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Pesquisa : B04.123.502 [Categoria DeCS]
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[PMID]:28901529
[Au] Autor:Joshi H; Seniya SP; Suryanarayanan V; Patidar ND; Singh SK; Jain V
[Ad] Endereço:Microbiology and Molecular Biology Laboratory, Department of Biological Sciences, Indian Institute of Science Education and Research (IISER), Bhopal, India.
[Ti] Título:Dissecting the structure-function relationship in lysozyme domain of mycobacteriophage D29-encoded peptidoglycan hydrolase.
[So] Source:FEBS Lett;591(20):3276-3287, 2017 Oct.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Most bacteriophages rapidly infect and kill bacteria and, therefore, qualify as the next generation therapeutics for rapidly emerging drug-resistant bacteria such as Mycobacterium tuberculosis. We have previously characterized the mycobacteriophage D29-generated endolysin, Lysin A, for its activity against mycobacteria. Here, we present a detailed characterization of the lysozyme domain (LD) of D29 Lysin A that hydrolyzes peptidoglycan of both gram-positive and gram-negative bacteria with high potency. By characterizing an exhaustive LD protein variant library, we have identified critical residues important for LD activity and stability. We further complement our in vitro experiments with detailed in silico investigations. We present LD as a potent candidate for developing phage-based broad-spectrum therapeutics.
[Mh] Termos MeSH primário: Endopeptidases/química
Lisogenia/genética
Muramidase/química
N-Acetil-Muramil-L-Alanina Amidase/química
Proteínas Virais/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sequência de Bases
Domínio Catalítico
Clonagem Molecular
Endopeptidases/genética
Endopeptidases/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Cinética
Ligantes
Simulação de Dinâmica Molecular
Muramidase/genética
Muramidase/metabolismo
Mutação
Micobacteriófagos/química
Micobacteriófagos/genética
Micobacteriófagos/patogenicidade
Mycobacterium tuberculosis/virologia
N-Acetil-Muramil-L-Alanina Amidase/genética
N-Acetil-Muramil-L-Alanina Amidase/metabolismo
Biblioteca de Peptídeos
Ligação Proteica
Conformação Proteica em alfa-Hélice
Domínios Proteicos
Domínios e Motivos de Interação entre Proteínas
Estabilidade Proteica
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Relação Estrutura-Atividade
Especificidade por Substrato
Termodinâmica
Proteínas Virais/genética
Proteínas Virais/metabolismo
[Pt] Tipo de publicação:LETTER
[Nm] Nome de substância:
0 (Ligands); 0 (Peptide Library); 0 (Recombinant Proteins); 0 (Viral Proteins); EC 3.2.1.17 (Muramidase); EC 3.4.- (Endopeptidases); EC 3.4.99.- (endolysin); EC 3.5.1.28 (N-Acetylmuramoyl-L-alanine Amidase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170914
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12848


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[PMID]:28828700
[Au] Autor:Fan X; Gao X; Wang Q; Shen J; Zhou L; Xie J
[Ad] Endereço:School of Biological Science and Technology, University of Jinan, Shandong, 250022, China.
[Ti] Título:Complete genome sequence analysis of the novel mycobacteriophage Shandong1.
[So] Source:Arch Virol;162(12):3903-3905, 2017 Dec.
[Is] ISSN:1432-8798
[Cp] País de publicação:Austria
[La] Idioma:eng
[Ab] Resumo:In this study, we isolated a mycobacteriophage infecting Mycobacterium smegmatis mc 155 from a soil sample collected in Shandong Province in China. This phage was named Shandong1. It is a member of the family Siphoviridae with an isometric head and a long tail. Its genome was found to be 60,618 bp long with 67.46% G + C content and 96 putative protein-coding genes. No tRNA-encoding genes were identified. Comparative genomics analysis showed that the mycobacteriophage Shandong1 should be considered a member of a new species in mycobacteriophage cluster K.
[Mh] Termos MeSH primário: Genoma Viral
Micobacteriófagos/genética
Micobacteriófagos/isolamento & purificação
Mycobacterium smegmatis/virologia
Análise de Sequência de DNA
Siphoviridae/genética
Siphoviridae/isolamento & purificação
[Mh] Termos MeSH secundário: Composição de Bases
China
Micobacteriófagos/classificação
Micobacteriófagos/ultraestrutura
Filogenia
Siphoviridae/classificação
Siphoviridae/ultraestrutura
Microbiologia do Solo
Vírion/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170823
[St] Status:MEDLINE
[do] DOI:10.1007/s00705-017-3534-7


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[PMID]:27287926
[Au] Autor:Lella M; Mahalakshmi R
[Ad] Endereço:Molecular Biophysics Laboratory, Department of Biological Sciences, Indian Institute of Science Education and Research, Bhopal, 462023, India.
[Ti] Título:Solvation driven conformational transitions in the second transmembrane domain of mycobacteriophage holin.
[So] Source:Biopolymers;108(1), 2017 Jan.
[Is] ISSN:1097-0282
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Holins are pore-forming membrane proteins synthesized by lytic phages. The second transmembrane domain (TM2) of Mycobacteriophage D29 holin presents an Ala- and Gly-rich sequence, with a currently unknown structure and function. In this study, we present the spectroscopic characterization of synthetic TM2 in various solvents, detergents, and lipids. We find that TM2 adopts α-helical conformation under conditions that promote intra-strand hydrogen bonding, such as organic solvents and detergent micelles. When we transfer the peptide to a well-hydrated environment, a polyproline II-like structure is obtained. Surprisingly, we find that the polyproline II-like conformation is retained in lipid vesicles. Based on our results, we present a putative role for TM2 in the process of pore formation by holin. © 2016 The Authors. Peptide Science Published by Wiley Periodicals, Inc. Biopolymers (Pept Sci) 108: 1-10, 2017.
[Mh] Termos MeSH primário: Micobacteriófagos/metabolismo
Solventes/química
Proteínas Virais/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Dicroísmo Circular
Ligações de Hidrogênio
Concentração de Íons de Hidrogênio
Micelas
Dados de Sequência Molecular
Peptídeos/síntese química
Peptídeos/química
Redobramento de Proteína
Estrutura Secundária de Proteína
Proteínas Virais/metabolismo
Água/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Micelles); 0 (Peptides); 0 (Solvents); 0 (Viral Proteins); 059QF0KO0R (Water)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170223
[Lr] Data última revisão:
170223
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160612
[St] Status:MEDLINE
[do] DOI:10.1002/bip.22894


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[PMID]:27795387
[Au] Autor:Jain P; Weinrick BC; Kalivoda EJ; Yang H; Munsamy V; Vilcheze C; Weisbrod TR; Larsen MH; O'Donnell MR; Pym A; Jacobs WR
[Ad] Endereço:Department of Microbiology and Immunology, Albert Einstein College of Medicine, New York,New York, USA.
[Ti] Título:Dual-Reporter Mycobacteriophages (Φ2DRMs) Reveal Preexisting Mycobacterium tuberculosis Persistent Cells in Human Sputum.
[So] Source:MBio;7(5), 2016 Oct 25.
[Is] ISSN:2150-7511
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Persisters are the minor subpopulation of bacterial cells that lack alleles conferring resistance to a specific bactericidal antibiotic but can survive otherwise lethal concentrations of that antibiotic. In infections with Mycobacterium tuberculosis, such persisters underlie the need for long-term antibiotic therapy and contribute to treatment failure in tuberculosis cases. Here, we demonstrate the value of dual-reporter mycobacteriophages (Φ DRMs) for characterizing M. tuberculosis persisters. The addition of isoniazid (INH) to exponentially growing M. tuberculosis cells consistently resulted in a 2- to 3-log decrease in CFU within 4 days, and the remaining ≤1% of cells, which survived despite being INH sensitive, were INH-tolerant persisters with a distinct transcriptional profile. We fused the promoters of several genes upregulated in persisters to the red fluorescent protein tdTomato gene in Φ GFP10, a mycobacteriophage constitutively expressing green fluorescent protein (GFP), thus generating Φ DRMs. A population enriched in INH persisters exhibited strong red fluorescence, by microscopy and flow cytometry, using a Φ DRM with tdTomato controlled from the dnaK promoter. Interestingly, we demonstrated that, prior to INH exposure, a population primed for persistence existed in M. tuberculosis cells from both cultures and human sputa and that this population was highly enriched following INH exposure. We conclude that Φ DRMs provide a new tool to identify and quantitate M. tuberculosis persister cells. IMPORTANCE: Tuberculosis (TB) is again the leading cause of death from a single infectious disease, having surpassed HIV. The recalcitrance of the TB pandemic is largely due to the ability of the pathogen Mycobacterium tuberculosis to enter a persistent state in which it is less susceptible to antibiotics and immune effectors, necessitating lengthy treatment. It has been difficult to study persister cells, as we have lacked tools to isolate these rare cells. In this article, we describe the development of dual-reporter mycobacteriophages that encode a green fluorescent marker of viability and in which the promoters of genes we have identified as induced in the persister state are fused to a gene encoding a red fluorescent protein. We show that these tools can identify heterogeneity in a cell population that correlates with propensity to survive antibiotic treatment and that the proportions of these subpopulations change in M. tuberculosis cells within human sputum during the course of treatment.
[Mh] Termos MeSH primário: Tolerância a Medicamentos
Micobacteriófagos/crescimento & desenvolvimento
Mycobacterium tuberculosis/efeitos dos fármacos
Mycobacterium tuberculosis/isolamento & purificação
Escarro/microbiologia
[Mh] Termos MeSH secundário: Técnicas Bacteriológicas
Fluorescência
Perfilação da Expressão Gênica
Genes Reporter
Seres Humanos
Proteínas Luminescentes/análise
Proteínas Luminescentes/genética
Micobacteriófagos/genética
Mycobacterium tuberculosis/genética
Mycobacterium tuberculosis/virologia
Coloração e Rotulagem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Luminescent Proteins)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170621
[Lr] Data última revisão:
170621
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161101
[St] Status:MEDLINE


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[PMID]:27703073
[Au] Autor:Kelley DS; Lennon CW; Belfort M; Novikova O; SEA-PHAGES
[Ad] Endereço:Department of Biomedical Sciences, School of Public Health, University at Albany, State University of New York, Albany, New York, USA.
[Ti] Título:Mycobacteriophages as Incubators for Intein Dissemination and Evolution.
[So] Source:MBio;7(5), 2016 Oct 04.
[Is] ISSN:2150-7511
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Inteins are self-splicing protein elements that are mobile at the DNA level and are sporadically distributed across microbial genomes. Inteins appear to be horizontally transferred, and it has been speculated that phages may play a role in intein distribution. Our attention turns to mycobacteriophages, which infect mycobacteria, where both phage and host harbor inteins. Using bioinformatics, mycobacteriophage genomes were mined for inteins. This study reveals that these mobile elements are present across multiple mycobacteriophage clusters and are pervasive in certain genes, like the large terminase subunit TerL and a RecB-like nuclease, with the majority of intein-containing genes being phage specific. Strikingly, despite this phage specificity, inteins localize to functional motifs shared with bacteria, such that intein-containing genes have similar roles, like hydrolase activity and nucleic acid binding, indicating a global commonality among intein-hosting proteins. Additionally, there are multiple insertion points within active centers, implying independent invasion events, with regulatory implications. Several phage inteins were shown to be splicing competent and to encode functional homing endonucleases, important for mobility. Further, bioinformatic analysis supports the potential for phages as facilitators of intein movement among mycobacteria and related genera. Analysis of catalytic intein residues finds the highly conserved penultimate histidine inconsistently maintained among mycobacteriophages. Biochemical characterization of a noncanonical phage intein shows that this residue influences precursor accumulation, suggesting that splicing has been tuned in phages to modulate generation of important proteins. Together, this work expands our understanding of phage-based intein dissemination and evolution and implies that phages provide a context for evolution of splicing-based regulation. IMPORTANCE: Inteins are mobile protein splicing elements found in critical genes across all domains of life. Mycobacterial inteins are of particular interest because of their occurrence in pathogenic species, such as Mycobacterium tuberculosis and Mycobacterium leprae, which harbor inteins in important proteins. We have discovered a similarity in activities of intein-containing proteins among mycobacteriophages and their intein-rich actinobacterial hosts, with implications for both posttranslational regulation by inteins and phages participating in horizontal intein transfer. Our demonstration of multiple insertion points within active centers of phage proteins implies independent invasion events, indicating the importance of intein maintenance at specific functional sites. The variable conservation of a catalytic splicing residue, leading to profoundly altered splicing rates, points to the regulatory potential of inteins and to mycobacteriophages playing a role in intein evolution. Collectively, these results suggest inteins as posttranslational regulators and mycobacteriophages as both vehicles for intein distribution and incubators for intein evolution.
[Mh] Termos MeSH primário: Transferência Genética Horizontal
Inteínas/genética
Micobacteriófagos/genética
Mycobacterium leprae/genética
Mycobacterium leprae/virologia
Mycobacterium tuberculosis/genética
Mycobacterium tuberculosis/virologia
[Mh] Termos MeSH secundário: Biologia Computacional
Evolução Molecular
Regulação Bacteriana da Expressão Gênica
Regulação Viral da Expressão Gênica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170623
[Lr] Data última revisão:
170623
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161006
[St] Status:MEDLINE


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[PMID]:27672191
[Au] Autor:Mayer O; Jain P; Weisbrod TR; Biro D; Ho L; Jacobs-Sera D; Hatfull GF; Jacobs WR
[Ad] Endereço:Department of Microbiology and Immunology, Albert Einstein College of Medicine, New York, New York, USA.
[Ti] Título:Fluorescent Reporter DS6A Mycobacteriophages Reveal Unique Variations in Infectibility and Phage Production in Mycobacteria.
[So] Source:J Bacteriol;198(23):3220-3232, 2016 Dec 01.
[Is] ISSN:1098-5530
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mycobacteriophage DS6A is unique among the more than 8,000 isolated mycobacteriophages due to its ability to form plaques exclusively on mycobacteria belonging to the Mycobacterium tuberculosis complex (MTBC). Speculation surrounding this specificity has led to unsupported assertions in published studies and patents that nontuberculous mycobacteria (NTM) are wholly resistant to DS6A infection. In this study, we identified two independent nonessential regions in the DS6A genome and replaced them with an mVenus-expressing plasmid to generate fluorescent reporter phages Φ GFP12 and Φ GFP13. We show that even though DS6A is able to form plaques only on MTBC bacteria, infection of various NTM results in mVenus expression in transduced cells. The efficiency of DS6A in delivering DNA varied between NTM species. Additionally, we saw a striking difference in the efficiency of DNA delivery between the closely related members of the Mycobacterium abscessus complex, M. abscessus and Mycobacterium massiliense We also demonstrated that TM4 and DS6A, two phages that do not form plaques on M. massiliense, differ in their ability to deliver DNA, suggesting that there is a phage-specific restriction between mycobacterial species. Phylogenetic analysis reveals that the DS6A genome has a characteristically mosaic structure but provided few insights into the basis for the specificity for MTBC hosts. This study demonstrates that the inability of the MTBC-specific phage DS6A to form plaques on NTM is more complex than previously thought. Moreover, the DS6A-derived fluorophages provide important new tools for the study of mycobacterial biology. IMPORTANCE: The coevolution of bacteria and their infecting phages involves a constant arms race for bacteria to prevent phage infection and phage to overcome these preventions. Although a diverse array of phage defense systems is well characterized in bacteria, very few phage restriction systems are known in mycobacteria. The DS6A mycobacteriophage is unique in the mycobacterial world in that it forms plaques only on members of the Mycobacterium tuberculosis complex. However, the novel DS6A reporter phages developed in this work demonstrate that DS6A can infect nontuberculous mycobacteria at various efficiencies. By comparing the abilities of DS6A and another phage, TM4, to infect and form plaques on various mycobacterial species, we can begin to discern new phage restriction systems employed within the genus.
[Mh] Termos MeSH primário: Micobacteriófagos/fisiologia
Mycobacterium tuberculosis/virologia
Micobactérias não Tuberculosas/virologia
[Mh] Termos MeSH secundário: Genes Reporter
Proteínas de Fluorescência Verde/genética
Proteínas de Fluorescência Verde/metabolismo
Micobacteriófagos/classificação
Micobacteriófagos/genética
Micobacteriófagos/crescimento & desenvolvimento
Filogenia
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
147336-22-9 (Green Fluorescent Proteins)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171020
[Lr] Data última revisão:
171020
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160928
[St] Status:MEDLINE


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[PMID]:27345061
[Au] Autor:Yan S; Xu M; Duan X; Yu Z; Li Q; Xie L; Fan X; Xie J
[Ad] Endereço:Institute of Modern Biopharmaceuticals, State Key Laboratory Breeding Base of Eco-Environment and Bio-Resource of the Three Gorges Area, Key Laboratory of Eco-Environments in Three Gorges Reservoir Region, Ministry of Education, School of Life Sciences, Southwest University, Beibei, Chongqing, 40071
[Ti] Título:Mycobacteriophage putative GTPase-activating protein can potentiate antibiotics.
[So] Source:Appl Microbiol Biotechnol;100(18):8169-77, 2016 Sep.
[Is] ISSN:1432-0614
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The soaring incidences of infection by antimicrobial resistant (AR) pathogens and shortage of effective antibiotics with new mechanisms of action have renewed interest in phage therapy. This scenario is exemplified by resistant tuberculosis (TB), caused by resistant Mycobacterium tuberculosis. Mycobacteriophage SWU1 A321_gp67 encodes a putative GTPase-activating protein. Mycobacterium smegmatis with gp67 overexpression showed changed colony formation and biofilm morphology and supports the efficacy of streptomycin and capreomycin against Mycobacterium. gp67 down-regulated the transcription of genes involved in cell wall and biofilm development. To our knowledge, this is the first report to show that phage protein in addition to lysin or recombination components can synergize with existing antibiotics. Phage components might represent a promising new clue for better antibiotic potentiators.
[Mh] Termos MeSH primário: Antituberculosos/farmacologia
Capreomicina/farmacologia
Ativadores de GTP Fosfo-Hidrolase/metabolismo
Proteínas Ativadoras de GTPase/metabolismo
Micobacteriófagos/enzimologia
Mycobacterium smegmatis/efeitos dos fármacos
Estreptomicina/farmacologia
[Mh] Termos MeSH secundário: Proteínas Ativadoras de GTPase/genética
Micobacteriófagos/genética
Mycobacterium smegmatis/genética
Mycobacterium smegmatis/metabolismo
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antitubercular Agents); 0 (GTP Phosphohydrolase Activators); 0 (GTPase-Activating Proteins); 0 (Recombinant Proteins); 11003-38-6 (Capreomycin); Y45QSO73OB (Streptomycin)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170131
[Lr] Data última revisão:
170131
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160628
[St] Status:MEDLINE
[do] DOI:10.1007/s00253-016-7681-7


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Leäo, Sylvia Cardoso
PubMed Central Texto completo
Texto completo
[PMID]:27316672
[Au] Autor:Lima-Junior JD; Viana-Niero C; Conde Oliveira DV; Machado GE; Rabello MC; Martins-Junior J; Martins LF; Digiampietri LA; da Silva AM; Setubal JC; Russell DA; Jacobs-Sera D; Pope WH; Hatfull GF; Leão SC
[Ad] Endereço:Departamento de Microbiologia, Imunologia e Parasitologia, Escola Paulista de Medicina, Universidade Federal de São Paulo, São Paulo, Brazil.
[Ti] Título:Characterization of mycobacteria and mycobacteriophages isolated from compost at the São Paulo Zoo Park Foundation in Brazil and creation of the new mycobacteriophage Cluster U.
[So] Source:BMC Microbiol;16(1):111, 2016 Jun 17.
[Is] ISSN:1471-2180
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: A large collection of sequenced mycobacteriophages capable of infecting a single host strain of Mycobacterium smegmatis shows considerable genomic diversity with dozens of distinctive types (clusters) and extensive variation within those sharing evident nucleotide sequence similarity. Here we profiled the mycobacterial components of a large composting system at the São Paulo zoo. RESULTS: We isolated and sequenced eight mycobacteriophages using Mycobacterium smegmatis mc(2)155 as a host. None of these eight phages infected any of mycobacterial strains isolated from the same materials. The phage isolates span considerable genomic diversity, including two phages (Barriga, Nhonho) related to Subcluster A1 phages, two Cluster B phages (Pops, Subcluster B1; Godines, Subcluster B2), three Subcluster F1 phages (Florinda, Girafales, and Quico), and Madruga, a relative of phage Patience with which it constitutes the new Cluster U. Interestingly, the two Subcluster A1 phages and the three Subcluster F1 phages have genomic relationships indicating relatively recent evolution within a geographically isolated niche in the composting system. CONCLUSIONS: We predict that composting systems such as those used to obtain these mycobacteriophages will be a rich source for the isolation of additional phages that will expand our view of bacteriophage diversity and evolution.
[Mh] Termos MeSH primário: Micobacteriófagos/genética
Micobacteriófagos/isolamento & purificação
Mycobacterium/genética
Mycobacterium/virologia
Microbiologia do Solo
Solo
[Mh] Termos MeSH secundário: Bacteriófagos/genética
Sequência de Bases
Brasil
DNA Bacteriano/genética
DNA Viral/genética
Evolução Molecular
Genes Bacterianos
Variação Genética
Genoma Viral
Família Multigênica
Micobacteriófagos/classificação
Mycobacterium/classificação
Mycobacterium/isolamento & purificação
Mycobacterium smegmatis/classificação
Mycobacterium smegmatis/genética
Mycobacterium smegmatis/isolamento & purificação
Mycobacterium smegmatis/virologia
Filogenia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Bacterial); 0 (DNA, Viral); 0 (Soil)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160619
[St] Status:MEDLINE
[do] DOI:10.1186/s12866-016-0734-3


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[PMID]:27197018
[Au] Autor:Swift BM; Convery TW; Rees CE
[Ad] Endereço:a School of Veterinary Medicine and Science, University of Nottingham, Sutton Bonington Campus , Nr Loughbotough, Leics , UK.
[Ti] Título:Evidence of Mycobacterium tuberculosis complex bacteraemia in intradermal skin test positive cattle detected using phage-RPA.
[So] Source:Virulence;7(7):779-88, 2016 Oct 02.
[Is] ISSN:2150-5608
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bovine tuberculosis is a zoonotic infectious disease caused by Mycobacterium bovis that affects cattle and can cause tuberculosis in a range of wildlife animals. A bacteriophage-based method combined with PCR (phage-PCR) has been recently used to detect and identify viable pathogenic mycobacteria in the peripheral blood mononuclear cells (PBMCs) of animals suffering from paratuberculosis. To adapt this method for the detection of M. bovis in blood, a new isothermal DNA amplification protocol using Recombinase Polymerase Amplification (RPA) was developed and was found to be able to detect M. bovis BCG within 48 h, with a limit of detection of approximately 10 cells per ml of blood for artificially inoculated blood samples. When blood samples (2 ml) from a Single Comparative Cervical Intradermal Tuberculin (SCCIT)- negative beef herd were tested, Mycobacterium tuberculosis complex (MTC) cells were not detected from any (45) of the blood samples. However when blood samples from SCCIT-positive animals were tested, viable MTC bacteria were detected in 66 % (27/41) of samples. Of these 41 animals sampled, 32 % (13) had visible lesions. In the visible lesion (VL) group, 85 % (11/13) had detectable levels of MTC whereas only 57 % (16/28) of animals which had no visible lesions (NVL) were found to have detectable mycobacteraemia. These results indicated that this simple, rapid method can be applied for the study of M. bovis infections. The frequency with which viable mycobacteria were detected in the peripheral blood of SCCIT-positive animals changes the paradigm of this disease.
[Mh] Termos MeSH primário: Bacteriemia/veterinária
Doenças dos Bovinos/diagnóstico
Mycobacterium bovis/isolamento & purificação
Técnicas de Amplificação de Ácido Nucleico/métodos
Tuberculose Bovina/diagnóstico
[Mh] Termos MeSH secundário: Animais
Bacteriemia/diagnóstico
Bovinos
Doenças dos Bovinos/microbiologia
DNA Bacteriano/genética
Limite de Detecção
Micobacteriófagos
Mycobacterium bovis/genética
Reação em Cadeia da Polimerase
Recombinases/metabolismo
Sensibilidade e Especificidade
Temperatura Ambiente
Teste Tuberculínico/veterinária
Tuberculose Bovina/microbiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Bacterial); 0 (Recombinases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170726
[Lr] Data última revisão:
170726
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160520
[St] Status:MEDLINE
[do] DOI:10.1080/21505594.2016.1191729


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[PMID]:27190284
[Au] Autor:Kirtania P; Ghosh S; Bhawsinghka N; Chakladar M; Das Gupta SK
[Ad] Endereço:Bose Institute, Department Of Microbiology, P1/12 C.I.T. Scheme VIIM, Kolkata 700054, India.
[Ti] Título:Vitamin C induced DevR-dependent synchronization of Mycobacterium smegmatis growth and its effect on the proliferation of mycobacteriophage D29.
[So] Source:FEMS Microbiol Lett;363(11), 2016 06.
[Is] ISSN:1574-6968
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Vitamin C is known to inhibit mycobacterial growth by acting as a hypoxia inducing agent. While investigating how mycobacteriophage growth is influenced by hypoxic conditions induced by vitamin C, using Mycobacterium smegmatis- mycobacteriophage D29 as a model system, it was observed that prior exposure of the host to such conditions resulted in increased burst size of the phage. Vitamin C pre-exposure was also found to induce synchronous growth of the host. A mutant defective in DevR, the response regulator that controls hypoxic responses in mycobacteria, neither supported higher phage bursts nor was it able to undergo synchronized growth following vitamin C pre-exposure, indicating thereby that the two phenomena are interrelated. Further evidence supporting such an interrelationship was obtained from the observation that phage burst sizes varied depending on the stage of synchronous growth that the host cells were in, at the time of infection-higher bursts were observed in the resting/synthetic phases and lower in the dividing ones. The effects were specific in nature as synchronization by an unrelated method, known as 'crowding', did not lead to the same consequence. The results indicate that growth synchronization induced by vitamin C treatment is a DevR-dependent phenomenon which is exploited by mycobacteriophage D29 to grow in larger numbers.
[Mh] Termos MeSH primário: Ácido Ascórbico/farmacologia
Proteínas de Bactérias/metabolismo
Micobacteriófagos/fisiologia
Mycobacterium smegmatis/crescimento & desenvolvimento
Mycobacterium smegmatis/fisiologia
Proteínas Quinases/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Regulação Bacteriana da Expressão Gênica
Mutação
Proteínas Quinases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); EC 2.7.- (Protein Kinases); EC 2.7.3.- (DosR protein, Mycobacterium tuberculosis); PQ6CK8PD0R (Ascorbic Acid)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171126
[Lr] Data última revisão:
171126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160519
[St] Status:MEDLINE



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