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[PMID]:29244831
[Au] Autor:Wang S; Xiao SZ; Gu FF; Tang J; Guo XK; Ni YX; Qu JM; Han LZ
[Ad] Endereço:Department of Clinical Microbiology, Ruijin Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China.
[Ti] Título:Antimicrobial susceptibility and molecular epidemiology of clinical Enterobacter cloacae bloodstream isolates in Shanghai, China.
[So] Source:PLoS One;12(12):e0189713, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Enterobacter cloacae is a major nosocomial pathogen causing bloodstream infections. We retrospectively conducted a study to assess antimicrobial susceptibility and phylogenetic relationships of E. cloacae bloodstream isolates in two tertiary university-affiliated hospitals in Shanghai, in order to facilitate managements of E. cloacae bloodstream infections and highlight some unknowns for future prevention. METHODS: Fifty-three non-duplicate E. cloacae bloodstream isolates were consecutively collected from 2013 to 2016. Antimicrobial susceptibility was determined by disk diffusion. PCR was performed to detect extended-spectrum ß-lactamase (ESBL), carbapenemase and colistin resistance (MCR-1) gene. Plasmid-mediated AmpC ß-lactamase (pAmpC) genes were detected using a multiplex PCR assay targeting MIR/ACT gene (closely related to chromosomal EBC family gene) and other plasmid-mediated genes, including DHA, MOX, CMY, ACC, and FOX. eBURST was applied to analyze multi-locus sequence typing (MLST). RESULTS: The rates of resistance to all tested antibiotics were <40%. Among 53 E. cloacae isolates, 8(15.1%) were ESBL producers, 3(5.7%) were carbapenemase producers and 18(34.0%) were pAmpC producers. ESBL producers bear significantly higher resistance to cefotaxime (100.0%), ceftazidime (100.0%), aztreonam (100.0%), piperacillin (87.5%), tetracycline (75.0%), and trimethoprim-sulfamethoxazole (62.5%) than non-producers (p<0.05). PAmpC- and non-producers both presented low resistance rates (<40%) to all antibiotics (p>0.05). SHV (6/8, 75.0%) and MIR/ACT (15/18, 83.3%) predominated in ESBL and pAmpC producers respectively. Moreover, 2 isolates co-carried TEM-1, SHV-12, IMP-26 and DHA-1. MLST analysis distinguished the 53 isolates into 51 STs and only ST414 and ST520 were assigned two isolates of each (2/53). CONCLUSION: The antimicrobial resistance rates were low among 53 E. cloacae bloodstream isolates in the two hospitals. Multiclonality disclosed no evidence on spread of these isolates in Shanghai. The simultaneous presence of ESBL, carbapenemase and pAmpC detected in 2 isolates was firstly reported in Shanghai, which necessitated active ongoing surveillances and consistent prevention and control of E. cloacae.
[Mh] Termos MeSH primário: Infecção Hospitalar/tratamento farmacológico
Farmacorresistência Bacteriana Múltipla/genética
Enterobacter cloacae/genética
Epidemiologia Molecular
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
China/epidemiologia
Infecção Hospitalar/epidemiologia
Infecção Hospitalar/genética
Infecção Hospitalar/microbiologia
Enterobacter cloacae/patogenicidade
Etanolaminofosfotransferase/genética
Seres Humanos
Filogenia
beta-Lactamases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); EC 2.7.8.1 (Ethanolaminephosphotransferase); EC 3.5.2.6 (beta-Lactamases); EC 3.5.2.6 (carbapenemase)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180102
[Lr] Data última revisão:
180102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171216
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189713


  2 / 107 MEDLINE  
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[PMID]:28874446
[Au] Autor:Harper M; Wright A; St Michael F; Li J; Deveson Lucas D; Ford M; Adler B; Cox AD; Boyce JD
[Ad] Endereço:Infection and Immunity Program, Monash Biomedicine Discovery Institute and Department of Microbiology, Monash University, VIC, Australia marina.harper@monash.edu.
[Ti] Título:Characterization of Two Novel Lipopolysaccharide Phosphoethanolamine Transferases in Pasteurella multocida and Their Role in Resistance to Cathelicidin-2.
[So] Source:Infect Immun;85(11), 2017 Nov.
[Is] ISSN:1098-5522
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The lipopolysaccharide (LPS) produced by the Gram-negative bacterial pathogen has phosphoethanolamine (PEtn) residues attached to lipid A, 3-deoxy-d-manno-octulosonic acid (Kdo), heptose, and galactose. In this report, we show that PEtn is transferred to lipid A by the EptA homologue, PetL, and is transferred to galactose by a novel PEtn transferase that is unique to called PetG. Transcriptomic analyses indicated that expression was positively regulated by the global regulator Fis and negatively regulated by an Hfq-dependent small RNA. Importantly, we have identified a novel PEtn transferase called PetK that is responsible for PEtn addition to the single Kdo molecule (Kdo ), directly linked to lipid A in the glycoform A LPS. assays showed that the presence of a functional and , and therefore the presence of PEtn on lipid A and Kdo , was essential for resistance to the cationic, antimicrobial peptide cathelicidin-2. The importance of PEtn on Kdo and the identification of the transferase responsible for this addition have not previously been shown. Phylogenetic analysis revealed that PetK is the first representative of a new family of predicted PEtn transferases. The PetK family consists of uncharacterized proteins from a range of Gram-negative bacteria that produce LPS glycoforms with only one Kdo molecule, including pathogenic species within the genera , , and We predict that many of these bacteria will require the addition of PEtn to Kdo for maximum protection against host antimicrobial peptides.
[Mh] Termos MeSH primário: Proteínas de Bactérias/genética
Proteínas Sanguíneas/toxicidade
Farmacorresistência Bacteriana/genética
Etanolaminofosfotransferase/genética
Regulação Bacteriana da Expressão Gênica
Pasteurella multocida/genética
Pasteurella multocida/patogenicidade
Precursores de Proteínas/toxicidade
[Mh] Termos MeSH secundário: Animais
Proteínas de Bactérias/metabolismo
Galinhas
Biologia Computacional
Etanolaminofosfotransferase/metabolismo
Etanolaminas/química
Etanolaminas/metabolismo
Fator Proteico para Inversão de Estimulação/genética
Fator Proteico para Inversão de Estimulação/metabolismo
Galactose/química
Galactose/metabolismo
Perfilação da Expressão Gênica
Heptoses/química
Heptoses/metabolismo
Isoenzimas
Lipídeo A/química
Lipídeo A/metabolismo
Mutação
Proteínas Nucleares/genética
Proteínas Nucleares/metabolismo
Infecções por Pasteurella/microbiologia
Infecções por Pasteurella/patologia
Pasteurella multocida/classificação
Pasteurella multocida/efeitos dos fármacos
Filogenia
Açúcares Ácidos/química
Açúcares Ácidos/metabolismo
Transcriptoma
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Blood Proteins); 0 (Ethanolamines); 0 (Factor For Inversion Stimulation Protein); 0 (Heptoses); 0 (Isoenzymes); 0 (Lipid A); 0 (Nuclear Proteins); 0 (Protein Precursors); 0 (Sugar Acids); 0 (cathelicidin 2 protein, mammal); 1069-03-0 (2-keto-3-deoxyoctonate); 78A2BX7AEU (phosphorylethanolamine); EC 2.7.8.1 (Ethanolaminephosphotransferase); X2RN3Q8DNE (Galactose)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170907
[St] Status:MEDLINE


  3 / 107 MEDLINE  
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[PMID]:28678874
[Au] Autor:Tijet N; Faccone D; Rapoport M; Seah C; Pasterán F; Ceriana P; Albornoz E; Corso A; Petroni A; Melano RG
[Ad] Endereço:Public Health Ontario Laboratory, Toronto, Ontario, Canada.
[Ti] Título:Molecular characteristics of mcr-1-carrying plasmids and new mcr-1 variant recovered from polyclonal clinical Escherichia coli from Argentina and Canada.
[So] Source:PLoS One;12(7):e0180347, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We have characterized nine mcr-1-harboring plasmids from clinical Escherichia coli isolates previously described in Argentina and Canada. Three of these plasmids carried a mcr-1-variant called here mcr-1.5. All these E. coli isolates were not clonally related and were recovered in different years and locations. However, their mcr-1-harboring plasmids showed high identity among them and to others characterized in other countries, which strongly suggests that this plasmid-type is playing an important role in spreading this mechanism of resistance to polymyxins.
[Mh] Termos MeSH primário: Proteínas de Escherichia coli/genética
Escherichia coli/genética
Etanolaminofosfotransferase/genética
Plasmídeos/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Antibacterianos/farmacologia
Argentina
Canadá
DNA Bacteriano/química
DNA Bacteriano/genética
Farmacorresistência Bacteriana/genética
Escherichia coli/enzimologia
Escherichia coli/isolamento & purificação
Infecções por Escherichia coli/microbiologia
Infecções por Escherichia coli/transmissão
Variação Genética
Genótipo
Seres Humanos
Testes de Sensibilidade Microbiana
Plasmídeos/química
Reação em Cadeia da Polimerase
Polimixinas/farmacologia
Análise de Sequência de DNA
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (DNA, Bacterial); 0 (Escherichia coli Proteins); 0 (MCR-1 protein, E coli); 0 (Polymyxins); EC 2.7.8.1 (Ethanolaminephosphotransferase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171006
[Lr] Data última revisão:
171006
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170706
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0180347


  4 / 107 MEDLINE  
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[PMID]:28052917
[Au] Autor:Ahmed MY; Al-Khayat A; Al-Murshedi F; Al-Futaisi A; Chioza BA; Pedro Fernandez-Murray J; Self JE; Salter CG; Harlalka GV; Rawlins LE; Al-Zuhaibi S; Al-Azri F; Al-Rashdi F; Cazenave-Gassiot A; Wenk MR; Al-Salmi F; Patton MA; Silver DL; Baple EL; McMaster CR; Crosby AH
[Ad] Endereço:Medical Research (Level 4), University of Exeter Medical School, RILD Wellcome Wolfson Centre, Royal Devon and Exeter NHS Foundation Trust, Barrack Road, Exeter, EX2 5DW, UK.
[Ti] Título:A mutation of EPT1 (SELENOI) underlies a new disorder of Kennedy pathway phospholipid biosynthesis.
[So] Source:Brain;140(3):547-554, 2017 Mar 01.
[Is] ISSN:1460-2156
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Mutations in genes involved in lipid metabolism have increasingly been associated with various subtypes of hereditary spastic paraplegia, a highly heterogeneous group of neurodegenerative motor neuron disorders characterized by spastic paraparesis. Here, we report an unusual autosomal recessive neurodegenerative condition, best classified as a complicated form of hereditary spastic paraplegia, associated with mutation in the ethanolaminephosphotransferase 1 (EPT1) gene (now known as SELENOI), responsible for the final step in Kennedy pathway forming phosphatidylethanolamine from CDP-ethanolamine. Phosphatidylethanolamine is a glycerophospholipid that, together with phosphatidylcholine, constitutes more than half of the total phospholipids in eukaryotic cell membranes. We determined that the mutation defined dramatically reduces the enzymatic activity of EPT1, thereby hindering the final step in phosphatidylethanolamine synthesis. Additionally, due to central nervous system inaccessibility we undertook quantification of phosphatidylethanolamine levels and species in patient and control blood samples as an indication of liver phosphatidylethanolamine biosynthesis. Although this revealed alteration to levels of specific phosphatidylethanolamine fatty acyl species in patients, overall phosphatidylethanolamine levels were broadly unaffected indicating that in blood EPT1 inactivity may be compensated for, in part, via alternate biochemical pathways. These studies define the first human disorder arising due to defective CDP-ethanolamine biosynthesis and provide new insight into the role of Kennedy pathway components in human neurological function.
[Mh] Termos MeSH primário: Etanolaminofosfotransferase/genética
Etanolaminofosfotransferase/metabolismo
Mutação/genética
Fosfolipídeos/biossíntese
Transdução de Sinais/genética
Paraplegia Espástica Hereditária/genética
[Mh] Termos MeSH secundário: Adolescente
Criança
Pré-Escolar
Cromatografia Líquida
Consanguinidade
Análise Mutacional de DNA
Saúde da Família
Feminino
Expressão Gênica
Seres Humanos
Lactente
Masculino
Espectrometria de Massas
Omã
Fosfolipídeos/sangue
Saccharomyces cerevisiae
Paraplegia Espástica Hereditária/diagnóstico por imagem
Paraplegia Espástica Hereditária/enzimologia
Paraplegia Espástica Hereditária/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Phospholipids); EC 2.7.8.1 (Ethanolaminephosphotransferase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170106
[St] Status:MEDLINE
[do] DOI:10.1093/brain/aww318


  5 / 107 MEDLINE  
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[PMID]:27564119
[Au] Autor:Liu L; Li Y; Wang X; Guo W
[Ad] Endereço:State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, China.
[Ti] Título:A phosphoethanolamine transferase specific for the 4'-phosphate residue of Cronobacter sakazakii lipid A.
[So] Source:J Appl Microbiol;121(5):1444-1456, 2016 Nov.
[Is] ISSN:1365-2672
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:AIMS: Investigate how Cronobacter sakazakii modify their lipid A structure to avoid recognition by the host immune cells. METHODS AND RESULTS: Lipid A modification was observed in C. sakazakii BAA894 grown at pH 5·0 but not pH 7·0. Overexpression of C. sakazakii gene ESA_RS09200 in Escherichia coli W3110 caused a phosphoethanolamine (PEA) modification of lipid A; when ESA_RS09200 was deleted in C. sakazakii BAA894, this lipid A modification disappeared. Lipid A modification was observed in BAA894 grown at pH 5·0 when the 1- phosphate residue of lipid A was removed, but disappeared when the 4'- phosphate residue of lipid A was removed. When ESA_RS16430, the orthologous gene of E. coli pmrA, was deleted in C. sakazakii BAA894, this PEA modification of lipid A was still observed, suggesting that this modification was not regulated by the PmrA-PmrB system. Compared to the wild-type BAA894, ESA_RS09200 deletion mutant showed decreased resistance to cationic antimicrobial peptides (CAMP), increased recognition by TLR4/MD2, decreased ability to invade and persist in mammalian cells. CONCLUSIONS: ESA_RS09200 in C. sakazakii BAA894 encodes a PEA transferase that specifically adds a PEA to the 4'-phosphate residue of lipid A, but not regulated by the PmrA-PmrB system. PEA modification of lipid A reduces recognition and killing by the host innate immune system. SIGNIFICANCE AND IMPACT OF THE STUDY: This study showed that modification of the lipid A moiety of C. sakazakii with PEA increased resistance to CAMP and recognition of the immune response although signalling of TLR4/MD2 cascade, suggesting that the organism could not successfully evade the host innate immune system without the transference of PEA to its lipid A moiety.
[Mh] Termos MeSH primário: Cronobacter sakazakii/enzimologia
Etanolaminofosfotransferase/metabolismo
Lipídeo A/metabolismo
[Mh] Termos MeSH secundário: Animais
Peptídeos Catiônicos Antimicrobianos/farmacologia
Células CACO-2
Cronobacter sakazakii/efeitos dos fármacos
Cronobacter sakazakii/genética
Etanolaminofosfotransferase/genética
Etanolaminas/metabolismo
Seres Humanos
Lipídeo A/química
Fosfatos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antimicrobial Cationic Peptides); 0 (Ethanolamines); 0 (Lipid A); 0 (Phosphates); 78A2BX7AEU (phosphorylethanolamine); EC 2.7.8.1 (Ethanolaminephosphotransferase)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160827
[St] Status:MEDLINE
[do] DOI:10.1111/jam.13280


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[PMID]:27062077
[Au] Autor:Pawlowic MC; Hsu FF; Moitra S; Biyani N; Zhang K
[Ad] Endereço:Department of Biological Sciences, Texas Tech University, Lubbock, TX, 79409, USA.
[Ti] Título:Plasmenylethanolamine synthesis in Leishmania major.
[So] Source:Mol Microbiol;101(2):238-49, 2016 Jul.
[Is] ISSN:1365-2958
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Ethanolamine glycerophospholipids are ubiquitous cell membrane components. Trypanosomatid parasites of the genus Leishmania synthesize the majority of their ethanolamine glycerophospholipids as 1-O-alk-1'-enyl-2-acyl-sn-glycero-3-phosphoethanolamine or plasmenylethanolamine (PME) through the Kennedy pathway. PME is a subtype of ether phospholipids also known as ethanolamine plasmalogen whose functions are not well characterized. In this study, we investigated the role of PME synthesis in Leishmania major through the characterization of an ethanolamine phosphotransferase (EPT) mutant. EPT-null parasites are largely devoid of PME and fully viable in regular medium but fail to proliferate in the absence of fetal bovine serum. They exhibit significant abnormalities in the synthesis and localization of GPI-anchored surface molecules. EPT-null mutants also show attenuated virulence in BALB/c mice. Furthermore, in addition to PME synthesis, ethanolamine also contributes to the production of phosphatidylcholine, the most abundant class of lipids in Leishmania. Together, these findings suggest that ethanolamine production is likely required for Leishmania promastigotes to generate bulk phospholipids, to handle stress, and to control the expression of membrane bound virulence factors.
[Mh] Termos MeSH primário: Leishmania major/metabolismo
Plasmalogênios/biossíntese
[Mh] Termos MeSH secundário: Animais
Etanolamina/metabolismo
Etanolaminofosfotransferase/metabolismo
Etanolaminas/metabolismo
Feminino
Camundongos
Camundongos Endogâmicos BALB C
Mutação
Fosfatidilcolinas/metabolismo
Fosfatidiletanolaminas/metabolismo
Fosfolipídeos/metabolismo
Plasmalogênios/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ethanolamines); 0 (Phosphatidylcholines); 0 (Phosphatidylethanolamines); 0 (Phospholipids); 0 (Plasmalogens); 0 (phosphatidal ethanolamines); 5KV86114PT (Ethanolamine); 78A2BX7AEU (phosphorylethanolamine); EC 2.7.8.1 (Ethanolaminephosphotransferase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170718
[Lr] Data última revisão:
170718
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160411
[St] Status:MEDLINE
[do] DOI:10.1111/mmi.13387


  7 / 107 MEDLINE  
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[PMID]:27048797
[Au] Autor:Ye H; Li Y; Li Z; Gao R; Zhang H; Wen R; Gao GF; Hu Q; Feng Y
[Ad] Endereço:Department of Medical Microbiology and Parasitology, Zhejiang University School of Medicine, Hangzhou, Zhejiang, China College of Life Science and Technology, Guangxi University, Nanning City, Guangxi, China.
[Ti] Título:Diversified mcr-1-Harbouring Plasmid Reservoirs Confer Resistance to Colistin in Human Gut Microbiota.
[So] Source:MBio;7(2):e00177, 2016 Apr 05.
[Is] ISSN:2150-7511
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:UNLABELLED: Colistin is an ultimate line of refuge against multidrug-resistant Gram-negative pathogens. Very recently, the emergence of plasmid-mediatedmcr-1colistin resistance has become a great challenge to global public health, raising the possibility that dissemination of themcr-1gene is underestimated and diversified. Here, we report three cases of plasmid-carried MCR-1 colistin resistance in isolates from gut microbiota of diarrhea patients. Structural and functional analyses determined that the colistin resistance is conferred purely by the singlemcr-1gene. Genetic and sequence mapping revealed thatmcr-1-harbouring plasmid reservoirs are present in diversity. Together, the data represent the first evidence of diversity inmcr-1-harbouring plasmid reservoirs of human gut microbiota. IMPORTANCE: The plasmid-mediated mobile colistin resistance gene (mcr-1) challenged greatly the conventional idea mentioned above that colistin is an ultimate line of refuge against lethal infections by multidrug-resistant Gram-negative pathogens. It is a possibility that diversified dissemination of themcr-1gene might be greatly underestimated. We report three cases of plasmid-carried MCR-1 colistin resistance in isolates from gut microbiota of diarrhea patients and functionally define the colistin resistance conferred purely by the singlemcr-1gene. Genetic and sequence mapping revealed unexpected diversity among themcr-1-harbouring plasmid reservoirs of human gut microbiota.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Colistina/farmacologia
Farmacorresistência Bacteriana
Etanolaminofosfotransferase/genética
Microbioma Gastrointestinal/efeitos dos fármacos
Bactérias Gram-Negativas/efeitos dos fármacos
Plasmídeos
[Mh] Termos MeSH secundário: Infecções Bacterianas/microbiologia
China
Diarreia/microbiologia
Fezes/microbiologia
Genes Bacterianos
Variação Genética
Bactérias Gram-Negativas/isolamento & purificação
Seres Humanos
Análise de Sequência de DNA
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); EC 2.7.8.1 (Ethanolaminephosphotransferase); Z67X93HJG1 (Colistin)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170111
[Lr] Data última revisão:
170111
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160407
[St] Status:MEDLINE


  8 / 107 MEDLINE  
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[PMID]:26498987
[Au] Autor:Telke AA; Rolain JM
[Ad] Endereço:Unité de recherche sur les maladies infectieuses et tropicales émergentes (URMITE), CNRS-IRD UMR 6236, Méditerranée Infection, Faculté de Médecine et de Pharmacie, Aix-Marseille Université, Marseille, France.
[Ti] Título:Functional genomics to discover antibiotic resistance genes: The paradigm of resistance to colistin mediated by ethanolamine phosphotransferase in Shewanella algae MARS 14.
[So] Source:Int J Antimicrob Agents;46(6):648-52, 2015 Dec.
[Is] ISSN:1872-7913
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Shewanella algae MARS 14 is a colistin-resistant clinical isolate retrieved from bronchoalveolar lavage of a hospitalised patient. A functional genomics strategy was employed to discover the molecular support for colistin resistance in S. algae MARS 14. A pZE21 MCS-1 plasmid-based genomic expression library was constructed in Escherichia coli TOP10. The estimated library size was 1.30×10(8) bp. Functional screening of colistin-resistant clones was carried out on Luria-Bertani agar containing 8 mg/L colistin. Five colistin-resistant clones were obtained after complete screening of the genomic expression library. Analysis of DNA sequencing results found a unique gene in all selected clones. Amino acid sequence analysis of this unique gene using the Integrated Microbial Genomes (IMG) and KEGG databases revealed that this gene encodes ethanolamine phosphotransferase (EptA, or so-called PmrC). Reverse transcription PCR analysis indicated that resistance to colistin in S. algae MARS 14 was associated with overexpression of EptA (27-fold increase), which plays a crucial role in the arrangement of outer membrane lipopolysaccharide.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Colistina/farmacologia
Farmacorresistência Bacteriana Múltipla/genética
Etanolaminofosfotransferase/genética
Shewanella/efeitos dos fármacos
Shewanella/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sequência de Bases
Etanolaminofosfotransferase/metabolismo
Biblioteca Gênica
Seres Humanos
Testes de Sensibilidade Microbiana
RNA Ribossômico 16S/genética
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Análise de Sequência de DNA
Shewanella/genética
Shewanella/isolamento & purificação
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (RNA, Ribosomal, 16S); EC 2.7.8.1 (Ethanolaminephosphotransferase); Z67X93HJG1 (Colistin)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:151224
[Lr] Data última revisão:
151224
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151027
[St] Status:MEDLINE


  9 / 107 MEDLINE  
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[PMID]:26370913
[Au] Autor:Sartelet A; Harland C; Tamma N; Karim L; Bayrou C; Li W; Ahariz N; Coppieters W; Georges M; Charlier C
[Ad] Endereço:Bovine Clinic, FARAH and Faculty of Veterinary Medicine, University of Liège, Liège, Belgium.
[Ti] Título:A stop-gain in the laminin, alpha 3 gene causes recessive junctional epidermolysis bullosa in Belgian Blue cattle.
[So] Source:Anim Genet;46(5):566-70, 2015 Oct.
[Is] ISSN:1365-2052
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Four newborn purebred Belgian Blue calves presenting a severe form of epidermolysis bullosa were recently referred to our heredo-surveillance platform. SNP array genotyping followed by autozygosity mapping located the causative gene in a 8.3-Mb interval on bovine chromosome 24. Combining information from (i) whole-genome sequencing of an affected calf, (ii) transcriptomic data from a panel of tissues and (iii) a list of functionally ranked positional candidates pinpointed a private G to A nucleotide substitution in the LAMA3 gene that creates a premature stop codon (p.Arg2609*) in exon 60, truncating 22% of the corresponding protein. The LAMA3 gene encodes the alpha 3 subunit of the heterotrimeric laminin-332, a key constituent of the lamina lucida that is part of the skin basement membrane connecting epidermis and dermis layers. Homozygous loss-of-function mutations in this gene are known to cause severe junctional epidermolysis bullosa in human, mice, horse, sheep and dog. Overall, our data strongly support the causality of the identified gene and mutation.
[Mh] Termos MeSH primário: Doenças dos Bovinos/genética
Bovinos/genética
Epidermólise Bolhosa Juncional/veterinária
Laminina/genética
[Mh] Termos MeSH secundário: Animais
Bovinos/classificação
Mapeamento Cromossômico
Análise Mutacional de DNA
Epidermólise Bolhosa Juncional/genética
Etanolaminofosfotransferase
Genótipo
Transcriptoma
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Laminin); 170834-93-2 (laminin alpha 3); EC 2.7.8.1 (Ethanolaminephosphotransferase)
[Em] Mês de entrada:1512
[Cu] Atualização por classe:150924
[Lr] Data última revisão:
150924
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150916
[St] Status:MEDLINE
[do] DOI:10.1111/age.12342


  10 / 107 MEDLINE  
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[PMID]:25902140
[Au] Autor:Trombley MP; Post DM; Rinker SD; Reinders LM; Fortney KR; Zwickl BW; Janowicz DM; Baye FM; Katz BP; Spinola SM; Bauer ME
[Ad] Endereço:Department of Microbiology and Immunology, Indiana University School of Medicine, Indianapolis, IN, United States of America.
[Ti] Título:Phosphoethanolamine Transferase LptA in Haemophilus ducreyi Modifies Lipid A and Contributes to Human Defensin Resistance In Vitro.
[So] Source:PLoS One;10(4):e0124373, 2015.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Haemophilus ducreyi resists the cytotoxic effects of human antimicrobial peptides (APs), including α-defensins, ß-defensins, and the cathelicidin LL-37. Resistance to LL-37, mediated by the sensitive to antimicrobial peptide (Sap) transporter, is required for H. ducreyi virulence in humans. Cationic APs are attracted to the negatively charged bacterial cell surface. In other gram-negative bacteria, modification of lipopolysaccharide or lipooligosaccharide (LOS) by the addition of positively charged moieties, such as phosphoethanolamine (PEA), confers AP resistance by means of electrostatic repulsion. H. ducreyi LOS has PEA modifications at two sites, and we identified three genes (lptA, ptdA, and ptdB) in H. ducreyi with homology to a family of bacterial PEA transferases. We generated non-polar, unmarked mutants with deletions in one, two, or all three putative PEA transferase genes. The triple mutant was significantly more susceptible to both α- and ß-defensins; complementation of all three genes restored parental levels of AP resistance. Deletion of all three PEA transferase genes also resulted in a significant increase in the negativity of the mutant cell surface. Mass spectrometric analysis revealed that LptA was required for PEA modification of lipid A; PtdA and PtdB did not affect PEA modification of LOS. In human inoculation experiments, the triple mutant was as virulent as its parent strain. While this is the first identified mechanism of resistance to α-defensins in H. ducreyi, our in vivo data suggest that resistance to cathelicidin LL-37 may be more important than defensin resistance to H. ducreyi pathogenesis.
[Mh] Termos MeSH primário: Proteínas de Bactérias/genética
Farmacorresistência Bacteriana/genética
Etanolaminofosfotransferase/genética
Haemophilus ducreyi/genética
Lipídeo A/metabolismo
[Mh] Termos MeSH secundário: Administração Oral
Adulto
Antibacterianos/uso terapêutico
Peptídeos Catiônicos Antimicrobianos/farmacologia
Proteínas de Bactérias/metabolismo
Cancroide/tratamento farmacológico
Cancroide/microbiologia
Cancroide/patologia
Ciprofloxacino/uso terapêutico
Etanolaminofosfotransferase/metabolismo
Etanolaminas/metabolismo
Feminino
Deleção de Genes
Expressão Gênica
Teste de Complementação Genética
Haemophilus ducreyi/efeitos dos fármacos
Haemophilus ducreyi/metabolismo
Haemophilus ducreyi/patogenicidade
Voluntários Saudáveis
Seres Humanos
Lipídeo A/química
Masculino
Mutação
Ligação Proteica
Eletricidade Estática
alfa-Defensinas/farmacologia
beta-Defensinas/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Antimicrobial Cationic Peptides); 0 (Bacterial Proteins); 0 (Ethanolamines); 0 (Lipid A); 0 (alpha-Defensins); 0 (beta-Defensins); 143108-26-3 (CAP18 lipopolysaccharide-binding protein); 5E8K9I0O4U (Ciprofloxacin); 78A2BX7AEU (phosphorylethanolamine); EC 2.7.8.1 (Ethanolaminephosphotransferase)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150423
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0124373



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