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[PMID]:28451521
[Au] Autor:Stolle AS; Norkowski S; Körner B; Schmitz J; Lüken L; Frankenberg M; Rüter C; Schmidt MA
[Ad] Endereço:Institute of Infectiology, Center for Molecular Biology of Inflammation, University of MünsterMünster, Germany.
[Ti] Título:T3SS-Independent Uptake of the Short-Trip Toxin-Related Recombinant NleC Effector of Enteropathogenic Leads to NF-κB p65 Cleavage.
[So] Source:Front Cell Infect Microbiol;7:119, 2017.
[Is] ISSN:2235-2988
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Effector proteins secreted by the type 3 secretion system (T3SS) of pathogenic bacteria have been shown to precisely modulate important signaling cascades of the host for the benefit of the pathogens. Among others, the non-LEE encoded T3SS effector protein NleC of enteropathogenic (EPEC) is a Zn-dependent metalloprotease and suppresses innate immune responses by directly targeting the NF-κB signaling pathway. Many pathogenic bacteria release potent bacterial toxins of the A-B type, which-in contrast to the direct cytoplasmic injection of T3SS effector proteins-are released first into the environment. In this study, we found that NleC displays characteristics of bacterial A-B toxins, when applied to eukaryotic cells as a recombinant protein. Although lacking a B subunit, that typically mediates the uptake of toxins, recombinant NleC (rNleC) induces endocytosis via lipid rafts and follows the endosomal-lysosomal pathway. The conformation of rNleC is altered by low pH to facilitate its escape from acidified endosomes. This is reminiscent of the homologous A-B toxin AIP56 of the fish pathogen ( ). The recombinant protease NleC is functional inside eukaryotic cells and cleaves p65 of the NF-κB pathway. Here, we describe the endocytic uptake mechanism of rNleC, characterize its intracellular trafficking and demonstrate that its specific activity of cleaving p65 requires activation of host cells e.g., by IL1ß. Further, we propose an evolutionary link between some T3SS effector proteins and bacterial toxins from apparently unrelated bacteria. In summary, these properties might suggest rNleC as an interesting candidate for future applications as a potential therapeutic against immune disorders.
[Mh] Termos MeSH primário: Escherichia coli Enteropatogênica/genética
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/toxicidade
Proteínas Recombinantes
Fator de Transcrição RelA/metabolismo
Sistemas de Secreção Tipo III/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Toxinas Bacterianas/metabolismo
Endocitose/efeitos dos fármacos
Proteínas de Escherichia coli/química
Proteínas de Escherichia coli/metabolismo
Proteínas de Escherichia coli/fisiologia
Células HeLa
Interações Hospedeiro-Patógeno
Seres Humanos
Concentração de Íons de Hidrogênio
Interleucina-1beta
Lisossomos/efeitos dos fármacos
NF-kappa B/metabolismo
Photobacterium/metabolismo
Domínios Proteicos
Estrutura Secundária de Proteína
Transporte Proteico
Alinhamento de Sequência
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Toxins); 0 (Escherichia coli Proteins); 0 (Interleukin-1beta); 0 (NF-kappa B); 0 (RELA protein, human); 0 (Recombinant Proteins); 0 (Transcription Factor RelA); 0 (Type III Secretion Systems); 0 (Z0986 protein, E coli)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180216
[Lr] Data última revisão:
180216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.3389/fcimb.2017.00119


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[PMID]:28728127
[Au] Autor:Rozhko TV; Guseynov OA; Guseynova VE; Bondar AA; Devyatlovskaya AN; Kudryasheva NS
[Ad] Endereço:Krasnoyarsk State Medical Academy, 1 P.Zheleznyaka, Krasnoyarsk, 660022, Russia.
[Ti] Título:Is bacterial luminescence response to low-dose radiation associated with mutagenicity?
[So] Source:J Environ Radioact;177:261-265, 2017 Oct.
[Is] ISSN:1879-1700
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Luminous marine bacteria are widely used in bioassays with luminescence intensity being a physiological parameter tested. The purpose of the study was to determine whether bacterial genetic alteration is responsible for bioluminescence kinetics change under low-dose radiation exposure. The alpha-emitting radionuclide Am and beta-emitting radionuclide H were used as the sources of low-dose ionizing radiation. Changes of bioluminescence kinetics of Photobacterium phosphoreum in solutions of Am(NO ) , 7 kBq/L, and tritiated water, 100 MBq/L, were studied; bioluminescence kinetics stages (absence of effect, activation, and inhibition) were determined. Bacterial suspension was sampled at different stages of the bioluminescent kinetics; the doses accumulated by the samples were close or a little higher than a tentative limit of a low-dose interval: 0.10 and 0.85 Gy for Am, or 0.11 and 0.18 Gy for H. Sequence analysis of the 16S ribosomal RNA gene did not reveal a mutagenic effect of low-dose alpha and beta radiation in the bacterial samples. Previous results on bacterial DNA exposed to low-dose gamma radiation (0.25 Gy) were analyzed and compared to those for alpha and beta irradiation. It is concluded that bioluminescence activation and/or inhibition under the applied conditions of low-dose alpha, beta and gamma radioactive exposure is not associated with DNA mutations in the gene sequences tested.
[Mh] Termos MeSH primário: Relação Dose-Resposta à Radiação
Testes de Mutagenicidade
Photobacterium/efeitos da radiação
Dose de Radiação
[Mh] Termos MeSH secundário: Partículas beta
Luminescência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170908
[Lr] Data última revisão:
170908
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170721
[St] Status:MEDLINE


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[PMID]:28665263
[Au] Autor:Li Y; Zhou M; Wang F; Wang ET; Du Z; Wu C; Zhang Z; Liu W; Xie Z
[Ad] Endereço:1​Key Laboratory of Coastal Biology and Utilization, Yantai Institute of Coastal Zone Research, Chinese Academy of Sciences, Yantai 264003, PR China.
[Ti] Título:Photobacterium proteolyticum sp. nov., a protease-producing bacterium isolated from ocean sediments of Laizhou Bay.
[So] Source:Int J Syst Evol Microbiol;67(6):1835-1840, 2017 Jun.
[Is] ISSN:1466-5034
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A protease-producing bacterial strain, 13-12T, was isolated from the ocean sediment of Laizhou Bay, PR China and systematically studied. The bacterium was Gram-stain negative, non spore-forming rods, which were motile with two flagella. It was positive for oxidase, the hydrolysis of starch, agar and gelatin, and for nitrate reduction. It was negative for catalase, esterase and the degradation of CM-cellulose. Optimum growth was observed at 28 °C, pH 6.5-7.0 and in the presence of 2-3 % (w/v) NaCl. Phylogenetic analysis of the 16S rRNA gene, and whole genome data, affiliated it to the genus Photobacterium. It was most closely related to Photobacterium jeanii R-40508T (96.7 % 16S rRNA gene similarity). Strain 13-12T was found to have less than 86.1 % similarities with the type strains of its most closely related species in multi-locus sequence analysis, less than 75.2 % using genome average nucleotide identities (ANI), and less than 18.5 % in DNA-DNA relatedness studies. Q8 was the predominant respiratory menaquinone. Phosphatidylethanolamine, phosphoaminolipid and phospholipid were the major polar phospholipids and summed feature 3 (48.2 %), C16 : 0 (18.4 %) and C18 : 1ω5c (14.1 %) the major fatty acids. The combined phenotypic, phylogenetic, genomic and chemotaxonomic data support this strain representing a novel species of the genus Photobacterium, for which the name Photobacterium proteolyticum sp. nov. is proposed, with 13-12T (=KCTC 42764T=CGMCC 1.14970) as the type strain. The genome size of 13-12T is 6.2 Mbp, comprising 5806 predicted genes and the DNA G+C content is 47.9 mol%.
[Mh] Termos MeSH primário: Sedimentos Geológicos/microbiologia
Photobacterium/classificação
Filogenia
Água do Mar/microbiologia
[Mh] Termos MeSH secundário: Técnicas de Tipagem Bacteriana
Composição de Bases
Baías
China
DNA Bacteriano/genética
Ácidos Graxos/química
Hibridização de Ácido Nucleico
Fosfolipídeos/química
Photobacterium/genética
Photobacterium/isolamento & purificação
RNA Ribossômico 16S/genética
Análise de Sequência de DNA
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Bacterial); 0 (Fatty Acids); 0 (Phospholipids); 0 (RNA, Ribosomal, 16S)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170701
[St] Status:MEDLINE
[do] DOI:10.1099/ijsem.0.001873


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[PMID]:28632300
[Au] Autor:Richard E; Pifferi C; Fiore M; Samain E; Le Gouëllec A; Fort S; Renaudet O; Priem B
[Ad] Endereço:Université Grenoble Alpes and CNRS, CERMAV, 601, rue de la chimie, 38000, Grenoble, France.
[Ti] Título:Chemobacterial Synthesis of a Sialyl-Tn Cyclopeptide Vaccine Candidate.
[So] Source:Chembiochem;18(17):1730-1734, 2017 Sep 05.
[Is] ISSN:1439-7633
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:A conjugatable form of the tumour-associated carbohydrate antigen sialyl-Tn (Neu5Ac-α-2,6-GalNAc) was efficiently produced in Escherichia coli. Metabolically engineered E. coli strains overexpressing the 6-sialyltransferase gene of Photobacterium sp. and CMP-Neu5Ac synthetase genes of Neisseria meningitidis were cultivated at high density in the presence of GalNAc-α-propargyl as the exogenous acceptor. The target disaccharides, which were produced on the scale of several hundreds of milligrams, were then conjugated by using copper(I)-catalysed azide-alkyne cycloaddition click chemistry to a fully synthetic and immunogenic scaffold with the aim to create a candidate anticancer vaccine. Four sialyl-Tn epitopes were introduced on the upper face of an azido-functionalised multivalent cyclopeptide scaffold, the lower face of which was previously modified by an immunogenic polypeptide, PADRE. The ability of the resulting glycoconjugate to interact with oncofoetal sialyl-Tn monoclonal antibodies was confirmed in ELISA assays.
[Mh] Termos MeSH primário: Antígenos Glicosídicos Associados a Tumores/metabolismo
Escherichia coli/metabolismo
Vacinas Sintéticas/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Anticorpos Monoclonais/imunologia
Reações Antígeno-Anticorpo
Antígenos Glicosídicos Associados a Tumores/química
Antígenos Glicosídicos Associados a Tumores/genética
Antígenos Glicosídicos Associados a Tumores/imunologia
Vacinas Anticâncer/genética
Vacinas Anticâncer/imunologia
Vacinas Anticâncer/metabolismo
Cromatografia em Camada Delgada
Química Click
Ensaio de Imunoadsorção Enzimática
Epitopos/química
Epitopos/genética
Epitopos/imunologia
Epitopos/metabolismo
Engenharia Metabólica
Neisseria/enzimologia
Peptídeos Cíclicos/genética
Peptídeos Cíclicos/imunologia
Peptídeos Cíclicos/metabolismo
Photobacterium/enzimologia
Sialiltransferases/genética
Sialiltransferases/metabolismo
Vacinas Sintéticas/genética
Vacinas Sintéticas/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Antigens, Tumor-Associated, Carbohydrate); 0 (Cancer Vaccines); 0 (Epitopes); 0 (Peptides, Cyclic); 0 (Vaccines, Synthetic); 0 (sialosyl-Tn antigen); EC 2.4.99.- (Sialyltransferases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170621
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201700240


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[PMID]:28613143
[Au] Autor:Wang X; Wang Y; Yang X; Sun H; Li B; Zhang XH
[Ad] Endereço:1​College of Marine Life Sciences, Ocean University of China, Qingdao 266003, PR China.
[Ti] Título:Photobacterium alginatilyticum sp. nov., a marine bacterium isolated from bottom seawater.
[So] Source:Int J Syst Evol Microbiol;67(6):1912-1917, 2017 Jun.
[Is] ISSN:1466-5034
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A Gram-straining-negative, facultatively aerobic, rod-shaped strain, motile by a polar flagellum and designated P03D4T, was isolated from the bottom seawater of the East China Sea. Growth occurred at 10-50 °C (optimum 32 °C), pH 5.0-10.0 (optimum pH 6.0) and in the presence of 1-7 % (w/v) NaCl (optimum 3 %). Phylogenetic analysis based on 16S rRNA gene sequence placed P03D4T within the genus Photobacterium of the family Vibrionaceae in the class Gammaproteobacteria, and revealed that strain P03D4T was most closely related to Photobacterium frigidiphilum SL13T with 96.9 % sequence similarity and had sequence similarities with other species of the genus Photobacterium in the range 94.6-96.9 %. The dominant fatty acids were summed feature 3 (C16 : 1ω7c and/or iso-C15 : 0 2-OH) and C16 : 0. The polar lipids of strain P03D4T comprised phosphatidylglycerol, phosphatidylcholine, phosphatidylethanolamine and one unknown lipid. The major respiratory quinone was ubiquinone-8 (Q-8). The DNA G+C content of strain P03D4T was 44.3 mol%. On the basis of the evidence from this polyphasic study, strain P03D4T is proposed as representing a novel species of the genus Photobacterium, for which the name Photobacterium alginatilyticum sp. nov. is proposed. The type strain is P03D4T (=KCTC 52365T=MCCC 1K03200T=CGMCC 1.15764T).
[Mh] Termos MeSH primário: Photobacterium/classificação
Filogenia
Água do Mar/microbiologia
[Mh] Termos MeSH secundário: Técnicas de Tipagem Bacteriana
Composição de Bases
China
DNA Bacteriano/genética
Ácidos Graxos/química
Fosfolipídeos/química
Photobacterium/genética
Photobacterium/isolamento & purificação
RNA Ribossômico 16S/genética
Análise de Sequência de DNA
Ubiquinona/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Bacterial); 0 (Fatty Acids); 0 (Phospholipids); 0 (RNA, Ribosomal, 16S); 1339-63-5 (Ubiquinone); CQA993F7P8 (ubiquinone 8)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170907
[Lr] Data última revisão:
170907
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170615
[St] Status:MEDLINE
[do] DOI:10.1099/ijsem.0.001886


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[PMID]:28359946
[Au] Autor:Núñez-Díaz JA; Fumanal M; Viguera E; Moriñigo MA; Balebona MC
[Ad] Endereço:Universidad de Málaga, Departamento de Microbiología, Campus de Teatinos s/n, 29071 Málaga, Spain.
[Ti] Título:Use of in vivo induced technology to identify antigens expressed by Photobacterium damselae subsp. piscicida during infection of Senegalese sole (Solea senegalensis).
[So] Source:Fish Shellfish Immunol;64:446-456, 2017 May.
[Is] ISSN:1095-9947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Photobacterium damselae subsp. piscicida (Phdp), the causative agent of photobacteriosis, is an important pathogen in marine aquaculture that affects many different fish species worldwide, including Solea senegalensis, an important fish species for aquaculture in the south of Europe. Bacteria express different repertoires of proteins in response to environmental conditions and when invading a host, sense in vivo environment and adapt by changing the expression of specific proteins. In the case of pathogens, identification of genes with up-regulated expression in vivo compared to in vitro conditions might give an insight into the genes relevant to the bacterial virulence. In the present work, in vivo induced antigen technology (IVIAT) has been used to search for Phdp genes only expressed or up-regulated in infected S. senegalensis. An expression library from Phdp was assayed against pooled sera from convalescent S. senegalensis specimens and 18 clones were positive, indicating that proteins encoded are expressed by Phdp during S. senegalensis infection and are immunogenic for this fish species. In addition, five proteins were reactive against adsorbed sera, indicating their in vivo induced character. Inosine-5'-monophosphate dehydrogenase, serine hydroxy methyltransferase and alanyl-tRNA synthethase, involved in aminoacid and nucleotide metabolism, the protein with antioxidant activity alkyl hydroperoxide reductase and a non-ribosomal peptide synthetase responsible for the synthesis of the siderophore piscibactin have been identified as antigens induced in Phdp during S. senegalensis infection. Proteins induced during in vivo growth of Phdp represent promising targets for the development of novel antimicrobial or prophylactic agents in the treatment and prevention of photobacteriosis.
[Mh] Termos MeSH primário: Antígenos de Bactérias/genética
Proteínas de Bactérias/genética
Doenças dos Peixes/imunologia
Linguados
Infecções por Bactérias Gram-Negativas/veterinária
Photobacterium/genética
Photobacterium/imunologia
[Mh] Termos MeSH secundário: Animais
Antígenos de Bactérias/metabolismo
Proteínas de Bactérias/metabolismo
Doenças dos Peixes/metabolismo
Infecções por Bactérias Gram-Negativas/imunologia
Infecções por Bactérias Gram-Negativas/microbiologia
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, Bacterial); 0 (Bacterial Proteins)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170628
[Lr] Data última revisão:
170628
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170401
[St] Status:MEDLINE


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[PMID]:28345146
[Au] Autor:Tabib CR; Brodl E; Macheroux P
[Ad] Endereço:Institute of Biochemistry, Graz University of Technology, Petersgasse 12/II, A-8010, Graz, Austria.
[Ti] Título:Evidence for the generation of myristylated FMN by bacterial luciferase.
[So] Source:Mol Microbiol;104(6):1027-1036, 2017 Jun.
[Is] ISSN:1365-2958
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The genes responsible for the light production in bioluminescent bacteria are present as an operon, luxCDABEG. Many strains of Photobacteria carry an additional gene, termed luxF. X-ray crystallographic analysis of LuxF revealed the presence of four molecules of a flavin derivative, i.e. 6-(3'-(R)-myristyl) flavin adenine mononucleotide (myrFMN) non-covalently bound to the homodimer. In the present study, we exploited the binding of myrFMN to recombinant apo-LuxF to explore the occurrence of myrFMN in various bioluminescent bacteria. MyrFMN was detected in all bacterial strains tested including Vibrio and Aliivibrio indicating that it is more widely occurring in bioluminescent bacteria than previously assumed. We also show that apo-LuxF captures myrFMN and thereby relieves the inhibitory effect on luciferase activity. Thus our results provide support for the hypothesis that LuxF acts as a scavenger of myrFMN in bioluminescent bacteria. However, the source of myrFMN remained obscure. To address this issue, we established a cofactor regeneration enzyme-catalyzed cascade reaction that supports luciferase activity in vitro for up to 3 days. This approach enabled us to unambiguously demonstrate that myrFMN is generated in the bacterial bioluminescent reaction. Based on this finding we postulate a reaction mechanism for myrFMN generation that is based on the luciferase reaction.
[Mh] Termos MeSH primário: FMN Redutase/genética
Mononucleotídeo de Flavina/metabolismo
Luciferases Bacterianas/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/metabolismo
Cristalografia por Raios X
FMN Redutase/metabolismo
Mononucleotídeo de Flavina/química
Flavinas/metabolismo
Cinética
Luciferases/genética
Luciferases/metabolismo
Luciferases Bacterianas/genética
Óperon/genética
Oxirredução
Photobacterium/metabolismo
Ligação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Flavins); 7N464URE7E (Flavin Mononucleotide); EC 1.13.12.- (Luciferases); EC 1.14.14.3 (Luciferases, Bacterial); EC 1.14.14.3 (alkanol monooxygenase (FMN-linked)); EC 1.5.1.38 (FMN Reductase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170921
[Lr] Data última revisão:
170921
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170328
[St] Status:MEDLINE
[do] DOI:10.1111/mmi.13676


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[PMID]:28284618
[Au] Autor:Puentes B; Balado M; Bermúdez-Crespo J; Osorio CR; Lemos ML
[Ad] Endereço:Department of Microbiology and Parasitology, Institute of Aquaculture, Universidade de Santiago de Compostela, Campus Sur, Santiago de Compostela 15782, Spain.
[Ti] Título:A proteomic analysis of the iron response of Photobacterium damselae subsp. damselae reveals metabolic adaptations to iron levels changes and novel potential virulence factors.
[So] Source:Vet Microbiol;201:257-264, 2017 Mar.
[Is] ISSN:1873-2542
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Photobacterium damselae subsp. damselae (Pdd) is a marine bacterium that can infect numerous species of marine fish as well as other species including humans. Low iron availability is one of the signs that bacterial pathogens can detect in order to begin colonizing their host, and the reduction of iron levels is a nonspecific host defense strategy that prevents bacterial proliferation. In this work a proteomic approach was used to study the gene expression adaptations of a Pdd strain in response to iron availability. A comparative analysis of induced proteins in both high- and low-iron conditions showed profound cellular metabolic adaptations that result, for instance, in amino acid requirement. It also provided important information about the changes that occur in the energetic metabolism induced by the surrounding iron levels, allowing for the identification of novel potential virulence factors. Among others, genes involved in the synthesis and transport of a vibrioferrin-like siderophore were identified for the first time. In addition to plasmid pPHDD1-encoded Dly and HlyA hemolysins, a pPHDD1-borne operon, which may encode a transferrin receptor, was also found. This operon identification suggests that this virulence plasmid could encode so-far unknown additional virulence factors other than hemolysins.
[Mh] Termos MeSH primário: Proteínas de Bactérias/genética
Doenças dos Peixes/microbiologia
Linguados/microbiologia
Ferro/metabolismo
Photobacterium/fisiologia
Proteômica
[Mh] Termos MeSH secundário: Adaptação Fisiológica
Animais
Proteínas Hemolisinas/genética
Óperon/genética
Photobacterium/genética
Plasmídeos/genética
Receptores da Transferrina/genética
Sideróforos/genética
Virulência/genética
Fatores de Virulência/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Hemolysin Proteins); 0 (Receptors, Transferrin); 0 (Siderophores); 0 (Virulence Factors); E1UOL152H7 (Iron)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170927
[Lr] Data última revisão:
170927
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170313
[St] Status:MEDLINE


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[PMID]:28127867
[Au] Autor:Thomas B; Lu X; Birmingham WR; Huang K; Both P; Reyes Martinez JE; Young RJ; Davie CP; Flitsch SL
[Ad] Endereço:Manchester Institute of Biotechnology and, School of Chemistry, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK.
[Ti] Título:Application of Biocatalysis to on-DNA Carbohydrate Library Synthesis.
[So] Source:Chembiochem;18(9):858-863, 2017 May 04.
[Is] ISSN:1439-7633
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:DNA-encoded libraries are increasingly used for the discovery of bioactive lead compounds in high-throughput screening programs against specific biological targets. Although a number of libraries are now available, they cover limited chemical space due to bias in ease of synthesis and the lack of chemical reactions that are compatible with DNA tagging. For example, compound libraries rarely contain complex biomolecules such as carbohydrates with high levels of functionality, stereochemistry, and hydrophilicity. By using biocatalysis in combination with chemical methods, we aimed to significantly expand chemical space and generate generic libraries with potentially better biocompatibility. For DNA-encoded libraries, biocatalysis is particularly advantageous, as it is highly selective and can be performed in aqueous environments, which is an essential feature for this split-and-mix library technology. In this work, we demonstrated the application of biocatalysis for the on-DNA synthesis of carbohydrate-based libraries by using enzymatic oxidation and glycosylation in combination with traditional organic chemistry.
[Mh] Termos MeSH primário: Carboidratos/química
DNA/química
Bibliotecas de Moléculas Pequenas/química
[Mh] Termos MeSH secundário: Biocatálise
DNA/metabolismo
Glicoconjugados/química
Glicoconjugados/metabolismo
Glicosilação
Neuraminidase/metabolismo
Oxirredução
Photobacterium/enzimologia
Sialiltransferases/metabolismo
Trypanosoma cruzi/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carbohydrates); 0 (Glycoconjugates); 0 (Small Molecule Libraries); 9007-49-2 (DNA); EC 2.4.99.- (Sialyltransferases); EC 3.2.1.18 (Neuraminidase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170607
[Lr] Data última revisão:
170607
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170128
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201600678


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[PMID]:28126438
[Au] Autor:Brodl E; Ivkovic J; Tabib CR; Breinbauer R; Macheroux P
[Ad] Endereço:Graz University of Technology, Institute of Biochemistry, Petersgasse 12/2, 8010 Graz, Austria.
[Ti] Título:Synthesis of α,ß-unsaturated aldehydes as potential substrates for bacterial luciferases.
[So] Source:Bioorg Med Chem;25(4):1487-1495, 2017 Feb 15.
[Is] ISSN:1464-3391
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Bacterial luciferase catalyzes the monooxygenation of long-chain aldehydes such as tetradecanal to the corresponding acid accompanied by light emission with a maximum at 490nm. In this study even numbered aldehydes with eight, ten, twelve and fourteen carbon atoms were compared with analogs having a double bond at the α,ß-position. These α,ß-unsaturated aldehydes were synthesized in three steps and were examined as potential substrates in vitro. The luciferase of Photobacterium leiognathi was found to convert these analogs and showed a reduced but significant bioluminescence activity compared to tetradecanal. This study showed the trend that aldehydes, both saturated and unsaturated, with longer chain lengths had higher activity in terms of bioluminescence than shorter chain lengths. The maximal light intensity of (E)-tetradec-2-enal was approximately half with luciferase of P. leiognathi, compared to tetradecanal. Luciferases of Vibrio harveyi and Aliivibrio fisheri accepted these newly synthesized substrates but light emission dropped drastically compared to saturated aldehydes. The onset and the decay rate of bioluminescence were much slower, when using unsaturated substrates, indicating a kinetic effect. As a result the duration of the light emission is doubled. These results suggest that the substrate scope of bacterial luciferases is broader than previously reported.
[Mh] Termos MeSH primário: Aldeídos/farmacologia
Aliivibrio fischeri/enzimologia
Luciferases Bacterianas/antagonistas & inibidores
Photobacterium/enzimologia
Vibrio/enzimologia
[Mh] Termos MeSH secundário: Aldeídos/síntese química
Aldeídos/química
Relação Dose-Resposta a Droga
Luciferases Bacterianas/metabolismo
Luminescência
Simulação de Acoplamento Molecular
Estrutura Molecular
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aldehydes); EC 1.14.14.3 (Luciferases, Bacterial)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170128
[St] Status:MEDLINE



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