wang L; Yu ML; Shi W; Jiang YP; Tang LJ; Xu YG; Li YJ
[Ad] Endereço:College of Veterinary Medicine, Northeast Agricultural University, Mu Cai Street No. 59, Xiang Fang District, Harbin, PR China.
[Ti] Título:Immunogenicity in chickens with orally administered recombinant chicken-borne Lactobacillus saerimneri expressing FimA and OmpC antigen of O78 avian pathogenic Escherichia coli.
[So] Source:J Med Microbiol;67(3):441-451, 2018 Mar.
[Is] ISSN:1473-5644
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:PURPOSE: Avian colibacillosis is responsible for economic losses to poultry producers worldwide. To combat this, we aimed to develop an effective oral vaccine for chicken against O78 avian pathogenic Escherichia coli (APEC) infection through a Lactobacillus delivery system. METHODOLOGY: Eight Lactobacillus strains isolated from the intestines of broiler chickens were evaluated based on their in vitro adherence ability to assess their potential as a delivery vector. Fimbrial subunit A (FimA) and outer-membrane protein C (OmpC) of APEC with and without fusion to dendritic cell-targeting peptide (DCpep) and microfold cell-targeting peptide (Co1) were displayed on the surface of Lactobacillus saerimneri M-11 and yielded vaccine groups (pPG-ompC-fimA/M-11 and pPG-ompC-fimA-Co1-DCpep/M-11, respectively). The colonization of the recombinant strains in vivo was assessed and the immunogenicity and protective efficacy of orally administered recombinant strains in chickens were evaluated. RESULTS: The colonization of the recombinant strains in vivo revealed no significant differences between the recombinant and wild-type strains. Chickens orally administered with vaccine groups showed significantly higher levels of OmpC/FimA-specific IgG in serum and mucosal IgA in cecum lavage, nasal lavage and stool compared to the pPG/M-11 group. After challenge with APEC CVCC1553, better protective efficacy was observed in chickens orally immunized with pPG-ompC-fimA/M-11 and pPG-ompC-fimA-Co1-DCpep/M-11, but no significant differences were observed between the two groups. CONCLUSIONS: Recombinant chicken-borne L. saerimneri M-11 showed good immunogenicity in chickens, suggesting that it may be a promising vaccine candidate against APEC infections. However, the activity of mammalian DCpep and Co1 was not significant in chickens.
[Mh] Termos MeSH primário: Infecções por Escherichia coli/veterinária
Vacinas contra Escherichia coli/imunologia
Proteínas de Fímbrias/imunologia
Imunogenicidade da Vacina
Lactobacillus/genética
Porinas/imunologia
Doenças das Aves Domésticas/imunologia
[Mh] Termos MeSH secundário: Administração Oral
Animais
Anticorpos Antibacterianos/sangue
Antígenos de Bactérias/genética
Antígenos de Bactérias/imunologia
Ceco/imunologia
Galinhas
Escherichia coli/imunologia
Escherichia coli/patogenicidade
Infecções por Escherichia coli/imunologia
Infecções por Escherichia coli/prevenção & controle
Proteínas de Fímbrias/genética
Imunoglobulina A/sangue
Imunoglobulina G/sangue
Intestinos/microbiologia
Lactobacillus/crescimento & desenvolvimento
Lactobacillus/imunologia
Lactobacillus/isolamento & purificação
Porinas/genética
Doenças das Aves Domésticas/prevenção & controle
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Bacterial); 0 (Antigens, Bacterial); 0 (Escherichia coli Vaccines); 0 (Immunoglobulin A); 0 (Immunoglobulin G); 0 (OmpC protein); 0 (Porins); 0 (fimbrillin); 147680-16-8 (Fimbriae Proteins)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180221
[St] Status:MEDLINE
[do] DOI:10.1099/jmm.0.000679


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[PMID]:28456528
[Au] Autor:Jiang P; Cai Y; Chen J; Ye X; Mao S; Zhu S; Xue X; Chen S; Zhang L
[Ad] Endereço:Institute of Molecular Virology and Immunology, Department of Microbiology and Immunology, School of Basic Medical Sciences, Wenzhou Medical University, Wenzhou 325035, Zhejiang, PR China.
[Ti] Título:Evaluation of tandem Chlamydia trachomatis MOMP multi-epitopes vaccine in BALB/c mice model.
[So] Source:Vaccine;35(23):3096-3103, 2017 05 25.
[Is] ISSN:1873-2518
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Chlamydia trachomatis (Ct), an obligate intracellular parasite, is the leading cause of bacterial sexually transmitted diseases worldwide. The best solution to control the spread of Ct is to develop safe and effective vaccines. However, an effective vaccine has not been developed due to some challenges such as selection of appropriate candidate antigens and an effective delivery system. In our previous study, we have developed a Ct vaccine that comprises a multi-epitope peptide of Ct major outer membrane protein (MOMP ) and Hepatitis B virus core antigen (HBcAg). The vaccine was evaluated in a murine model with chlamydial genital infection. The results indicated that Ct MOMP multi-epitope delivered by HBcAg could be an effective vaccine for the prevention of Ct. In this study, another two epitopes were selected from the MOMP protein and tandemly linked with MOMP to enhance the immunogenicity and the protective effect of the candidate vaccine. Our results revealed that both the immunogenicity and the protective effect of the tandem Ct MOMP multi-epitopes were much better than that of the single epitope. Therefore, vaccines based on the tandem Ct MOMP multi-epitopes could be more effective immune prophylactics to prevent Ct infection than the single epitope in murine model system.
[Mh] Termos MeSH primário: Vacinas Bacterianas/imunologia
Infecções por Chlamydia/prevenção & controle
Chlamydia trachomatis/imunologia
Epitopos/imunologia
Porinas/imunologia
[Mh] Termos MeSH secundário: Animais
Anticorpos Antibacterianos/sangue
Vacinas Bacterianas/administração & dosagem
Vacinas Bacterianas/química
Infecções por Chlamydia/microbiologia
Chlamydia trachomatis/química
Modelos Animais de Doenças
Epitopos/química
Feminino
Imunogenicidade da Vacina
Camundongos
Camundongos Endogâmicos BALB C
Porinas/química
[Pt] Tipo de publicação:EVALUATION STUDIES; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibodies, Bacterial); 0 (Bacterial Vaccines); 0 (Epitopes); 0 (Porins); 146409-23-6 (omp1 protein, Chlamydia trachomatis)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170501
[St] Status:MEDLINE


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[PMID]:29335469
[Au] Autor:Aunkham A; Zahn M; Kesireddy A; Pothula KR; Schulte A; Baslé A; Kleinekathöfer U; Suginta W; van den Berg B
[Ad] Endereço:Biochemistry-Electrochemistry Research Unit, Institute of Science, Suranaree University of Technology, Nakhon Ratchasima, 30000, Thailand.
[Ti] Título:Structural basis for chitin acquisition by marine Vibrio species.
[So] Source:Nat Commun;9(1):220, 2018 01 15.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Chitin, an insoluble polymer of N-acetylglucosamine, is one of the most abundant biopolymers on Earth. By degrading chitin, chitinolytic bacteria such as Vibrio harveyi are critical for chitin recycling and maintenance of carbon and nitrogen cycles in the world's oceans. A decisive step in chitin degradation is the uptake of chito-oligosaccharides by an outer membrane protein channel named chitoporin (ChiP). Here, we report X-ray crystal structures of ChiP from V. harveyi in the presence and absence of chito-oligosaccharides. Structures without bound sugar reveal a trimeric assembly with an unprecedented closing of the transport pore by the N-terminus of a neighboring subunit. Substrate binding ejects the pore plug to open the transport channel. Together with molecular dynamics simulations, electrophysiology and in vitro transport assays our data provide an explanation for the exceptional affinity of ChiP for chito-oligosaccharides and point to an important role of the N-terminal gate in substrate transport.
[Mh] Termos MeSH primário: Carbono/metabolismo
Quitina/metabolismo
Nitrogênio/metabolismo
Vibrio/metabolismo
[Mh] Termos MeSH secundário: Acetilglucosamina/metabolismo
Proteínas da Membrana Bacteriana Externa/química
Proteínas da Membrana Bacteriana Externa/genética
Proteínas da Membrana Bacteriana Externa/metabolismo
Ciclo do Carbono
Cristalografia por Raios X
Modelos Moleculares
Ciclo do Nitrogênio
Oceanos e Mares
Oligossacarídeos/metabolismo
Porinas/química
Porinas/genética
Porinas/metabolismo
Conformação Proteica
Água do Mar/química
Água do Mar/microbiologia
Vibrio/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Outer Membrane Proteins); 0 (Oligosaccharides); 0 (Porins); 1398-61-4 (Chitin); 7440-44-0 (Carbon); N762921K75 (Nitrogen); V956696549 (Acetylglucosamine)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180306
[Lr] Data última revisão:
180306
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180117
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02523-y


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[PMID]:29297851
[Au] Autor:Molitor A; James CE; Fanning S; Pagès JM; Davin-Regli A
[Ad] Endereço:1​UMR_MD1, Facultés de Pharmacie and Médecine, Aix-Marseille Univ, Marseille, France.
[Ti] Título:Ram locus is a key regulator to trigger multidrug resistance in Enterobacter aerogenes.
[So] Source:J Med Microbiol;67(2):148-159, 2018 Feb.
[Is] ISSN:1473-5644
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:PURPOSE: Several genetic regulators belonging to AraC family are involved in the emergence of MDR isolates of E. aerogenes due to alterations in membrane permeability. Compared with the genetic regulator Mar, RamA may be more relevant towards the emergence of antibiotic resistance. METHODOLOGY: Focusing on the global regulators, Mar and Ram, we compared the amino acid sequences of the Ram repressor in 59 clinical isolates and laboratory strains of E. aerogenes. Sequence types were associated with their corresponding multi-drug resistance phenotypes and membrane protein expression profiles using MIC and immunoblot assays. Quantitative gene expression analysis of the different regulators and their targets (porins and efflux pump components) were performed. RESULTS: In the majority of the MDR isolates tested, ramR and a region upstream of ramA were mutated but marR or marA were unchanged. Expression and cloning experiments highlighted the involvement of the ram locus in the modification of membrane permeability. Overexpression of RamA lead to decreased porin production and increased expression of efflux pump components, whereas overexpression of RamR had the opposite effects. CONCLUSION: Mutations or deletions in ramR, leading to the overexpression of RamA predominated in clinical MDR E. aerogenes isolates and were associated with a higher-level of expression of efflux pump components. It was hypothesised that mutations in ramR, and the self-regulating region proximal to ramA, probably altered the binding properties of the RamR repressor; thereby producing the MDR phenotype. Consequently, mutability of RamR may play a key role in predisposing E. aerogenes towards the emergence of a MDR phenotype.
[Mh] Termos MeSH primário: Farmacorresistência Bacteriana Múltipla/genética
Enterobacter aerogenes/efeitos dos fármacos
Enterobacter aerogenes/genética
Regulação Bacteriana da Expressão Gênica
Proteínas Associadas à Resistência a Múltiplos Medicamentos/genética
Fatores de Transcrição/genética
[Mh] Termos MeSH secundário: Antibacterianos/farmacologia
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Infecções por Enterobacteriaceae/microbiologia
Genes araC
Loci Gênicos
Seres Humanos
Testes de Sensibilidade Microbiana
Proteínas Associadas à Resistência a Múltiplos Medicamentos/metabolismo
Mutação
Porinas/biossíntese
Porinas/genética
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Bacterial Proteins); 0 (Multidrug Resistance-Associated Proteins); 0 (Porins); 0 (RamA protein, Enterobacter aerogenes); 0 (Transcription Factors)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180206
[Lr] Data última revisão:
180206
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180104
[St] Status:MEDLINE
[do] DOI:10.1099/jmm.0.000667


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[PMID]:29198700
[Au] Autor:Citak F; Ghai I; Rosenkötter F; Benier L; Winterhalter M; Wagner R
[Ad] Endereço:Department of Life Sciences and Chemistry, key, 28719 Bremen, Germany.
[Ti] Título:Probing transport of fosfomycin through substrate specific OprO and OprP from Pseudomonas aeruginosa.
[So] Source:Biochem Biophys Res Commun;495(1):1454-1460, 2018 01 01.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Increasing antimicrobial drug resistance is a global threat especially with respect to Gram-negative bacteria. The low permeability of the bacterial outer cell wall has been identified as an important bottleneck that prevents a sufficient antibacterial effect to be achieved at low doses of the antibiotics. In particular, the outer membrane permeability for negatively charged molecules of the clinical important ESKAPE bacterium Pseudomonas aeruginosa is determined by the low conductance porins OprO and OprP Here we show that the alternative phosphonic-acid antibiotic fosfomycin is highly permeable through the OprO and OprP channels. For this, we applied an electrophysiological zero-current assay using concentration gradients of fosfomycin under tri-ionic conditions to quantify flux of fosfomycin through OprO and OprP. Our analyzes show that OprO, and to a lesser degree OprP, have unexpected very high permeability to fosfomycin, so the antibiotic should be a potentially excellent alternative choice for the control of Pseudomonas aeruginosa infections.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Permeabilidade da Membrana Celular/fisiologia
Fosfomicina/farmacocinética
Porinas/metabolismo
Pseudomonas aeruginosa/metabolismo
[Mh] Termos MeSH secundário: Análise do Fluxo Metabólico/métodos
Técnicas de Sonda Molecular
Especificidade por Substrato/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (OprO protein, Pseudomonas aeruginosa); 0 (Porins); 0 (oprP protein, Pseudomonas aeruginosa); 2N81MY12TE (Fosfomycin)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180105
[Lr] Data última revisão:
180105
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171205
[St] Status:MEDLINE


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[PMID]:29223157
[Au] Autor:Sidorin EV; Khomenko VA; Kim NY; Dmitrenok PS; Stenkova AM; Novikova OD; Solov'eva TF
[Ad] Endereço:Elyakov Pacific Institute of Bioorganic Chemistry, Far-Eastern Branch of the Russian Academy of Sciences, Vladivostok, 690022, Russia. sev1972@mail.ru.
[Ti] Título:Self-Organization of Recombinant Membrane Porin OmpF from Yersinia pseudotuberculosis in Aqueous Environments.
[So] Source:Biochemistry (Mosc);82(11):1304-1313, 2017 Nov.
[Is] ISSN:1608-3040
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Recombinant porin OmpF (an integral protein of bacterial outer membrane) from Yersinia pseudotuberculosis was synthesized in Escherichia coli cells as inclusion bodies. By combining the methods of anion-exchange and gel filtration chromatographies, recombinant OmpF (rOmpF) was isolated as an individual protein in its denatured state, and its characteristic properties (molecular mass, N-terminal amino acid sequence, and hydrodynamic radius of the protein in 8 M urea solution) were determined. According to the data of gel filtration, dynamic light scattering, optical spectroscopy, and binding of the hydrophobic fluorescent probe 8-anilino-1-naphthalenesulfonic acid, the rOmpF is fully unfolded in 8 M urea and exists in random coil conformation. In aqueous solutions, rOmpF undergoes conformational changes, reversible self-association, and aggregation. When transferred from 8 M urea into water, PBS (containing 0.15 M NaCl, pH 7.4), or buffer containing 0.8 M urea (pH 8.0), fully unfolded rOmpF forms relatively compact monomeric intermediates prone to self-association with formation of multimers. The oligomeric intermediates have high content of native protein-like secondary structure and pronounced tertiary structure. In acidic media (pH 5.0, close to the protein isoelectric point), rOmpF undergoes rapid irreversible aggregation. Therefore, we found that medium composition significantly affects both porin folding and processes of its self-association and aggregation.
[Mh] Termos MeSH primário: Porinas/química
Yersinia pseudotuberculosis/química
[Mh] Termos MeSH secundário: Proteínas da Membrana Bacteriana Externa
Proteínas de Bactérias
Escherichia coli/genética
Escherichia coli/metabolismo
Corpos de Inclusão
Porinas/biossíntese
Porinas/isolamento & purificação
Conformação Proteica
Desnaturação Proteica/efeitos dos fármacos
Dobramento de Proteína/efeitos dos fármacos
Multimerização Proteica/efeitos dos fármacos
Renaturação Proteica/efeitos dos fármacos
Proteínas Recombinantes
Soluções/química
Soluções/farmacologia
Água
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Outer Membrane Proteins); 0 (Bacterial Proteins); 0 (OmpF protein); 0 (Porins); 0 (Recombinant Proteins); 0 (Solutions); 059QF0KO0R (Water)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180103
[Lr] Data última revisão:
180103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171211
[St] Status:MEDLINE
[do] DOI:10.1134/S0006297917110086


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[PMID]:29211780
[Au] Autor:Schiavano GF; Carloni E; Andreoni F; Magi S; Chironna M; Brandi G; Amagliani G
[Ad] Endereço:Department of Biomolecular Sciences, Toxicological, Hygienistic and Environmental Sciences Unit, University of Urbino Carlo Bo, Urbino, PU, Italy.
[Ti] Título:Prevalence and antibiotic resistance of Pseudomonas aeruginosa in water samples in central Italy and molecular characterization of oprD in imipenem resistant isolates.
[So] Source:PLoS One;12(12):e0189172, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:SCOPE: This study aimed to analyse the prevalence, antibiotic resistance and genetic relatedness of P. aeruginosa isolates obtained from potable and recreational water samples (n. 8,351) collected from different settings (swimming pools, n. 207; healthcare facilities, n 1,684; accommodation facilities, n. 1,518; municipal waterworks, n. 4,500; residential buildings, n. 235). Possible mechanisms underlying resistance to imipenem, with particular focus on those involving oprD-based uptake, were also explored. METHODS AND RESULTS: Isolation and identification of Pseudomonas aeruginosa was performed according to the standardized procedure UNI EN ISO 16266:2008 followed by PCR confirmation. Antibiotic Susceptibility testing was conducted according to EUCAST standardized disk diffusion method. Genetic relatedness of strains was carried out by RAPD. The sequence of the oprD gene was analyzed by standard method. Fifty-three samples (0.63%) were positive for P. aeruginosa, of which 10/207 (4.83%) were from swimming pools. Five isolates (9.43%) were resistant to imipenem, one to Ticarcillin + Clavulanate, one to both Piperacillin and Ticarcillin + Clavulanate. The highest isolation rate of imipenem resistant P. aeruginosa was observed in swimming pool water. Identical RAPD profiles were found in isolates from the same location in the same year or even in different years. CONCLUSIONS: Imipenem resistant strains were identified as carbapenemase-negative and resistance has been associated with inactivating mutations within the oprD gene, with a concomitant loss of porin. RAPD results proved that a water system can remain colonized by one strain for long periods and the contamination may be difficult to eradicate. This study has revealed the presence of P. aeruginosa in different water samples, including resistant strains, especially in swimming pools, and confirmed the role of porins as a contributing factor in carbapenem resistance in Gram-negative bacteria.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Farmacorresistência Bacteriana/genética
Imipenem/farmacologia
Porinas/genética
Pseudomonas aeruginosa/isolamento & purificação
Microbiologia da Água
[Mh] Termos MeSH secundário: Genes Bacterianos
Itália
Testes de Sensibilidade Microbiana
Pseudomonas aeruginosa/efeitos dos fármacos
Pseudomonas aeruginosa/genética
Reação em Cadeia da Polimerase em Tempo Real
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Porins); 148412-32-2 (OprD protein, Pseudomonas aeruginosa); 71OTZ9ZE0A (Imipenem)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171229
[Lr] Data última revisão:
171229
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171207
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189172


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[PMID]:28460189
[Au] Autor:Abady NR; Guglielmino CJD; Graham RM; Adelskov J; Smith HV; Patel BKC; Jennison AV
[Ad] Endereço:a Microbial Gene Research and Resources Facility, School of Natural Sciences, Griffith University, Queensland, Australia.
[Ti] Título:Genetic characterization of a Neisseria meningitidis cluster in Queensland, Australia.
[So] Source:Can J Microbiol;63(7):644-647, 2017 Jul.
[Is] ISSN:1480-3275
[Cp] País de publicação:Canada
[La] Idioma:eng
[Ab] Resumo:Neisseria meningitidis serogroups B and C have been responsible for the majority of invasive meningococcal disease in Australia, with serogroup B strains causing an increasing proportion of cases in recent years. Serogroup Y has typically caused sporadic disease in Australia. In 2002, a cluster of 4 cases was reported from a rural region in Queensland. Three of these cases were serogroup C, with 1 case diagnosed by molecular detection only, and the fourth case was identified as a serogroup Y infection. Genomic analysis, including antigen finetyping, multilocus sequence typing (MLST), and core genome MLST, demonstrated that the serogroup Y case, though spatially and temporally linked to a serogroup C disease cluster, was not the product of a capsule switch and that one of the serogroup C isolates had a deletion of the entire porA sequence.
[Mh] Termos MeSH primário: Surtos de Doenças
Infecções Meningocócicas/microbiologia
Neisseria meningitidis/genética
Porinas/genética
[Mh] Termos MeSH secundário: Análise por Conglomerados
Seres Humanos
Infecções Meningocócicas/epidemiologia
Tipagem de Sequências Multilocus
Neisseria meningitidis/imunologia
Neisseria meningitidis/isolamento & purificação
Queensland
Análise de Sequência de DNA
Sorogrupo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Porins); 0 (porin protein, Neisseria)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170502
[St] Status:MEDLINE
[do] DOI:10.1139/cjm-2017-0017


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[PMID]:28931058
[Au] Autor:Moura ARSS; Kretz CB; Ferreira IE; Nunes AMPB; de Moraes JC; Reis MG; McBride AJA; Wang X; Campos LC
[Ad] Endereço:Laboratório de Patologia e Biologia Molecular, Instituto Gonçalo Moniz, FIOCRUZ-BA, Salvador, Bahia, Brazil.
[Ti] Título:Molecular characterization of Neisseria meningitidis isolates recovered from 11-19-year-old meningococcal carriers in Salvador, Brazil.
[So] Source:PLoS One;12(9):e0185038, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Characterization of meningococci isolated from the pharynx is essential towards understanding the dynamics of meningococcal carriage and disease. Meningococcal isolates, collected from adolescents resident in Salvador, Brazil during 2014, were characterized by multilocus sequence typing, genotyping or whole-genome sequencing. Most were nongroupable (61.0%), followed by genogroups B (11.9%) and Y (8.5%). We identified 34 different sequence types (STs), eight were new STs, distributed among 14 clonal complexes (cc), cc1136 represented 20.3% of the nongroupable isolates. The porA and fetA genotypes included P1.18,25-37 (11.9%), P1.18-1,3 (10.2%); F5-5 (23.7%), F4-66 (16.9%) and F1-7 (13.6%). The porB class 3 protein and the fHbp subfamily A (variants 2 and 3) genotypes were found in 93.0 and 71.0% of the isolates, respectively. NHBA was present in all isolates, and while most lacked NadA (94.9%), we detected the hyperinvasive lineages B:P1.19,15:F5-1:ST-639 (cc32); C:P1.22,14-6:F3-9:ST-3780 (cc103) and W:P1.5,2:F1-1:ST-11 (cc11). This is the first report on the genetic diversity and vaccine antigen prevalence among N. meningitidis carriage isolates in the Northeast of Brazil. This study highlights the need for ongoing characterization of meningococcal isolates following the introduction of vaccines and for determining public health intervention strategies.
[Mh] Termos MeSH primário: Neisseria meningitidis/genética
Neisseria meningitidis/isolamento & purificação
Filogenia
[Mh] Termos MeSH secundário: Adesinas Bacterianas/genética
Adolescente
Antígenos de Bactérias/genética
Proteínas da Membrana Bacteriana Externa/genética
Proteínas de Bactérias/genética
Brasil
Proteínas de Transporte/genética
Portador Sadio
Criança
Variação Genética
Genótipo
Seres Humanos
Tipagem de Sequências Multilocus
Porinas/genética
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adhesins, Bacterial); 0 (Antigens, Bacterial); 0 (Bacterial Outer Membrane Proteins); 0 (Bacterial Proteins); 0 (Carrier Proteins); 0 (FrpB protein, bacteria); 0 (NHBA protein, Neisseria meningitidis); 0 (NadA protein, Neisseria meningitidis); 0 (Porins); 0 (factor H-binding protein, Neisseria meningitidis); 0 (porin protein, Neisseria)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170921
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185038



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