Base de dados : MEDLINE
Pesquisa : B03.440.400.425.340 [Categoria DeCS]
Referências encontradas : 341 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 35 ir para página                         

  1 / 341 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29339744
[Au] Autor:Lagrange B; Benaoudia S; Wallet P; Magnotti F; Provost A; Michal F; Martin A; Di Lorenzo F; Py BF; Molinaro A; Henry T
[Ad] Endereço:CIRI, Centre International de Recherche en Infectiologie, Inserm, U1111, Université Claude Bernard Lyon 1, CNRS, UMR5308, École Normale Supérieure de Lyon, Univ Lyon, F-69007, Lyon, France.
[Ti] Título:Human caspase-4 detects tetra-acylated LPS and cytosolic Francisella and functions differently from murine caspase-11.
[So] Source:Nat Commun;9(1):242, 2018 01 16.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Caspase-4/5 in humans and caspase-11 in mice bind hexa-acylated lipid A, the lipid moeity of lipopolysaccharide (LPS), to induce the activation of non-canonical inflammasome. Pathogens such as Francisella novicida express an under-acylated lipid A and escape caspase-11 recognition in mice. Here, we show that caspase-4 drives inflammasome responses to F. novicida infection in human macrophages. Caspase-4 triggers F. novicida-mediated, gasdermin D-dependent pyroptosis and activates the NLRP3 inflammasome. Inflammasome activation could be recapitulated by transfection of under-acylated LPS from different bacterial species or synthetic tetra-acylated lipid A into cytosol of human macrophage. Our results indicate functional differences between human caspase-4 and murine caspase-11. We further establish that human Guanylate-binding proteins promote inflammasome responses to under-acylated LPS. Altogether, our data demonstrate a broader reactivity of caspase-4 to under-acylated LPS than caspase-11, which may have important clinical implications for management of sepsis.
[Mh] Termos MeSH primário: Caspases Iniciadoras/metabolismo
Caspases/metabolismo
Francisella/metabolismo
Lipopolissacarídeos/metabolismo
Macrófagos/metabolismo
[Mh] Termos MeSH secundário: Acilação
Animais
Caspases/genética
Caspases Iniciadoras/genética
Células Cultivadas
Citosol/microbiologia
Francisella/fisiologia
Seres Humanos
Inflamassomos/genética
Inflamassomos/metabolismo
Macrófagos/microbiologia
Camundongos Endogâmicos C57BL
Camundongos Knockout
Proteína 3 que Contém Domínio de Pirina da Família NLR/genética
Proteína 3 que Contém Domínio de Pirina da Família NLR/metabolismo
Interferência de RNA
Especificidade da Espécie
Células U937
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Inflammasomes); 0 (Lipopolysaccharides); 0 (NLR Family, Pyrin Domain-Containing 3 Protein); EC 3.4.22.- (CASP4 protein, human); EC 3.4.22.- (Casp11 protein, mouse); EC 3.4.22.- (Caspases); EC 3.4.22.- (Caspases, Initiator)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180118
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02682-y


  2 / 341 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28968459
[Au] Autor:Wallet P; Benaoudia S; Mosnier A; Lagrange B; Martin A; Lindgren H; Golovliov I; Michal F; Basso P; Djebali S; Provost A; Allatif O; Meunier E; Broz P; Yamamoto M; Py BF; Faudry E; Sjöstedt A; Henry T
[Ad] Endereço:CIRI, Centre International de Recherche en Infectiologie, Inserm, U1111, Université Claude Bernard Lyon 1, CNRS, UMR5308, École Normale Supérieure de Lyon, Univ Lyon, Lyon, France.
[Ti] Título:IFN-γ extends the immune functions of Guanylate Binding Proteins to inflammasome-independent antibacterial activities during Francisella novicida infection.
[So] Source:PLoS Pathog;13(10):e1006630, 2017 Oct.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Guanylate binding proteins (GBPs) are interferon-inducible proteins involved in the cell-intrinsic immunity against numerous intracellular pathogens. The molecular mechanisms underlying the potent antibacterial activity of GBPs are still unclear. GBPs have been functionally linked to the NLRP3, the AIM2 and the caspase-11 inflammasomes. Two opposing models are currently proposed to explain the GBPs-inflammasome link: i) GBPs would target intracellular bacteria or bacteria-containing vacuoles to increase cytosolic PAMPs release ii) GBPs would directly facilitate inflammasome complex assembly. Using Francisella novicida infection, we investigated the functional interactions between GBPs and the inflammasome. GBPs, induced in a type I IFN-dependent manner, are required for the F. novicida-mediated AIM2-inflammasome pathway. Here, we demonstrate that GBPs action is not restricted to the AIM2 inflammasome, but controls in a hierarchical manner the activation of different inflammasomes complexes and apoptotic caspases. IFN-γ induces a quantitative switch in GBPs levels and redirects pyroptotic and apoptotic pathways under the control of GBPs. Furthermore, upon IFN-γ priming, F. novicida-infected macrophages restrict cytosolic bacterial replication in a GBP-dependent and inflammasome-independent manner. Finally, in a mouse model of tularemia, we demonstrate that the inflammasome and the GBPs are two key immune pathways functioning largely independently to control F. novicida infection. Altogether, our results indicate that GBPs are the master effectors of IFN-γ-mediated responses against F. novicida to control antibacterial immune responses in inflammasome-dependent and independent manners.
[Mh] Termos MeSH primário: Francisella tularensis/imunologia
Proteínas de Ligação ao GTP/imunologia
Inflamassomos/imunologia
Interferon gama/imunologia
Tularemia/imunologia
[Mh] Termos MeSH secundário: Animais
Modelos Animais de Doenças
Ensaio de Imunoadsorção Enzimática
Feminino
Citometria de Fluxo
Imunofluorescência
Francisella
Técnicas de Silenciamento de Genes
Infecções por Bactérias Gram-Negativas/imunologia
Immunoblotting
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Inflammasomes); 82115-62-6 (Interferon-gamma); EC 3.6.1.- (GTP-Binding Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171018
[Lr] Data última revisão:
171018
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171003
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006630


  3 / 341 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28837612
[Au] Autor:Challacombe JF; Pillai S; Kuske CR
[Ad] Endereço:Bioscience Division, Los Alamos National Laboratory, Los Alamos, New Mexico, United States of America.
[Ti] Título:Shared features of cryptic plasmids from environmental and pathogenic Francisella species.
[So] Source:PLoS One;12(8):e0183554, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Francisella genus includes several recognized species, additional potential species, and other representatives that inhabit a range of incredibly diverse ecological niches, but are not closely related to the named species. Francisella species have been obtained from a wide variety of clinical and environmental sources; documented species include highly virulent human and animal pathogens, fish pathogens, opportunistic human pathogens, tick endosymbionts, and free-living isolates inhabiting brackish water. While more than 120 Francisella genomes have been sequenced to date, only a few contain plasmids, and most of these appear to be cryptic, with unknown benefit to the host cell. We have identified several putative cryptic plasmids in the sequenced genomes of three Francisella novicida and F. novicida-like strains (TX07-6608, AZ06-7470, DPG_3A-IS) and two new Francisella species (F. frigiditurris CA97-1460 and F. opportunistica MA06-7296). These plasmids were compared to each other and to previously identified plasmids from other Francisella species. Some of the plasmids encoded functions potentially involved in replication, conjugal transfer and partitioning, environmental survival (transcriptional regulation, signaling, metabolism), and hypothetical proteins with no assignable functions. Genomic and phylogenetic comparisons of these new plasmids to the other known Francisella plasmids revealed some similarities that add to our understanding of the evolutionary relationships among the diverse Francisella species.
[Mh] Termos MeSH primário: Francisella/genética
Plasmídeos
[Mh] Termos MeSH secundário: Animais
Francisella/classificação
Seres Humanos
Filogenia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170825
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0183554


  4 / 341 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28627495
[Au] Autor:Meyer GR; Lowe GJ; Gilmore SR; Bower SM
[Ad] Endereço:Fisheries and Oceans Canada, Pacific Biological Station, Nanaimo, BC V9T 6N7, Canada.
[Ti] Título:Disease and mortality among Yesso scallops Patinopecten yessoensis putatively caused by infection with Francisella halioticida.
[So] Source:Dis Aquat Organ;125(1):79-84, 2017 Jun 19.
[Is] ISSN:0177-5103
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:During the fall of 2015, up to 40% mortality occurred in juvenile Yesso scallops Patinopecten yessoensis at an aquaculture site in Baynes Sound, British Columbia, Canada. Macroscopic lesions were present in 11% of the scallops, and histopathology consisting of multifocal and diffuse haemocyte infiltration was observed in 44% of the specimens examined. Histologically, small Gram-negative intracellular bacteria-like particles were observed within necrotic haemocytes of the lesions, suggesting a bacterial aetiology. DNA was extracted from adductor muscle lesions of diseased scallops, and the 16s rDNA gene as well as the DNA-directed RNA polymerase beta subunit (rpoB) were amplified by PCR. Sequence analyses of the resulting 413 and 925 bp fragments were a 100% match to the reference sequence for Francisella halioticida, originally described as the cause of mortality in abalone from Japan. Isolation and culture of the bacteria was not possible at the time, as no further diseased specimens were available. Results from in situ hybridization assays as well as examination by transmission electron microscopy provide further evidence supporting the hypothesis that F. halioticida was the most probable causative agent of the lesions and mortality.
[Mh] Termos MeSH primário: Francisella/fisiologia
Pectinidae/microbiologia
[Mh] Termos MeSH secundário: Animais
Interações Hospedeiro-Patógeno
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170831
[Lr] Data última revisão:
170831
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170620
[St] Status:MEDLINE
[do] DOI:10.3354/dao03130


  5 / 341 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28627489
[Au] Autor:Ulanova LS; Pinheiro M; Vibe C; Nunes C; Misaghian D; Wilson S; Zhu K; Fenaroli F; Winther-Larsen HC; Reis S; Griffiths G
[Ad] Endereço:Department of Biosciences, University of Oslo, 0371 Oslo, Norway.
[Ti] Título:Treatment of Francisella infections via PLGA- and lipid-based nanoparticle delivery of antibiotics in a zebrafish model.
[So] Source:Dis Aquat Organ;125(1):19-29, 2017 06 19.
[Is] ISSN:0177-5103
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:We tested the efficiency of 2 different antibiotics, rifampicin and oxolinic acid, against an established infection caused by fish pathogen Francisella noatunensis ssp. orientalis (F.n.o.) in zebrafish. The drugs were tested in the free form as well as encapsulated into biodegradable nanoparticles, either polylactic-co-glycolic acid (PLGA) nanoparticles or nanostructured lipid carriers. The most promising therapies were PLGA-rifampicin nanoparticles and free oxolinic acid; the PLGA nanoparticles significantly delayed embryo mortality while free oxolinic acid prevented it. Encapsulation of rifampicin in both PLGA and nanostructured lipid carriers enhanced its efficiency against F.n.o. infection relative to the free drug. We propose that the zebrafish model is a robust, rapid system for initial testing of different treatments of bacterial diseases important for aquaculture.
[Mh] Termos MeSH primário: Antibacterianos/uso terapêutico
Doenças dos Peixes/microbiologia
Infecções por Bactérias Gram-Negativas/veterinária
Ácido Láctico/química
Lipídeos/química
Nanopartículas/química
Ácido Poliglicólico/química
[Mh] Termos MeSH secundário: Animais
Antibacterianos/administração & dosagem
Doenças dos Peixes/tratamento farmacológico
Francisella
Ácido Oxolínico/administração & dosagem
Ácido Oxolínico/uso terapêutico
Rifampina/administração & dosagem
Rifampina/uso terapêutico
Peixe-Zebra
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Lipids); 0 (polylactic acid-polyglycolic acid copolymer); 26009-03-0 (Polyglycolic Acid); 33X04XA5AT (Lactic Acid); L0A22B22FT (Oxolinic Acid); VJT6J7R4TR (Rifampin)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170831
[Lr] Data última revisão:
170831
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170620
[St] Status:MEDLINE
[do] DOI:10.3354/dao03129


  6 / 341 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28562584
[Au] Autor:Stella S; Alcón P; Montoya G
[Ad] Endereço:Protein Structure &Function Programme, Macromolecular Crystallography Group, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, Copenhagen 2200, Denmark.
[Ti] Título:Structure of the Cpf1 endonuclease R-loop complex after target DNA cleavage.
[So] Source:Nature;546(7659):559-563, 2017 06 22.
[Is] ISSN:1476-4687
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cpf1 is an RNA-guided endonuclease that is emerging as a powerful genome-editing tool. Here we provide insight into its DNA-targeting mechanism by determining the structure of Francisella novicida Cpf1 with the triple-stranded R-loop generated after DNA cleavage. The structure reveals the machinery involved in DNA unwinding to form a CRISPR RNA (crRNA)-DNA hybrid and a displaced DNA strand. The protospacer adjacent motif (PAM) is recognized by the PAM-interacting domain. The loop-lysine helix-loop motif in this domain contains three conserved lysine residues that are inserted in a dentate manner into the double-stranded DNA. Unzipping of the double-stranded DNA occurs in a cleft arranged by acidic and hydrophobic residues facilitating the crRNA-DNA hybrid formation. The PAM single-stranded DNA is funnelled towards the nuclease site through a mixed hydrophobic and basic cavity. In this catalytic conformation, the PAM-interacting domain and the helix-loop-helix motif in the REC1 domain adopt a 'rail' shape and 'flap-on' conformations, respectively, channelling the PAM strand into the cavity. A steric barrier between the RuvC-II and REC1 domains forms the 'septum', separating the displaced PAM strand and the crRNA-DNA hybrid, avoiding DNA re-annealing. Mutations in key residues reveal a mechanism linking the PAM and DNA nuclease sites. Analysis of the Cpf1 structures proposes a singular working model of RNA-guided DNA cleavage, suggesting new avenues for redesign of Cpf1.
[Mh] Termos MeSH primário: Clivagem do DNA
DNA/metabolismo
Endonucleases/química
Endonucleases/metabolismo
Francisella/enzimologia
RNA Guia/metabolismo
[Mh] Termos MeSH secundário: Acidaminococcus/enzimologia
Trifosfato de Adenosina/metabolismo
Pareamento de Bases
Cristalografia por Raios X
DNA/genética
Edição de Genes
Bactérias Gram-Positivas/enzimologia
Lisina/metabolismo
Modelos Moleculares
Domínios Proteicos
Engenharia de Proteínas
RNA Guia/genética
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (RNA, Guide); 8L70Q75FXE (Adenosine Triphosphate); 9007-49-2 (DNA); EC 3.1.- (Endonucleases); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171115
[Lr] Data última revisão:
171115
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170601
[St] Status:MEDLINE
[do] DOI:10.1038/nature22398


  7 / 341 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28550119
[Au] Autor:Kinkead LC; Fayram DC; Allen LH
[Ad] Endereço:Inflammation Program, University of Iowa, Iowa City, Iowa, USA.
[Ti] Título: inhibits spontaneous apoptosis and extends human neutrophil lifespan.
[So] Source:J Leukoc Biol;102(3):815-828, 2017 Sep.
[Is] ISSN:1938-3673
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:is a Gram-negative bacterium that is closely related to the highly virulent facultative intracellular pathogen, Data published by us and others demonstrate that virulence correlates directly with its ability to impair constitutive apoptosis and extend human neutrophil lifespan. In contrast, is attenuated in humans, and the mechanisms that account for this are incompletely defined. Our published data demonstrate that binds natural IgG that is present in normal human serum, which in turn, elicits NADPH oxidase activation that does not occur in response to As it is established that phagocytosis and oxidant production markedly accelerate neutrophil death, we predicted that may influence the neutrophil lifespan in an opsonin-dependent manner. To test this hypothesis, we quantified bacterial uptake, phosphatidylserine (PS) externalization, and changes in nuclear morphology, as well as the kinetics of procaspase-3, -8, and -9 processing and activation. To our surprise, we discovered that not only failed to accelerate neutrophil death but also diminished and delayed apoptosis in a dose-dependent, but opsonin-independent, manner. In keeping with this, studies of conditioned media (CM) showed that neutrophil longevity could be uncoupled from phagocytosis and that stimulated neutrophil secretion of CXCL8. Taken together, the results of this study reveal shared and unique aspects of the mechanisms used by species to manipulate neutrophil lifespan and as such, advance understanding of cell death regulation during infection.
[Mh] Termos MeSH primário: Apoptose/imunologia
Francisella/imunologia
Neutrófilos/imunologia
Fagocitose/imunologia
[Mh] Termos MeSH secundário: Adulto
Caspase 3/imunologia
Caspase 8/imunologia
Caspase 9/imunologia
Ativação Enzimática/imunologia
Seres Humanos
Interleucina-8/imunologia
Neutrófilos/microbiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (IL8 protein, human); 0 (Interleukin-8); EC 3.4.22.- (Caspase 3); EC 3.4.22.- (Caspase 8); EC 3.4.22.- (Caspase 9)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171006
[Lr] Data última revisão:
171006
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170528
[St] Status:MEDLINE
[do] DOI:10.1189/jlb.4MA0117-014R


  8 / 341 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28431230
[Au] Autor:Swarts DC; van der Oost J; Jinek M
[Ad] Endereço:Department of Biochemistry, University of Zurich, CH-8057 Zurich, Switzerland.
[Ti] Título:Structural Basis for Guide RNA Processing and Seed-Dependent DNA Targeting by CRISPR-Cas12a.
[So] Source:Mol Cell;66(2):221-233.e4, 2017 Apr 20.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The CRISPR-associated protein Cas12a (Cpf1), which has been repurposed for genome editing, possesses two distinct nuclease activities: endoribonuclease activity for processing its own guide RNAs and RNA-guided DNase activity for target DNA cleavage. To elucidate the molecular basis of both activities, we determined crystal structures of Francisella novicida Cas12a bound to guide RNA and in complex with an R-loop formed by a non-cleavable guide RNA precursor and a full-length target DNA. Corroborated by biochemical experiments, these structures reveal the mechanisms of guide RNA processing and pre-ordering of the seed sequence in the guide RNA that primes Cas12a for target DNA binding. Furthermore, the R-loop complex structure reveals the strand displacement mechanism that facilitates guide-target hybridization and suggests a mechanism for double-stranded DNA cleavage involving a single active site. Together, these insights advance our mechanistic understanding of Cas12a enzymes and may contribute to further development of genome editing technologies.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Proteínas Associadas a CRISPR/metabolismo
Sistemas CRISPR-Cas
Repetições Palindrômicas Curtas Agrupadas e Regularmente Espaçadas
DNA Bacteriano/metabolismo
Endonucleases/metabolismo
Francisella/enzimologia
Edição de Genes/métodos
Precursores de RNA/metabolismo
RNA Bacteriano/metabolismo
RNA Guia/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Proteínas Associadas a CRISPR/química
Proteínas Associadas a CRISPR/genética
Catálise
DNA Bacteriano/química
DNA Bacteriano/genética
Endonucleases/química
Endonucleases/genética
Escherichia coli/enzimologia
Escherichia coli/genética
Francisella/genética
Modelos Moleculares
Conformação de Ácido Nucleico
Conformação Proteica
Precursores de RNA/química
Precursores de RNA/genética
RNA Bacteriano/química
RNA Bacteriano/genética
RNA Guia/química
RNA Guia/genética
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (CRISPR-Associated Proteins); 0 (DNA, Bacterial); 0 (RNA Precursors); 0 (RNA, Bacterial); 0 (RNA, Guide); EC 3.1.- (Endonucleases)
[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:170422
[St] Status:MEDLINE


  9 / 341 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28402703
[Au] Autor:Ghoneim NH; Abdel-Moein KA; Zaher HM
[Ad] Endereço:Department of Zoonoses, Faculty of Veterinary Medicine, Cairo University , Cairo, Egypt .
[Ti] Título:Molecular Detection of Francisella spp. Among Ticks Attached to Camels in Egypt.
[So] Source:Vector Borne Zoonotic Dis;17(6):384-387, 2017 Jun.
[Is] ISSN:1557-7759
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:This study was conducted to investigate the possible role of camels and attached ticks in the epidemiology of Francisella spp. including Francisella tularensis. For this purpose, a total of 319 ticks (248 Hyalomma dromedarii and 71 Amblyomma spp.) as well as 100 blood and 50 fecal samples collected from camels were screened for the presence of Francisella spp. by PCR through amplification of Francisella 16S rRNA gene. Positive samples were then tested for F. tularensis by PCR. In addition, serum samples from 75 camel abattoir workers were examined for the presence of IgG antibodies against F. tularensis using enzyme-linked immunosorbent assay (ELISA). Of the examined ticks, 15 were positive for Francisella spp. with prevalence of 4.7%, all positive results were recorded in Hyalomma dromedarii (6%). Neither blood nor fecal samples from camels yielded Francisella spp. even camels which carried Francisella spp. positive ticks. Moreover, F. tularensis could not be detected among Francisella-positive ticks. Phylogenetic analysis of some Francisella 16S rRNA gene sequences obtained in this study points out that these sequences are closely related to Francisella-like endosymbionts. In contrast, seroprevalence of F. tularensis antibodies among examined abattoir workers was 9.3% with significantly high prevalence among workers frequently exposed to tick bites (20.7%) rather than occasionally exposed workers (2.2%). In conclusion, however, F. tularensis could not be detected in this study; the high seroprevalence among camel abattoir workers especially those frequently exposed to tick bites underlines the possible role of ticks attached to camels in transmission of tularemia to humans.
[Mh] Termos MeSH primário: Camelus/parasitologia
Francisella/isolamento & purificação
Ixodidae/microbiologia
Infestações por Carrapato/veterinária
[Mh] Termos MeSH secundário: Animais
Egito/epidemiologia
Filogenia
RNA Bacteriano/isolamento & purificação
RNA Ribossômico 16S/genética
Infestações por Carrapato/epidemiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Bacterial); 0 (RNA, Ribosomal, 16S)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170414
[St] Status:MEDLINE
[do] DOI:10.1089/vbz.2016.2100


  10 / 341 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28286149
[Au] Autor:Soto E; Yun S; Lewis J; Kearney MT; Hansen J
[Ad] Endereço:University of California-Davis, Department of Medicine and Epidemiology, School of Veterinary Medicine, Davis, CA 95616, USA. Electronic address: sotomartinez@ucdavis.edu.
[Ti] Título:Interaction of Francisella noatunensis subsp. orientalis with Oreochromis mossambicus bulbus arteriosus cell line.
[So] Source:Microb Pathog;105:326-333, 2017 Apr.
[Is] ISSN:1096-1208
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Francisella noatunensis subsp. orientalis (Fno) (syn. F. asiatica) is an emergent warmwater fish pathogen and the causative agent of piscine francisellosis. Although Fno causes septicemia and can live extracellularly in infected tilapia (Oreochromis spp.), the early interaction of Fno with vasculature endothelium is unknown. In the present study, we examined the interaction of wild-type Fno (WT) and two Fno knockout [intracellular growth loci C (ΔiglC) and pathogenicity determinant protein A (ΔpdpA)] strains with the endothelial O. mossambicus bulbus arteriosus cell line (TmB) at 25 °C and 30 °C. Similar amounts of WT, ΔiglC, and ΔpdpA attached and were detected intracellularly after 5 h of incubation at both temperatures; however temperature affected attachment and uptake. While significantly greater amounts of Fno (WT, ΔiglC, and ΔpdpA) were detected intracellularly when TmB cells were incubated at 30 °C, bacteria attached to TmBs at greater levels at 25 °C. Only WT Fno was able to replicate intracellularly at 25 °C, which resulted in Fno mediated cytotoxicity and apoptosis at 24 and 72 h post-infection. WT Fno incubated at 30 °C as well as ΔiglC, and ΔpdpA incubated at 25 °C and 30 °C were all defective for survival, replication, and the ability to cause cytotoxicity in TmB. Taken together, these results demonstrate that temperature plays a vital role for Fno intracellular survival, persistence and cytotoxicity.
[Mh] Termos MeSH primário: Doenças dos Peixes/microbiologia
Francisella/fisiologia
Tilápia/microbiologia
[Mh] Termos MeSH secundário: Adesinas Bacterianas/genética
Animais
Proteínas de Bactérias/genética
Linhagem Celular
Endotélio/microbiologia
Doenças dos Peixes/patologia
Francisella/genética
Francisella/crescimento & desenvolvimento
Técnicas de Inativação de Genes
Genoma Bacteriano
Infecções por Bactérias Gram-Negativas/microbiologia
Infecções por Bactérias Gram-Negativas/patologia
Infecções por Bactérias Gram-Negativas/veterinária
Interações Hospedeiro-Patógeno
Mutação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adhesins, Bacterial); 0 (Bacterial Proteins)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170505
[Lr] Data última revisão:
170505
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170314
[St] Status:MEDLINE



página 1 de 35 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde