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Pesquisa : D08.811.277.450.430.400 [Categoria DeCS]
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  1 / 1229 MEDLINE  
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[PMID]:28334607
[Au] Autor:Essuman K; Summers DW; Sasaki Y; Mao X; DiAntonio A; Milbrandt J
[Ad] Endereço:Department of Genetics, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
[Ti] Título:The SARM1 Toll/Interleukin-1 Receptor Domain Possesses Intrinsic NAD Cleavage Activity that Promotes Pathological Axonal Degeneration.
[So] Source:Neuron;93(6):1334-1343.e5, 2017 Mar 22.
[Is] ISSN:1097-4199
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Axonal degeneration is an early and prominent feature of many neurological disorders. SARM1 is the central executioner of the axonal degeneration pathway that culminates in depletion of axonal NAD , yet the identity of the underlying NAD -depleting enzyme(s) is unknown. Here, in a series of experiments using purified proteins from mammalian cells, bacteria, and a cell-free protein translation system, we show that the SARM1-TIR domain itself has intrinsic NADase activity-cleaving NAD into ADP-ribose (ADPR), cyclic ADPR, and nicotinamide, with nicotinamide serving as a feedback inhibitor of the enzyme. Using traumatic and vincristine-induced injury models in neurons, we demonstrate that the NADase activity of full-length SARM1 is required in axons to promote axonal NAD depletion and axonal degeneration after injury. Hence, the SARM1 enzyme represents a novel therapeutic target for axonopathies. Moreover, the widely utilized TIR domain is a protein motif that can possess enzymatic activity.
[Mh] Termos MeSH primário: Proteínas do Domínio Armadillo/metabolismo
Axônios/metabolismo
Domínio Catalítico
Proteínas do Citoesqueleto/metabolismo
NAD+ Nucleosidase/metabolismo
NAD/metabolismo
Degeneração Neural/metabolismo
[Mh] Termos MeSH secundário: Animais
Proteínas do Domínio Armadillo/genética
Axônios/patologia
Células Cultivadas
Proteínas do Citoesqueleto/genética
Seres Humanos
Camundongos
Camundongos Knockout
Degeneração Neural/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Armadillo Domain Proteins); 0 (Cytoskeletal Proteins); 0 (SARM1 protein, mouse); 0U46U6E8UK (NAD); EC 3.2.2.5 (NAD+ Nucleosidase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170929
[Lr] Data última revisão:
170929
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170324
[St] Status:MEDLINE


  2 / 1229 MEDLINE  
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[PMID]:28334598
[Au] Autor:Goldner R; Yaron A
[Ad] Endereço:Department of Biomolecular Sciences, Weizmann Institute of Science, Rehovot 76100, Israel.
[Ti] Título:TIR Axons Apart: Unpredicted NADase Controls Axonal Degeneration.
[So] Source:Neuron;93(6):1239-1241, 2017 Mar 22.
[Is] ISSN:1097-4199
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:SARM1 is a key regulator of axonal degeneration. However, SARM1 mechanism of action is not clear. In this issue of Neuron, Essuman et al. (2017) reveal an intrinsic NADase activity in the SARM1-TIR domain that is required for axonal degeneration.
[Mh] Termos MeSH primário: Proteínas do Domínio Armadillo
NAD+ Nucleosidase
[Mh] Termos MeSH secundário: Axônios
Proteínas do Citoesqueleto
Seres Humanos
Degeneração Neural
Neurônios
Degeneração Walleriana
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Armadillo Domain Proteins); 0 (Cytoskeletal Proteins); 0 (SARM1 protein, human); EC 3.2.2.5 (NAD+ Nucleosidase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170324
[St] Status:MEDLINE


  3 / 1229 MEDLINE  
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[PMID]:28034602
[Au] Autor:Zhu L; Olsen RJ; Lee JD; Porter AR; DeLeo FR; Musser JM
[Ad] Endereço:Center for Molecular and Translational Human Infectious Diseases Research, Houston Methodist Research Institute, Houston, Texas; Department of Pathology and Genomic Medicine, Houston Methodist Hospital, Houston, Texas.
[Ti] Título:Contribution of Secreted NADase and Streptolysin O to the Pathogenesis of Epidemic Serotype M1 Streptococcus pyogenes Infections.
[So] Source:Am J Pathol;187(3):605-613, 2017 Mar.
[Is] ISSN:1525-2191
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Streptococcus pyogenes secretes many toxins that facilitate human colonization, invasion, and dissemination. NADase (SPN) and streptolysin O (SLO) are two toxins that play important roles in pathogenesis. We previously showed that increased production of SPN and SLO in epidemic serotype M1 and M89 S. pyogenes strains is associated with rapid intercontinental spread and enhanced virulence. The biological functions of SPN and SLO have been extensively studied using eukaryotic cell lines, but the relative contribution of each of these two toxins to pathogenesis of epidemic M1 or M89 strains remains unexplored. Herein, using a genetically representative epidemic M1 strain and a panel of isogenic mutant derivative strains, we evaluated the relative contributions of SPN and SLO toxins to virulence in mouse models of necrotizing myositis, bacteremia, and skin and soft tissue infection. We found that isogenic mutants lacking SPN, SLO, and both toxins are equally impaired in ability to cause necrotizing myositis. In addition, mutants lacking either SPN or SLO are significantly attenuated in the bacteremia and soft tissue infection models, and the mutant strain lacking production of both toxins is further attenuated. The mutant strain lacking both SPN and SLO production is severely attenuated in ability to resist killing by human polymorphonuclear leukocytes. We conclude that both SPN and SLO contribute significantly to S. pyogenes pathogenesis in these virulence assays.
[Mh] Termos MeSH primário: NAD+ Nucleosidase/metabolismo
Infecções Estreptocócicas/epidemiologia
Infecções Estreptocócicas/metabolismo
Streptococcus pyogenes/classificação
Streptococcus pyogenes/patogenicidade
Estreptolisinas/metabolismo
[Mh] Termos MeSH secundário: Animais
Proteínas de Bactérias/metabolismo
Modelos Animais de Doenças
Seres Humanos
Evasão da Resposta Imune
Viabilidade Microbiana
Mutação/genética
Neutrófilos/microbiologia
Fenótipo
Sorotipagem
Virulência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Streptolysins); 0 (streptolysin O); EC 3.2.2.5 (NAD+ Nucleosidase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170529
[Lr] Data última revisão:
170529
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:161231
[St] Status:MEDLINE


  4 / 1229 MEDLINE  
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[PMID]:27304511
[Au] Autor:Camacho-Pereira J; Tarragó MG; Chini CCS; Nin V; Escande C; Warner GM; Puranik AS; Schoon RA; Reid JM; Galina A; Chini EN
[Ad] Endereço:Signal Transduction Laboratory, Kogod Aging Center, Department of Anesthesiology, Mayo Clinic College of Medicine, Rochester, MN 55905, USA; Instituto de Bioquímica Médica, Centro de Ciências da Saúde, Universidade Federal do Rio de Janeiro, Cidade Universitária, Ilha do Fundão, Rio de Janeiro, RJ 2
[Ti] Título:CD38 Dictates Age-Related NAD Decline and Mitochondrial Dysfunction through an SIRT3-Dependent Mechanism.
[So] Source:Cell Metab;23(6):1127-1139, 2016 Jun 14.
[Is] ISSN:1932-7420
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nicotinamide adenine dinucleotide (NAD) levels decrease during aging and are involved in age-related metabolic decline. To date, the mechanism responsible for the age-related reduction in NAD has not been elucidated. Here we demonstrate that expression and activity of the NADase CD38 increase with aging and that CD38 is required for the age-related NAD decline and mitochondrial dysfunction via a pathway mediated at least in part by regulation of SIRT3 activity. We also identified CD38 as the main enzyme involved in the degradation of the NAD precursor nicotinamide mononucleotide (NMN) in vivo, indicating that CD38 has a key role in the modulation of NAD-replacement therapy for aging and metabolic diseases.
[Mh] Termos MeSH primário: ADP-Ribosil Ciclase 1/metabolismo
Envelhecimento/metabolismo
Mitocôndrias/metabolismo
NAD/metabolismo
Sirtuína 3/metabolismo
[Mh] Termos MeSH secundário: Animais
Dieta Hiperlipídica
Mamíferos/metabolismo
Camundongos Endogâmicos C57BL
Camundongos Knockout
Mitocôndrias/ultraestrutura
NAD+ Nucleosidase/genética
NAD+ Nucleosidase/metabolismo
Niacinamida/análogos & derivados
Niacinamida/metabolismo
Especificidade de Órgãos
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Messenger); 0I8H2M0L7N (nicotinamide-beta-riboside); 0U46U6E8UK (NAD); 25X51I8RD4 (Niacinamide); EC 3.2.2.5 (NAD+ Nucleosidase); EC 3.2.2.6 (ADP-ribosyl Cyclase 1); EC 3.5.1.- (Sirtuin 3)
[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:160616
[St] Status:MEDLINE


  5 / 1229 MEDLINE  
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[PMID]:27141081
[Au] Autor:Zhu L; Olsen RJ; Horstmann N; Shelburne SA; Fan J; Hu Y; Musser JM
[Ad] Endereço:Center for Molecular and Translational Human Infectious Diseases Research, Houston Methodist Research Institute, and Department of Pathology and Genomic Medicine, Houston Methodist Hospital, Houston, Texas, USA.
[Ti] Título:Intergenic Variable-Number Tandem-Repeat Polymorphism Upstream of rocA Alters Toxin Production and Enhances Virulence in Streptococcus pyogenes.
[So] Source:Infect Immun;84(7):2086-93, 2016 Jul.
[Is] ISSN:1098-5522
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Variable-number tandem-repeat (VNTR) polymorphisms are ubiquitous in bacteria. However, only a small fraction of them has been functionally studied. Here, we report an intergenic VNTR polymorphism that confers an altered level of toxin production and increased virulence in Streptococcus pyogenes The nature of the polymorphism is a one-unit deletion in a three-tandem-repeat locus upstream of the rocA gene encoding a sensor kinase. S. pyogenes strains with this type of polymorphism cause human infection and produce significantly larger amounts of the secreted cytotoxins S. pyogenes NADase (SPN) and streptolysin O (SLO). Using isogenic mutant strains, we demonstrate that deleting one or more units of the tandem repeats abolished RocA production, reduced CovR phosphorylation, derepressed multiple CovR-regulated virulence factors (such as SPN and SLO), and increased virulence in a mouse model of necrotizing fasciitis. The phenotypic effect of the VNTR polymorphism was nearly the same as that of inactivating the rocA gene. In summary, we identified and characterized an intergenic VNTR polymorphism in S. pyogenes that affects toxin production and virulence. These new findings enhance understanding of rocA biology and the function of VNTR polymorphisms in S. pyogenes.
[Mh] Termos MeSH primário: Repetições Minissatélites
Polimorfismo Genético
Streptococcus pyogenes/fisiologia
Estreptolisinas/biossíntese
Transativadores/genética
[Mh] Termos MeSH secundário: Animais
Proteínas de Bactérias/metabolismo
Sequência de Bases
Modelos Animais de Doenças
Feminino
Regulação Bacteriana da Expressão Gênica
Camundongos
NAD+ Nucleosidase/metabolismo
Fenótipo
Fosforilação
Deleção de Sequência
Infecções Estreptocócicas/microbiologia
Infecções Estreptocócicas/mortalidade
Streptococcus pyogenes/patogenicidade
Estreptolisinas/metabolismo
Virulência/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (RocA protein, Streptococcus pyogenes); 0 (Streptolysins); 0 (Trans-Activators); 0 (streptolysin O); EC 3.2.2.5 (NAD+ Nucleosidase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171114
[Lr] Data última revisão:
171114
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160504
[St] Status:MEDLINE
[do] DOI:10.1128/IAI.00258-16


  6 / 1229 MEDLINE  
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[PMID]:26938870
[Au] Autor:Sharma O; O'Seaghdha M; Velarde JJ; Wessels MR
[Ad] Endereço:Division of Infectious Diseases, Boston Children's Hospital, and Department of Pediatrics, Harvard Medical School, Boston, Massachusetts, United States of America.
[Ti] Título:NAD+-Glycohydrolase Promotes Intracellular Survival of Group A Streptococcus.
[So] Source:PLoS Pathog;12(3):e1005468, 2016 Mar.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A global increase in invasive infections due to group A Streptococcus (S. pyogenes or GAS) has been observed since the 1980s, associated with emergence of a clonal group of strains of the M1T1 serotype. Among other virulence attributes, the M1T1 clone secretes NAD+-glycohydrolase (NADase). When GAS binds to epithelial cells in vitro, NADase is translocated into the cytosol in a process mediated by streptolysin O (SLO), and expression of these two toxins is associated with enhanced GAS intracellular survival. Because SLO is required for NADase translocation, it has been difficult to distinguish pathogenic effects of NADase from those of SLO. To resolve the effects of the two proteins, we made use of anthrax toxin as an alternative means to deliver NADase to host cells, independently of SLO. We developed a novel method for purification of enzymatically active NADase fused to an amino-terminal fragment of anthrax toxin lethal factor (LFn-NADase) that exploits the avid, reversible binding of NADase to its endogenous inhibitor. LFn-NADase was translocated across a synthetic lipid bilayer in vitro in the presence of anthrax toxin protective antigen in a pH-dependent manner. Exposure of human oropharyngeal keratinocytes to LFn-NADase in the presence of protective antigen resulted in cytosolic delivery of NADase activity, inhibition of protein synthesis, and cell death, whereas a similar construct of an enzymatically inactive point mutant had no effect. Anthrax toxin-mediated delivery of NADase in an amount comparable to that observed during in vitro infection with live GAS rescued the defective intracellular survival of NADase-deficient GAS and increased the survival of SLO-deficient GAS. Confocal microscopy demonstrated that delivery of LFn-NADase prevented intracellular trafficking of NADase-deficient GAS to lysosomes. We conclude that NADase mediates cytotoxicity and promotes intracellular survival of GAS in host cells.
[Mh] Termos MeSH primário: NAD+ Nucleosidase/metabolismo
Infecções Estreptocócicas/microbiologia
Streptococcus pyogenes/enzimologia
Estreptolisinas/metabolismo
[Mh] Termos MeSH secundário: Antígenos de Bactérias/genética
Antígenos de Bactérias/metabolismo
Proteínas de Bactérias/genética
Proteínas de Bactérias/isolamento & purificação
Proteínas de Bactérias/metabolismo
Toxinas Bacterianas/genética
Toxinas Bacterianas/metabolismo
Sobrevivência Celular
Células Epiteliais/microbiologia
Exotoxinas/metabolismo
Seres Humanos
Espaço Intracelular/enzimologia
Espaço Intracelular/microbiologia
Queratinócitos/microbiologia
Lisossomos/microbiologia
NAD+ Nucleosidase/genética
NAD+ Nucleosidase/isolamento & purificação
Transporte Proteico
Proteínas Recombinantes
Infecções Estreptocócicas/imunologia
Streptococcus pyogenes/imunologia
Streptococcus pyogenes/patogenicidade
Streptococcus pyogenes/fisiologia
Virulência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Antigens, Bacterial); 0 (Bacterial Proteins); 0 (Bacterial Toxins); 0 (Exotoxins); 0 (Recombinant Proteins); 0 (Streptolysins); 0 (anthrax toxin); 0 (streptolysin O); EC 3.2.2.5 (NAD+ Nucleosidase)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:170714
[Lr] Data última revisão:
170714
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160304
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1005468


  7 / 1229 MEDLINE  
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[PMID]:26838722
[Au] Autor:Chandrasekaran S; Caparon MG
[Ad] Endereço:Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, Missouri, USA.
[Ti] Título:The NADase-Negative Variant of the Streptococcus pyogenes Toxin NAD⁺ Glycohydrolase Induces JNK1-Mediated Programmed Cellular Necrosis.
[So] Source:MBio;7(1):e02215-15, 2016 Feb 02.
[Is] ISSN:2150-7511
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:UNLABELLED: Virulence factors are often multifunctional and contribute to pathogenesis through synergistic mechanisms. For the human pathogen Streptococcus pyogenes, two factors that act synergistically are the S. pyogenes NAD(+) glycohydrolase (SPN) and streptolysin O (SLO). Through distinct mechanisms, SLO forms pores in host cell membranes and translocates SPN into the host cell cytosol. Two natural variants of SPN exist, one that exhibits NADase activity and one that lacks this function, and both versions are translocated and act in concert with SLO to cause an accelerated death response in epithelial cells. While NADase(+) SPN is known to trigger a metabolic form of necrosis through the depletion of NAD(+), the mechanism by which NADase(-) SPN induces cell death was unknown. In the studies described here, we examined the pathway of NADase(-) cell death through analysis of activation patterns of mitogen-activated protein kinases (MAPKs). S. pyogenes infection resulted in activation of members of three MAPK subfamilies (p38, ERK, and JNK). However, only JNK was activated in an SLO-specific manner. NADase(-) SPN induced necrosis in HeLa epithelial cells associated with depolarization of mitochondrial membranes, activation of NF-κB, and the generation of reactive oxygen species. Remarkably, RNA interference (RNAi) silencing of JNK protected cells from NADase(-)-SPN-mediated necrosis, suggesting that NADase(-) SPN triggers a form of programmed necrosis dependent on JNK signaling. Taken together, these data demonstrate that SPN acts with SLO to elicit necrosis through two different mechanisms depending on its NADase activity, i.e., metabolic (NADase(+)) or programmed (NADase(-)), leading to distinct inflammatory profiles. IMPORTANCE: Many bacterial pathogens produce toxins that alter how infected host cells interact with the immune system. For Streptococcus pyogenes, two toxins, a NAD(+) glycohydrolase (SPN) and streptolysin O (SLO), act in combination to cause infected cells to die. However, there are two natural forms of SPN, and these variants cause dying cells to produce different types of signaling molecules. The NADase(+) form of SPN kills cells by depleting reserves of NAD(+) and cellular energy. The other form of SPN lacks this activity (NADase(-)); thus, the mechanism by which this variant induces toxicity was unknown. Here, we show that infected cells recognize NADase(-) SPN through a specific signaling molecule called JNK, which causes these cells to undergo a form of cellular suicide known as programmed necrosis. This helps us to understand how different forms of toxins alter host cell signaling to help S. pyogenes cause different types of diseases.
[Mh] Termos MeSH primário: Toxinas Bacterianas/metabolismo
Morte Celular
Células Epiteliais/microbiologia
Células Epiteliais/fisiologia
Proteína Quinase 8 Ativada por Mitógeno/metabolismo
NAD+ Nucleosidase/metabolismo
Streptococcus pyogenes/patogenicidade
[Mh] Termos MeSH secundário: Células HeLa
Seres Humanos
NAD+ Nucleosidase/deficiência
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Bacterial Toxins); EC 2.7.11.24 (Mitogen-Activated Protein Kinase 8); EC 3.2.2.5 (NAD+ Nucleosidase)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160204
[St] Status:MEDLINE


  8 / 1229 MEDLINE  
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[PMID]:26567838
[Au] Autor:Matsumoto M; Yamada K; Suzuki M; Adachi H; Kobayashi S; Yamashita T; Minagawa H; Tatsuno I; Hasegawa T
[Ad] Endereço:Department of Microbiology and Medical Zoology, Aichi Prefectural Institute of Public Health.
[Ti] Título:Description of the Pathogenic Features of Streptococcus pyogenes Isolates from Invasive and Non-Invasive Diseases in Aichi, Japan.
[So] Source:Jpn J Infect Dis;69(4):338-41, 2016 Jul 22.
[Is] ISSN:1884-2836
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:We identified hypervirulent Streptococcus pyogenes in 27 and 420 isolates from patients with invasive and non-invasive diseases, respectively, in Aichi Prefecture, Japan, between 2003 and 2012, in an attempt to understand why the prevalence of streptococcal toxic shock syndrome (STSS) suddenly increased in this location during 2011. Hypervirulent strains belong to the emm1 genotype, with a mutation in the covR/S genes that regulate many other genes, encoding virulence determinants and resulting in the absence of the proteinase streptococcal exotoxin B and the production of virulence factors such as the superantigen streptococcal exotoxin A, the nuclease streptococcal DNase, the cytotoxin NAD-glycohydrolase, and the hemolysin streptolysin O. We found 1 strain from invasive disease and 1 from non-invasive disease with traits similar to those of hypervirulent strains, except that the sda1 gene was absent. We also found 1 non-emm1 strain with phenotypic and genetic traits identical to those of the emm1 hypervirulent strains except that it did not belong to emm1 genotype, from non-invasive diseases cases in 2011. These findings suggested that hypervirulent and hypervirulent-like strains from invasive and non-invasive disease cases could have at least partially contributed to the sudden increase in the number of patients with STSS in Aichi during 2011.
[Mh] Termos MeSH primário: Antígenos de Bactérias/genética
Proteínas da Membrana Bacteriana Externa/genética
Proteínas de Transporte/genética
Desoxirribonuclease I/genética
Regulação Bacteriana da Expressão Gênica
Choque Séptico/patologia
Infecções Estreptocócicas/patologia
Streptococcus pyogenes/genética
Streptococcus pyogenes/patogenicidade
[Mh] Termos MeSH secundário: Antígenos de Bactérias/metabolismo
Proteínas da Membrana Bacteriana Externa/metabolismo
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Proteínas de Transporte/metabolismo
Cisteína Endopeptidases/deficiência
Cisteína Endopeptidases/genética
Desoxirribonuclease I/deficiência
Desoxirribonucleases/genética
Desoxirribonucleases/metabolismo
Exotoxinas/genética
Exotoxinas/metabolismo
Genótipo
Seres Humanos
Peptídeos e Proteínas de Sinalização Intracelular/genética
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Japão/epidemiologia
Mutação
NAD+ Nucleosidase/genética
NAD+ Nucleosidase/metabolismo
Proteínas Repressoras/genética
Proteínas Repressoras/metabolismo
Choque Séptico/diagnóstico
Choque Séptico/epidemiologia
Choque Séptico/microbiologia
Infecções Estreptocócicas/diagnóstico
Infecções Estreptocócicas/epidemiologia
Infecções Estreptocócicas/microbiologia
Streptococcus pyogenes/classificação
Streptococcus pyogenes/isolamento & purificação
Estreptolisinas/genética
Estreptolisinas/metabolismo
Virulência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, Bacterial); 0 (Bacterial Outer Membrane Proteins); 0 (Bacterial Proteins); 0 (Carrier Proteins); 0 (CovS protein, Streptococcus pyogenes); 0 (CsrR protein, Streptococcus pyogenes); 0 (Exotoxins); 0 (Intracellular Signaling Peptides and Proteins); 0 (Repressor Proteins); 0 (Streptolysins); 0 (streptococcal M protein); 0 (streptolysin O); EC 3.1.- (Deoxyribonucleases); EC 3.1.21.1 (Deoxyribonuclease I); EC 3.1.21.1 (Sda1 protein, Streptococcus pyogenes); EC 3.2.2.5 (NAD+ Nucleosidase); EC 3.4.22.- (Cysteine Endopeptidases); EC 3.4.22.10 (streptopain)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170307
[Lr] Data última revisão:
170307
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151117
[St] Status:MEDLINE
[do] DOI:10.7883/yoken.JJID.2015.334


  9 / 1229 MEDLINE  
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[PMID]:26584048
[Au] Autor:Irikura D; Monma C; Suzuki Y; Nakama A; Kai A; Fukui-Miyazaki A; Horiguchi Y; Yoshinari T; Sugita-Konishi Y; Kamata Y
[Ad] Endereço:Division of Microbiology, National Institute of Health Sciences, Tokyo, Japan.
[Ti] Título:Identification and Characterization of a New Enterotoxin Produced by Clostridium perfringens Isolated from Food Poisoning Outbreaks.
[So] Source:PLoS One;10(11):e0138183, 2015.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:There is a strain of Clostridium perfringens, W5052, which does not produce a known enterotoxin. We herein report that the strain W5052 expressed a homologue of the iota-like toxin components sa and sb of C. spiroforme, named Clostridium perfringens iota-like enterotoxin, CPILE-a and CPILE-b, respectively, based on the results of a genome sequencing analysis and a systematic protein screening. In the nicotinamide glyco-hydrolase (NADase) assay the hydrolysis activity was dose-dependently increased by the concentration of rCPILE-a, as judged by the mass spectrometry analysis. In addition, the actin monomer of the lysates of Vero and L929 cells were radiolabeled in the presence of [32P]NAD and rCPILE-a. These findings indicated that CPILE-a possesses ADP-ribosylation activity. The culture supernatant of W5052 facilitated the rounding and killing of Vero and L929 cells, but the rCPILE-a or a non-proteolyzed rCPILE-b did not. However, a trypsin-treated rCPILE-b did. Moreover, a mixture of rCPILE-a and the trypsin-treated rCPILE-b enhanced the cell rounding and killing activities, compared with that induced by the trypsin-treated rCPILE-b alone. The injection of the mixture of rCPILE-a and the trypsin-treated rCPILE-b into an ileum loop of rabbits evoked the swelling of the loop and accumulation of the fluid dose-dependently, suggesting that CPILE possesses enterotoxic activity. The evidence presented in this communication will facilitate the epidemiological, etiological, and toxicological studies of C. perfringens food poisoning, and also stimulate studies on the transfer of the toxins' gene(s) among the Genus Clostridium.
[Mh] Termos MeSH primário: Infecções por Clostridium/microbiologia
Clostridium perfringens/genética
Enterotoxinas/genética
Doenças Transmitidas por Alimentos/microbiologia
[Mh] Termos MeSH secundário: Fatores de Ribosilação do ADP/biossíntese
Fatores de Ribosilação do ADP/genética
Fatores de Ribosilação do ADP/imunologia
Sequência de Aminoácidos
Animais
Sequência de Bases
Cercopithecus aethiops
Infecções por Clostridium/epidemiologia
Clostridium perfringens/isolamento & purificação
Sequência Conservada
Surtos de Doenças
Enterotoxinas/biossíntese
Enterotoxinas/imunologia
Doenças Transmitidas por Alimentos/epidemiologia
Expressão Gênica
Seres Humanos
Íleo/microbiologia
Masculino
Dados de Sequência Molecular
NAD+ Nucleosidase/biossíntese
NAD+ Nucleosidase/genética
NAD+ Nucleosidase/imunologia
Coelhos
Análise de Sequência de DNA
Tóquio
Células Vero
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Enterotoxins); EC 3.2.2.5 (NAD+ Nucleosidase); EC 3.6.5.2 (ADP-Ribosylation Factors)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:151126
[Lr] Data última revisão:
151126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151120
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0138183


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[PMID]:26496597
[Au] Autor:Cabeen MT; Losick R
[Ad] Endereço:Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA.
[Ti] Título:Bacterial backstabbing: EF-Tu, brute?
[So] Source:Cell;163(3):537-9, 2015 Oct 22.
[Is] ISSN:1097-4172
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bacterial type VI secretion is an offensive and defensive weapon that utilizes a molecular warhead to inject toxins into neighboring cells. In this issue of Cell, Whitney et al. report a new class of toxin that disrupts the core metabolism of recipient cells and uncover a surprising requirement for EF-Tu.
[Mh] Termos MeSH primário: Toxinas Bacterianas/metabolismo
NAD+ Nucleosidase/metabolismo
Fator Tu de Elongação de Peptídeos/metabolismo
Pseudomonas aeruginosa/metabolismo
Sistemas de Secreção Tipo VI/química
[Pt] Tipo de publicação:COMMENT; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Toxins); 0 (Type VI Secretion Systems); EC 3.2.2.5 (NAD+ Nucleosidase); EC 3.6.1.- (Peptide Elongation Factor Tu)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:161208
[Lr] Data última revisão:
161208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151027
[St] Status:MEDLINE



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