Base de dados : MEDLINE
Pesquisa : G02.111.660.333 [Categoria DeCS]
Referências encontradas : 168 [refinar]
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  1 / 168 MEDLINE  
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[PMID]:28389564
[Au] Autor:Wilson MR; Zha L; Balskus EP
[Ad] Endereço:From the Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138.
[Ti] Título:Natural product discovery from the human microbiome.
[So] Source:J Biol Chem;292(21):8546-8552, 2017 May 26.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Human-associated microorganisms have the potential to biosynthesize numerous secondary metabolites that may mediate important host-microbe and microbe-microbe interactions. However, there is currently a limited understanding of microbiome-derived natural products. A variety of complementary discovery approaches have begun to illuminate this microbial "dark matter," which will in turn allow detailed mechanistic studies of the effects of these molecules on microbiome and host. Herein, we review recent efforts to uncover microbiome-derived natural products, describe the key approaches that were used to identify and characterize these metabolites, discuss potential functional roles of these molecules, and highlight challenges related to this emerging research area.
[Mh] Termos MeSH primário: Microbioma Gastrointestinal/fisiologia
Consórcios Microbianos/fisiologia
[Mh] Termos MeSH secundário: Antibacterianos/biossíntese
Antifúngicos/metabolismo
Antineoplásicos/metabolismo
Seres Humanos
Biossíntese de Peptídeos Independentes de Ácido Nucleico/fisiologia
Peptídeos/metabolismo
Policetídeos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Antifungal Agents); 0 (Antineoplastic Agents); 0 (Peptides); 0 (Polyketides)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170609
[Lr] Data última revisão:
170609
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170409
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.R116.762906


  2 / 168 MEDLINE  
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[PMID]:28108400
[Au] Autor:Sung CT; Chang SL; Entwistle R; Ahn G; Lin TS; Petrova V; Yeh HH; Praseuth MB; Chiang YM; Oakley BR; Wang CC
[Ad] Endereço:Department of Pharmacology and Pharmaceutical Sciences, School of Pharmacy, University of Southern California, Los Angeles, CA 90089, USA. Electronic address: calvin.sung@medsch.ucr.edu.
[Ti] Título:Overexpression of a three-gene conidial pigment biosynthetic pathway in Aspergillus nidulans reveals the first NRPS known to acetylate tryptophan.
[So] Source:Fungal Genet Biol;101:1-6, 2017 Apr.
[Is] ISSN:1096-0937
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Fungal nonribosomal peptide synthetases (NRPSs) are megasynthetases that produce cyclic and acyclic peptides. In Aspergillus nidulans, the NRPS ivoA (AN10576) has been associated with the biosynthesis of grey-brown conidiophore pigments. Another gene, ivoB (AN0231), has been demonstrated to be an N-acetyl-6-hydroxytryptophan oxidase that putatively acts downstream of IvoA. A third gene, ivoC, has also been predicted to be involved in pigment biosynthesis based on publicly available genomic and transcriptomic information. In this paper, we report the replacement of the promoters of the ivoA, ivoB, and ivoC genes with the inducible promoter alcA in a single cotransformation. Co-overexpression of the three genes resulted in the production of a dark-brown pigment in hyphae. In addition, overexpression of each of the Ivo genes, ivoA-C, individually or in combination, allowed us to isolate intermediates and confirm the function of each gene. IvoA was found to be the first known NRPS to carry out the acetylation of the amino acid, tryptophan.
[Mh] Termos MeSH primário: Monofenol Mono-Oxigenase/genética
Biossíntese de Peptídeos Independentes de Ácido Nucleico/genética
Peptídeo Sintases/genética
Pigmentação/genética
[Mh] Termos MeSH secundário: Aspergillus nidulans/enzimologia
Aspergillus nidulans/genética
Proteínas Fúngicas/biossíntese
Proteínas Fúngicas/genética
Regulação Enzimológica da Expressão Gênica
Regulação Fúngica da Expressão Gênica
Família Multigênica/genética
Regiões Promotoras Genéticas
Esporos Fúngicos/genética
Esporos Fúngicos/crescimento & desenvolvimento
Triptofano/biossíntese
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fungal Proteins); 8DUH1N11BX (Tryptophan); EC 1.14.18.- (N-acetyl-6-hydroxytryptophan oxidase); EC 1.14.18.1 (Monophenol Monooxygenase); EC 6.3.2.- (Peptide Synthases); EC 6.3.2.- (non-ribosomal peptide synthase)
[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:170122
[St] Status:MEDLINE


  3 / 168 MEDLINE  
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[PMID]:27900439
[Au] Autor:González O; Ortíz-Castro R; Díaz-Pérez C; Díaz-Pérez AL; Magaña-Dueñas V; López-Bucio J; Campos-García J
[Ad] Endereço:Laboratorio de Biotecnología Microbiana, Instituto de Investigaciones Químico-Biológicas, Universidad Michoacana de San Nicolás de Hidalgo, Edif. B-3, Ciudad Universitaria, 58030, Morelia, Michoacán, México.
[Ti] Título:Non-ribosomal Peptide Synthases from Pseudomonas aeruginosa Play a Role in Cyclodipeptide Biosynthesis, Quorum-Sensing Regulation, and Root Development in a Plant Host.
[So] Source:Microb Ecol;73(3):616-629, 2017 Apr.
[Is] ISSN:1432-184X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Diverse molecules mediate cross-kingdom communication between bacteria and their eukaryotic partners and determine pathogenic or symbiotic relationships. N-acyl-L-homoserine lactone-dependent quorum-sensing signaling represses the biosynthesis of bacterial cyclodipeptides (CDPs) that act as auxin signal mimics in the host plant Arabidopsis thaliana. In this work, we performed bioinformatics, biochemical, and plant growth analyses to identify non-ribosomal peptide synthase (NRPS) proteins of Pseudomonas aeruginosa, which are involved in CDP synthesis. A reverse genetics strategy allowed the identification of the genes encoding putative multi-modular-NRPS (MM-NRPS). Mutations in these genes affected the synthesis of the CDPs cyclo(L-Pro-L-Val), cyclo(L-Pro-L-Leu), and cyclo(L-Pro-L-Tyr), while showing wild-type-like levels of virulence factors, such as violacein, elastase, and pyocyanin. When analyzing the bioactivity of purified, naturally produced CDPs, it was found that cyclo(L-Pro-L-Tyr) and cyclo(L-Pro-L-Val) were capable of antagonizing quorum-sensing-LasR (QS-LasR)-dependent signaling in a contrasting manner in the cell-free supernatants of the selected NRPS mutants, which showed QS induction. Using a bacteria-plant interaction system, we further show that the pvdJ, ambB, and pchE P. aeruginosa mutants failed to repress primary root growth, but improved root branching in A. thaliana seedlings. These results indicated that the CDP production in P. aeruginosa depended on the functional MM-NRPS, which influences quorum-sensing of bacteria and plays a role in root architecture remodeling.
[Mh] Termos MeSH primário: Arabidopsis/microbiologia
Dipeptídeos/metabolismo
Regulação Bacteriana da Expressão Gênica/genética
Biossíntese de Peptídeos Independentes de Ácido Nucleico/genética
Peptídeos Cíclicos/metabolismo
Piperazinas/metabolismo
Raízes de Plantas/embriologia
Pseudomonas aeruginosa/metabolismo
Percepção de Quorum/fisiologia
[Mh] Termos MeSH secundário: Dipeptídeos/genética
Ácidos Indolacéticos/metabolismo
Indóis/metabolismo
Peptídeos Cíclicos/genética
Pseudomonas aeruginosa/enzimologia
Pseudomonas aeruginosa/genética
Piocianina/metabolismo
Percepção de Quorum/genética
Transdução de Sinais
Fatores de Virulência/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Dipeptides); 0 (Indoleacetic Acids); 0 (Indoles); 0 (Peptides, Cyclic); 0 (Piperazines); 0 (Virulence Factors); 0 (cyclo(prolyl-valyl)); 4549-02-4 (maculosin); 9OQM399341 (Pyocyanine); QJH0DSQ3SG (violacein)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161201
[St] Status:MEDLINE
[do] DOI:10.1007/s00248-016-0896-4


  4 / 168 MEDLINE  
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[PMID]:27812802
[Au] Autor:Riquelme C; Enes Dapkevicius ML; Miller AZ; Charlop-Powers Z; Brady S; Mason C; Cheeptham N
[Ad] Endereço:Food Science and Health Group (CITA-A), Departamento de Ciências Agrárias, Universidade dos Açores, Angra do Heroísmo, Açores, Portugal.
[Ti] Título:Biotechnological potential of Actinobacteria from Canadian and Azorean volcanic caves.
[So] Source:Appl Microbiol Biotechnol;101(2):843-857, 2017 Jan.
[Is] ISSN:1432-0614
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Caves are regarded as extreme habitats with appropriate conditions for the development of Actinobacteria. In comparison with other habitats, caves have not yet been the target of intensive screening for bioactive secondary metabolites produced by actinomycetes. As a primary screening strategy, we conducted a metagenomic analysis of the diversity and richness of a key gene required for non-ribosomal peptide (NRP) biosynthesis, focusing on cave-derived sediments from two Canadian caves (a lava tube and a limestone cave) to help us predict whether different types of caves may harbor drug-producing actinobacteria. Using degenerate PCR primers targeting adenylation domains (AD), a conserved domain in the core gene in NRP biosynthesis, a number of amplicons were obtained that mapped back to biomedically relevant NRP gene cluster families. This result guided our culture-dependent sampling strategy of actinomycete isolation from the volcanic caves of Canada (British Columbia) and Portugal (Azores) and subsequent characterization of their antibacterial and enzymatic activities. Multiple enzymatic and antimicrobial activities were identified from bacterial of the Arthrobacter and Streptomyces genera demonstrating that actinomycetes from volcanic caves are promising sources of antibacterial, antibiofilm compounds and industrially relevant enzymes.
[Mh] Termos MeSH primário: Arthrobacter/isolamento & purificação
Produtos Biológicos/metabolismo
Cavernas/microbiologia
Biossíntese de Peptídeos Independentes de Ácido Nucleico/genética
Metabolismo Secundário
Streptomyces/isolamento & purificação
[Mh] Termos MeSH secundário: Antibacterianos/metabolismo
Arthrobacter/genética
Arthrobacter/metabolismo
Açores
Colúmbia Britânica
Biologia Computacional
Enzimas/análise
Genoma Bacteriano
Metagenômica
Streptomyces/genética
Streptomyces/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Biological Products); 0 (Enzymes)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170117
[Lr] Data última revisão:
170117
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161105
[St] Status:MEDLINE
[do] DOI:10.1007/s00253-016-7932-7


  5 / 168 MEDLINE  
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[PMID]:27478992
[Au] Autor:Goering AW; Li J; McClure RA; Thomson RJ; Jewett MC; Kelleher NL
[Ad] Endereço:Department of Molecular Biosciences, and the Feinberg School of Medicine, ‡Department of Chemistry, and §Department of Chemical and Biological Engineering, Northwestern University , Evanston, Illinois 60208, United States.
[Ti] Título:In Vitro Reconstruction of Nonribosomal Peptide Biosynthesis Directly from DNA Using Cell-Free Protein Synthesis.
[So] Source:ACS Synth Biol;6(1):39-44, 2017 01 20.
[Is] ISSN:2161-5063
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Genome sequencing has revealed that a far greater number of natural product biosynthetic pathways exist than there are known natural products. To access these molecules directly and deterministically, a new generation of heterologous expression methods is needed. Cell-free protein synthesis has not previously been used to study nonribosomal peptide biosynthesis, and provides a tunable platform with advantages over conventional methods for protein expression. Here, we demonstrate the use of cell-free protein synthesis to biosynthesize a cyclic dipeptide with correct absolute stereochemistry. From a single-pot reaction, we measured the expression of two nonribosomal peptide synthetases larger than 100 kDa, and detected high-level production of a diketopiperazine. Using quantitative LC-MS and synthetically prepared standard, we observed production of this metabolite at levels higher than previously reported from cell-based recombinant expression, approximately 12 mg/L. Overall, this work represents a first step to apply cell-free protein synthesis to discover and characterize new natural products.
[Mh] Termos MeSH primário: DNA/genética
Biossíntese de Peptídeos Independentes de Ácido Nucleico/genética
[Mh] Termos MeSH secundário: Vias Biossintéticas
Sistema Livre de Células
Cromatografia Líquida
Dipeptídeos/biossíntese
Dipeptídeos/química
Escherichia coli/genética
Escherichia coli/metabolismo
Gramicidina/biossíntese
Gramicidina/química
Técnicas In Vitro
Espectrometria de Massas
Peptídeo Sintases/metabolismo
Peptídeos Cíclicos/biossíntese
Peptídeos Cíclicos/química
Piperazinas/química
Piperazinas/metabolismo
Biologia Sintética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Dipeptides); 0 (Peptides, Cyclic); 0 (Piperazines); 1405-97-6 (Gramicidin); 26488-24-4 (phenylalanyl-prolyl diketopiperazine); 9007-49-2 (DNA); EC 6.3.2.- (Peptide Synthases); EC 6.3.2.- (non-ribosomal peptide synthase)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170526
[Lr] Data última revisão:
170526
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160802
[St] Status:MEDLINE
[do] DOI:10.1021/acssynbio.6b00160


  6 / 168 MEDLINE  
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[PMID]:27917781
[Au] Autor:Schmeing TM
[Ad] Endereço:. martin.schmeing@mcgill.ca.
[Ti] Título:Visualizing A Natural Antibiotic Nanofactory.
[So] Source:Clin Invest Med;39(6):E220-E226, 2016 12 01.
[Is] ISSN:1488-2353
[Cp] País de publicação:Canada
[La] Idioma:eng
[Ab] Resumo:Environmental samples are excellent sources of natural products that possess numerous kinds of therapeutic activities. One important family of natural products is the nonribosomal peptides, which includes penicillin, cyclosporin, viomycin and daptomycin (Cubicin). These peptides are made in bacteria or fungi by large enzymes called nonribosomal peptide synthetases (NRPS). NRPSs are true macromolecular machines or nanofactories, with modular assembly-line logic, a complex catalytic cycle, moving parts and many active sites. Visualization of large fragments of NRPSs at various functional states is required to understand the manner in which NRPSs synthesize their important products. Many excellent structural experiments have been performed to date. Recently, we added to the structural knowledge by visualizing the first module of the NRPS, which makes linear gramicidin, a clinical topical antibiotic, in all its major functional states. These experiments show how the individual domains, including an unusual tailoring domain, function together in assembly-line synthesis. Along with the ever-expanding body of biophysical, biochemical and genetic work, this work brings us closer to a fundamental understanding of these natural antibiotic nanofactories, and perhaps the ability to exploit them to produce novel therapeutics.
[Mh] Termos MeSH primário: Antibacterianos/biossíntese
Bactérias/metabolismo
Bactérias/ultraestrutura
Biossíntese de Peptídeos Independentes de Ácido Nucleico/fisiologia
[Pt] Tipo de publicação:LECTURES; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anti-Bacterial Agents)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170322
[Lr] Data última revisão:
170322
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161206
[St] Status:MEDLINE


  7 / 168 MEDLINE  
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[PMID]:27821051
[Au] Autor:Zhao X; Kuipers OP
[Ad] Endereço:Department of Molecular Genetics, University of Groningen, Nijenborgh 7, Groningen, 9747AG, The Netherlands.
[Ti] Título:Identification and classification of known and putative antimicrobial compounds produced by a wide variety of Bacillales species.
[So] Source:BMC Genomics;17(1):882, 2016 11 07.
[Is] ISSN:1471-2164
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Gram-positive bacteria of the Bacillales are important producers of antimicrobial compounds that might be utilized for medical, food or agricultural applications. Thanks to the wide availability of whole genome sequence data and the development of specific genome mining tools, novel antimicrobial compounds, either ribosomally- or non-ribosomally produced, of various Bacillales species can be predicted and classified. Here, we provide a classification scheme of known and putative antimicrobial compounds in the specific context of Bacillales species. RESULTS: We identify and describe known and putative bacteriocins, non-ribosomally synthesized peptides (NRPs), polyketides (PKs) and other antimicrobials from 328 whole-genome sequenced strains of 57 species of Bacillales by using web based genome-mining prediction tools. We provide a classification scheme for these bacteriocins, update the findings of NRPs and PKs and investigate their characteristics and suitability for biocontrol by describing per class their genetic organization and structure. Moreover, we highlight the potential of several known and novel antimicrobials from various species of Bacillales. CONCLUSIONS: Our extended classification of antimicrobial compounds demonstrates that Bacillales provide a rich source of novel antimicrobials that can now readily be tapped experimentally, since many new gene clusters are identified.
[Mh] Termos MeSH primário: Anti-Infecciosos/metabolismo
Antibiose
Bacillales/fisiologia
Bacteriocinas/biossíntese
[Mh] Termos MeSH secundário: Anti-Infecciosos/farmacologia
Bacillales/classificação
Bacillales/efeitos dos fármacos
Bacteriocinas/genética
Bacteriocinas/farmacologia
Genoma Bacteriano
Família Multigênica
Biossíntese de Peptídeos Independentes de Ácido Nucleico
Peptídeos/genética
Peptídeos/metabolismo
Peptídeos/farmacologia
Filogenia
Policetídeos/metabolismo
Policetídeos/farmacologia
Processamento de Proteína Pós-Traducional
Ribossomos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anti-Infective Agents); 0 (Bacteriocins); 0 (Peptides); 0 (Polyketides)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171119
[Lr] Data última revisão:
171119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161109
[St] Status:MEDLINE


  8 / 168 MEDLINE  
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[PMID]:27694801
[Au] Autor:Dejong CA; Chen GM; Li H; Johnston CW; Edwards MR; Rees PN; Skinnider MA; Webster AL; Magarvey NA
[Ad] Endereço:Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Ontario, Canada.
[Ti] Título:Polyketide and nonribosomal peptide retro-biosynthesis and global gene cluster matching.
[So] Source:Nat Chem Biol;12(12):1007-1014, 2016 Dec.
[Is] ISSN:1552-4469
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Polyketides (PKs) and nonribosomal peptides (NRPs) are profoundly important natural products, forming the foundations of many therapeutic regimes. Decades of research have revealed over 11,000 PK and NRP structures, and genome sequencing is uncovering new PK and NRP gene clusters at an unprecedented rate. However, only ∼10% of PK and NRPs are currently associated with gene clusters, and it is unclear how many of these orphan gene clusters encode previously isolated molecules. Therefore, to efficiently guide the discovery of new molecules, we must first systematically de-orphan emergent gene clusters from genomes. Here we provide to our knowledge the first comprehensive retro-biosynthetic program, generalized retro-biosynthetic assembly prediction engine (GRAPE), for PK and NRP families and introduce a computational pipeline, global alignment for natural products cheminformatics (GARLIC), to uncover how observed biosynthetic gene clusters relate to known molecules, leading to the identification of gene clusters that encode new molecules.
[Mh] Termos MeSH primário: Família Multigênica
Biossíntese de Peptídeos Independentes de Ácido Nucleico
Peptídeos/metabolismo
Policetídeos/metabolismo
[Mh] Termos MeSH secundário: Algoritmos
Família Multigênica/genética
Biossíntese de Peptídeos Independentes de Ácido Nucleico/genética
Peptídeos/química
Peptídeos/genética
Policetídeos/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptides); 0 (Polyketides)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170509
[Lr] Data última revisão:
170509
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161004
[St] Status:MEDLINE
[do] DOI:10.1038/nchembio.2188


  9 / 168 MEDLINE  
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[PMID]:27632173
[Au] Autor:Blättner S; Das S; Paprotka K; Eilers U; Krischke M; Kretschmer D; Remmele CW; Dittrich M; Müller T; Schuelein-Voelk C; Hertlein T; Mueller MJ; Huettel B; Reinhardt R; Ohlsen K; Rudel T; Fraunholz MJ
[Ad] Endereço:Biocenter, Chair of Microbiology, University of Würzburg, Würzburg, Germany.
[Ti] Título:Staphylococcus aureus Exploits a Non-ribosomal Cyclic Dipeptide to Modulate Survival within Epithelial Cells and Phagocytes.
[So] Source:PLoS Pathog;12(9):e1005857, 2016 Sep.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Community-acquired (CA) Staphylococcus aureus cause various diseases even in healthy individuals. Enhanced virulence of CA-strains is partly attributed to increased production of toxins such as phenol-soluble modulins (PSM). The pathogen is internalized efficiently by mammalian host cells and intracellular S. aureus has recently been shown to contribute to disease. Upon internalization, cytotoxic S. aureus strains can disrupt phagosomal membranes and kill host cells in a PSM-dependent manner. However, PSM are not sufficient for these processes. Here we screened for factors required for intracellular S. aureus virulence. We infected escape reporter host cells with strains from an established transposon mutant library and detected phagosomal escape rates using automated microscopy. We thereby, among other factors, identified a non-ribosomal peptide synthetase (NRPS) to be required for efficient phagosomal escape and intracellular survival of S. aureus as well as induction of host cell death. By genetic complementation as well as supplementation with the synthetic NRPS product, the cyclic dipeptide phevalin, wild-type phenotypes were restored. We further demonstrate that the NRPS is contributing to virulence in a mouse pneumonia model. Together, our data illustrate a hitherto unrecognized function of the S. aureus NRPS and its dipeptide product during S. aureus infection.
[Mh] Termos MeSH primário: Dipeptídeos/biossíntese
Células Epiteliais/metabolismo
Viabilidade Microbiana
Biossíntese de Peptídeos Independentes de Ácido Nucleico/fisiologia
Peptídeos Cíclicos/biossíntese
Fagócitos/metabolismo
Staphylococcus aureus/metabolismo
[Mh] Termos MeSH secundário: Animais
Células Epiteliais/citologia
Células Epiteliais/microbiologia
Células HeLa
Seres Humanos
Camundongos
Fagócitos/citologia
Fagócitos/microbiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Dipeptides); 0 (Peptides, Cyclic)
[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:160916
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1005857


  10 / 168 MEDLINE  
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[PMID]:27490569
[Au] Autor:Li YH; Han WJ; Gui XW; Wei T; Tang SY; Jin JM
[Ad] Endereço:Beijing Key Laboratory of Plant Resources Research and Development, Beijing Technology and Business University, Beijing 100048, China. lyhlf11@sina.com.
[Ti] Título:Putative Nonribosomal Peptide Synthetase and Cytochrome P450 Genes Responsible for Tentoxin Biosynthesis in Alternaria alternata ZJ33.
[So] Source:Toxins (Basel);8(8), 2016 08 02.
[Is] ISSN:2072-6651
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Tentoxin, a cyclic tetrapeptide produced by several Alternaria species, inhibits the F1-ATPase activity of chloroplasts, resulting in chlorosis in sensitive plants. In this study, we report two clustered genes, encoding a putative non-ribosome peptide synthetase (NRPS) TES and a cytochrome P450 protein TES1, that are required for tentoxin biosynthesis in Alternaria alternata strain ZJ33, which was isolated from blighted leaves of Eupatorium adenophorum. Using a pair of primers designed according to the consensus sequences of the adenylation domain of NRPSs, two fragments containing putative adenylation domains were amplified from A. alternata ZJ33, and subsequent PCR analyses demonstrated that these fragments belonged to the same NRPS coding sequence. With no introns, TES consists of a single 15,486 base pair open reading frame encoding a predicted 5161 amino acid protein. Meanwhile, the TES1 gene is predicted to contain five introns and encode a 506 amino acid protein. The TES protein is predicted to be comprised of four peptide synthase modules with two additional N-methylation domains, and the number and arrangement of the modules in TES were consistent with the number and arrangement of the amino acid residues of tentoxin, respectively. Notably, both TES and TES1 null mutants generated via homologous recombination failed to produce tentoxin. This study provides the first evidence concerning the biosynthesis of tentoxin in A. alternata.
[Mh] Termos MeSH primário: Ageratina/microbiologia
Alternaria/enzimologia
Proteínas de Bactérias/metabolismo
Sistema Enzimático do Citocromo P-450/metabolismo
Biossíntese de Peptídeos Independentes de Ácido Nucleico
Peptídeo Sintases/metabolismo
Peptídeos Cíclicos/biossíntese
[Mh] Termos MeSH secundário: Alternaria/genética
Sistema Enzimático do Citocromo P-450/genética
Regulação Bacteriana da Expressão Gênica
Regulação Enzimológica da Expressão Gênica
Peptídeo Sintases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Peptides, Cyclic); 9035-51-2 (Cytochrome P-450 Enzyme System); EC 6.3.2.- (Peptide Synthases); EC 6.3.2.- (non-ribosomal peptide synthase); FW4EQ02E0Z (tentoxin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171122
[Lr] Data última revisão:
171122
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160805
[St] Status:MEDLINE



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