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  1 / 98 MEDLINE  
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[PMID]:28449081
[Au] Autor:Luedtke BE; Mahapatra S; Lutter EI; Shaw EI
[Ad] Endereço:Department of Biology, University of Nebraska at Kearney, Kearney, NE 68849, USA.
[Ti] Título:The Coxiella Burnetii type IVB secretion system (T4BSS) component DotA is released/secreted during infection of host cells and during in vitro growth in a T4BSS-dependent manner.
[So] Source:Pathog Dis;75(4), 2017 Jun 01.
[Is] ISSN:2049-632X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Coxiella burnetii is a Gram-negative intracellular pathogen and is the causative agent of the zoonotic disease Q fever. To cause disease, C. burnetii requires a functional type IVB secretion system (T4BSS) to transfer effector proteins required for the establishment and maintenance of a membrane-bound parasitophorous vacuole (PV) and further modulation of host cell process. However, it is not clear how the T4BSS interacts with the PV membrane since neither a secretion pilus nor an extracellular pore forming apparatus has not been described. To address this, we used the acidified citrate cysteine medium (ACCM) along with cell culture infection and immunological techniques to identify the cellular and extracellular localization of T4BSS components. Interestingly, we found that DotA and IcmX were secreted/released in a T4BSS-dependent manner into the ACCM. Analysis of C. burnetii-infected cell lines revealed that DotA colocalized with the host cell marker CD63 (LAMP3) at the PV membrane. In the absence of bacterial protein synthesis, DotA also became depleted from the PV membrane. These data are the first to identify the release/secretion of C. burnetii T4BSS components during axenic growth and the interaction of a T4BSS component with the PV membrane during infection of host cells.
[Mh] Termos MeSH primário: Proteínas de Bactérias/secreção
Coxiella burnetii/crescimento & desenvolvimento
Coxiella burnetii/metabolismo
Interações Hospedeiro-Patógeno
Sistemas de Secreção Tipo IV/metabolismo
Vacúolos/microbiologia
[Mh] Termos MeSH secundário: Proteínas de Bactérias/análise
Tetraspanina 30/análise
Vacúolos/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (CD63 protein, human); 0 (Tetraspanin 30); 0 (Type IV Secretion Systems)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170428
[St] Status:MEDLINE
[do] DOI:10.1093/femspd/ftx047


  2 / 98 MEDLINE  
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[PMID]:28470874
[Au] Autor:Merino E; Flores-Encarnación M; Aguilar-Gutiérrez GR
[Ad] Endereço:Enrique Merino, Departamento de Microbiología Molecular, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Cuernavaca, Morelos, México.
[Ti] Título:Functional interaction and structural characteristics of unique components of Helicobacter pylori T4SS.
[So] Source:FEBS J;284(21):3540-3549, 2017 Nov.
[Is] ISSN:1742-4658
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The Helicobacter pylori infection of the human gastric mucosa causes chronic active gastritis and peptic ulcers and is associated with the development of gastric cancer. Epidemiological studies show that these gastric diseases are related to virulent H. pylori strains that harbor the cytotoxin-associated gene pathogenicity island (cag PAI). The cag PAI is a DNA insertion in the H. pylori chromosome that encodes ~ 27 proteins, including the oncoprotein CagA. Approximately 20 of these proteins have been designated as cag type IV secretion system (T4SS) components. However, only 11 of these proteins share function, structure, and/or sequence similarities with the prototypical VirB/VirD4 T4SS of Agrobacterium tumefaciens. The VirB/VirD4 orthologs of the cag T4SS of H. pylori are required for CagA translocation and stimulate the gastric epithelial cells to produce and secrete interleukin-8 (IL-8). The cag PAI encodes eight additional proteins, such as Cag3 (Cagδ/HP0522), CagM (Cag16/HP0537), CagU (Cag11/HP0531), CagI (Cag19/HP0540), and CagH (Cag20/HP0541), which are also required for the translocation of CagA and IL-8 secretion, meanwhile CagF (Cag22/HP0543), CagG (Cag21/HP0542), and CagZ (Cag6/HP0526) are just required for the translocation of CagA. However, relatively little is known about their functions and structural organization because they exhibit a nondetectable sequence similarity with T4SS components in the current databases. In this review, we conducted an exhaustive analysis of the literature to present the biochemistry, putative role, localization, and interactions of each of these eight additional cag T4SS components.
[Mh] Termos MeSH primário: Helicobacter pylori/química
Sistemas de Secreção Tipo IV
[Mh] Termos MeSH secundário: Helicobacter pylori/metabolismo
Modelos Moleculares
Sistemas de Secreção Tipo IV/química
Sistemas de Secreção Tipo IV/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Type IV Secretion Systems)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1111/febs.14092


  3 / 98 MEDLINE  
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[PMID]:28452085
[Au] Autor:Gordon JE; Costa TRD; Patel RS; Gonzalez-Rivera C; Sarkar MK; Orlova EV; Waksman G; Christie PJ
[Ad] Endereço:Department of Microbiology and Molecular Genetics, McGovern Medical School, 6431 Fannin St, Houston, TX, 77030, USA.
[Ti] Título:Use of chimeric type IV secretion systems to define contributions of outer membrane subassemblies for contact-dependent translocation.
[So] Source:Mol Microbiol;105(2):273-293, 2017 Jul.
[Is] ISSN:1365-2958
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Recent studies have shown that conjugation systems of Gram-negative bacteria are composed of distinct inner and outer membrane core complexes (IMCs and OMCCs, respectively). Here, we characterized the OMCC by focusing first on a cap domain that forms a channel across the outer membrane. Strikingly, the OMCC caps of the Escherichia coli pKM101 Tra and Agrobacterium tumefaciens VirB/VirD4 systems are completely dispensable for substrate transfer, but required for formation of conjugative pili. The pKM101 OMCC cap and extended pilus also are dispensable for activation of a Pseudomonas aeruginosa type VI secretion system (T6SS). Chimeric conjugation systems composed of the IMC joined to OMCCs from the A. tumefaciens VirB/VirD4, E. coli R388 Trw, and Bordetella pertussis Ptl systems support conjugative DNA transfer in E. coli and trigger P. aeruginosa T6SS killing, but not pilus production. The A. tumefaciens VirB/VirD4 OMCC, solved by transmission electron microscopy, adopts a cage structure similar to the pKM101 OMCC. The findings establish that OMCCs are highly structurally and functionally conserved - but also intrinsically conformationally flexible - scaffolds for translocation channels. Furthermore, the OMCC cap and a pilus tip protein coregulate pilus extension but are not required for channel assembly or function.
[Mh] Termos MeSH primário: Proteínas da Membrana Bacteriana Externa/metabolismo
Conjugação Genética/genética
[Mh] Termos MeSH secundário: Agrobacterium tumefaciens/genética
Proteínas da Membrana Bacteriana Externa/fisiologia
Proteínas de Bactérias/metabolismo
DNA Bacteriano/metabolismo
Proteínas de Ligação a DNA/metabolismo
Escherichia coli/genética
Fímbrias Bacterianas/metabolismo
Ligação Proteica
Transporte Proteico/genética
Sistemas de Secreção Tipo IV/genética
Sistemas de Secreção Tipo IV/metabolismo
Fatores de Virulência/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Outer Membrane Proteins); 0 (Bacterial Proteins); 0 (DNA, Bacterial); 0 (DNA-Binding Proteins); 0 (Type IV Secretion Systems); 0 (Virulence Factors)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1111/mmi.13700


  4 / 98 MEDLINE  
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[PMID]:28923826
[Au] Autor:Redzej A; Ukleja M; Connery S; Trokter M; Felisberto-Rodrigues C; Cryar A; Thalassinos K; Hayward RD; Orlova EV; Waksman G
[Ad] Endereço:Department of Biological Sciences, Institute of Structural and Molecular Biology, Birkbeck, London, UK.
[Ti] Título:Structure of a VirD4 coupling protein bound to a VirB type IV secretion machinery.
[So] Source:EMBO J;36(20):3080-3095, 2017 Oct 16.
[Is] ISSN:1460-2075
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Type IV secretion (T4S) systems are versatile bacterial secretion systems mediating transport of protein and/or DNA T4S systems are generally composed of 11 VirB proteins and 1 VirD protein (VirD4). The VirB1-11 proteins assemble to form a secretion machinery and a pilus while the VirD4 protein is responsible for substrate recruitment. The structure of VirD4 in isolation is known; however, its structure bound to the VirB1-11 apparatus has not been determined. Here, we purify a T4S system with VirD4 bound, define the biochemical requirements for complex formation and describe the protein-protein interaction network in which VirD4 is involved. We also solve the structure of this complex by negative stain electron microscopy, demonstrating that two copies of VirD4 dimers locate on both sides of the apparatus, in between the VirB4 ATPases. Given the central role of VirD4 in type IV secretion, our study provides mechanistic insights on a process that mediates the dangerous spread of antibiotic resistance genes among bacterial populations.
[Mh] Termos MeSH primário: Agrobacterium tumefaciens/ultraestrutura
Substâncias Macromoleculares/isolamento & purificação
Substâncias Macromoleculares/ultraestrutura
Sistemas de Secreção Tipo IV/isolamento & purificação
Sistemas de Secreção Tipo IV/ultraestrutura
[Mh] Termos MeSH secundário: Agrobacterium tumefaciens/genética
Conjugação Genética
Microscopia Eletrônica de Transmissão
Mapas de Interação de Proteínas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Macromolecular Substances); 0 (Type IV Secretion Systems)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171020
[Lr] Data última revisão:
171020
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170920
[St] Status:MEDLINE
[do] DOI:10.15252/embj.201796629


  5 / 98 MEDLINE  
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[PMID]:28863473
[Au] Autor:Laverde D; Probst I; Romero-Saavedra F; Kropec A; Wobser D; Keller W; Grohmann E; Huebner J
[Ad] Endereço:Division of Pediatric Infectious Diseases, Dr. von Hauner Children's Hospital, Ludwig Maximilians University, Munich.
[Ti] Título:Targeting Type IV Secretion System Proteins to Combat Multidrug-Resistant Gram-positive Pathogens.
[So] Source:J Infect Dis;215(12):1836-1845, 2017 Jun 15.
[Is] ISSN:1537-6613
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:For many gram-positive pathogens, conjugative plasmid transfer is an important means of spreading antibiotic resistance . Therefore, the search for alternative treatments to fight and prevent infections caused by these bacteria has become of major interest. In the present study, we evaluated the protein TraM, from the conjugative plasmid pIP501, as a potential vaccine candidate. Anti-TraM antiserum mediated in vitro opsonophagocytic killing of the strain harboring the pIP501 plasmid and also proved to be cross-reactive against other clinically relevant enterococcal and staphylococcal strains. Specificity of antibodies toward TraM was confirmed by results of an opsonophagocytic inhibition assay and Western blot. In addition, conjugative transfer experiments proved that TraM is essential for the transfer of pIP501. Finally, immunization with either TraM or anti-TraM antiserum reduced significantly the colony counts in mice livers, demonstrating that TraM is a promising vaccine candidate against enterococci and other gram-positive pathogens.
[Mh] Termos MeSH primário: Proteínas de Bactérias/imunologia
Vacinas Bacterianas/imunologia
Farmacorresistência Bacteriana Múltipla/imunologia
Enterococcus faecalis/imunologia
Escherichia coli/imunologia
Sistemas de Secreção Tipo IV/imunologia
[Mh] Termos MeSH secundário: Animais
Proteínas de Bactérias/genética
Western Blotting
Enterococcus faecalis/genética
Escherichia coli/genética
Feminino
Fígado/microbiologia
Camundongos
Camundongos Endogâmicos BALB C
Plasmídeos
Transporte Proteico
Coelhos
Staphylococcus aureus/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Bacterial Vaccines); 0 (Type IV Secretion Systems); 104042-79-7 (TraM protein, bacterial)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170907
[Lr] Data última revisão:
170907
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170903
[St] Status:MEDLINE
[do] DOI:10.1093/infdis/jix227


  6 / 98 MEDLINE  
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[PMID]:28813514
[Au] Autor:Dela Pena-Ponce MG; Jimenez MT; Hansen LM; Solnick JV; Miller LA
[Ad] Endereço:California National Primate Research Center, University of California Davis, Davis, California, United States of America.
[Ti] Título:The Helicobacter pylori type IV secretion system promotes IL-8 synthesis in a model of pediatric airway epithelium via p38 MAP kinase.
[So] Source:PLoS One;12(8):e0183324, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Epidemiologic studies have reported an inverse relationship between childhood Helicobacter pylori infection and development of allergic asthma. Because lung epithelium plays an important role in allergic asthma pathogenesis, we hypothesized that H. pylori may directly influence airway epithelial cell innate immune function, particularly in early childhood. To test our hypothesis, we established an in vitro H. pylori infection model using primary tracheobronchial epithelial cell cultures derived from infant, juvenile and adult rhesus monkeys. Airway epithelial cell cultures were infected with wild-type or cag pathogenicity island mutant H. pylori strains, followed by evaluation of IL-8 and IL-6 protein synthesis. We found that H. pylori primarily increased IL-8 synthesis in a MOI and age-dependent fashion, with a greater than 4-fold induction in infant versus adult cultures. H. pylori-induced IL-8 synthesis in infant and juvenile cultures was significantly reduced by cag pathogenicity island mutants, indicating a requirement for the type IV secretion system. Although peptidoglycan recognition of nucleotide binding oligomerization domain-containing protein 1 (NOD1) and NF-kappaB have been implicated as key cytokine signaling molecules for H. pylori infection in gastric epithelium, NOD1 (ML130) or NF-kappaB (JSH-23) inhibitors minimally affected IL-8 synthesis in airway epithelial cell cultures following H. pylori infection. In contrast, inhibition of the p38 MAP kinase pathway (SB203580) resulted in almost complete suppression of H. pylori-induced IL-8 synthesis. Collectively, these results indicate that H. pylori can preferentially elicit IL-8 synthesis in a model of pediatric airway epithelium using the type IV secretion system via p38 MAP kinase.
[Mh] Termos MeSH primário: Helicobacter pylori/fisiologia
Interleucina-8/metabolismo
Mucosa Respiratória/imunologia
Mucosa Respiratória/microbiologia
Sistemas de Secreção Tipo IV/metabolismo
Proteínas Quinases p38 Ativadas por Mitógeno/metabolismo
[Mh] Termos MeSH secundário: Animais
Proteínas de Bactérias/metabolismo
Linhagem Celular
Infecções por Helicobacter/metabolismo
Helicobacter pylori/metabolismo
Seres Humanos
Técnicas In Vitro
Interleucina-6/metabolismo
Primatas
Mucosa Respiratória/enzimologia
Transdução de Sinais/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Interleukin-6); 0 (Interleukin-8); 0 (Type IV Secretion Systems); EC 2.7.11.24 (p38 Mitogen-Activated Protein Kinases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171013
[Lr] Data última revisão:
171013
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170817
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0183324


  7 / 98 MEDLINE  
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[PMID]:28808128
[Au] Autor:Burbank LP; Van Horn CR
[Ad] Endereço:U.S. Department of Agriculture-Agricultural Research Service, San Joaquin Valley Agricultural Sciences Center, Parlier, California, USA lindsey.burbank@ars.usda.gov.
[Ti] Título:Conjugative Plasmid Transfer in Xylella fastidiosa Is Dependent on and Operon Functions.
[So] Source:J Bacteriol;199(21), 2017 Nov 01.
[Is] ISSN:1098-5530
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The insect-transmitted plant pathogen is capable of efficient horizontal gene transfer (HGT) and recombination. Natural transformation occurs at high rates in , but there also is evidence that certain strains of carry native plasmids equipped with transfer and mobilization genes, suggesting conjugation as an additional mechanism of HGT in some instances. Two operons, and , putatively encoding a conjugative type IV secretion system, are found in some but not all isolates, often on native plasmids. strains that carry the conjugative transfer genes can belong to different subspecies and frequently differ in host ranges. Using strain M23 ( subsp. ) or Dixon ( subsp. ) as the donor strain and Temecula ( subsp. ) as the recipient strain, plasmid transfer was characterized using the mobilizable broad-host-range vector pBBR5pemIK. Transfer of plasmid pBBR5pemIK was observed under conditions with both donor strains and was dependent on both and operon functions. A conjugative mechanism likely contributes to gene transfer between diverse strains of , possibly facilitating adaptation to new environments or different hosts. is an important plant pathogen worldwide, infecting a wide range of different plant species. The emergence of new diseases caused by , or host switching of existing strains, is thought to be primarily due to the high frequency of HGT and recombination in this pathogen. Transfer of plasmids by a conjugative mechanism enables movement of larger amounts of genetic material at one time, compared with other routes of gene transfer such as natural transformation. Establishing the prevalence and functionality of this mechanism in contributes to a better understanding of HGT, adaptation, and disease emergence in this diverse pathogen.
[Mh] Termos MeSH primário: Conjugação Genética
Transferência Genética Horizontal
Genes Bacterianos
Óperon
Plasmídeos
Xylella/genética
[Mh] Termos MeSH secundário: Sistemas de Secreção Tipo IV/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Type IV Secretion Systems)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171009
[Lr] Data última revisão:
171009
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170816
[St] Status:MEDLINE


  8 / 98 MEDLINE  
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[PMID]:28766702
[Au] Autor:Sharifahmadian M; Nlend IU; Lecoq L; Omichinski JG; Baron C
[Ad] Endereço:Department of Biochemistry and Molecular Medicine, Faculty of Medicine, Université de Montréal, QC, Canada.
[Ti] Título:The type IV secretion system core component VirB8 interacts via the ß1-strand with VirB10.
[So] Source:FEBS Lett;591(16):2491-2500, 2017 Aug.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In this work, we provide evidence for the interactions between VirB8 and VirB10, two core components of the type IV secretion system (T4SS). Using nuclear magnetic resonance experiments, we identified residues on the ß1-strand of Brucella VirB8 that undergo chemical shift changes in the presence of VirB10. Bacterial two-hybrid experiments confirm the importance of the ß1-strand, whereas phage display experiments suggest that the α2-helix of VirB8 may also contribute to the interaction with VirB10. Conjugation assays using the VirB8 homolog TraE as a model show that several residues on the ß1-strand of TraE are important for T4SS function. Together, our results suggest that the ß1-strand of VirB8-like proteins is essential for their interaction with VirB10 in the T4SS complex.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Proteínas de Bactérias/metabolismo
Sistemas de Secreção Tipo IV/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Brucella/metabolismo
Modelos Moleculares
Ligação Proteica
Conformação Proteica em Folha beta
[Pt] Tipo de publicação:LETTER
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Type IV Secretion Systems)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171002
[Lr] Data última revisão:
171002
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170803
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12770


  9 / 98 MEDLINE  
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[PMID]:28759055
[Au] Autor:Alandiyjany MN; Croxall NJ; Grove JI; Delahay RM
[Ad] Endereço:NIHR Nottingham Digestive Diseases Biomedical Research Unit, Nottingham University Hospitals NHS Trust and University of Nottingham, Nottingham, United Kingdom.
[Ti] Título:A role for the tfs3 ICE-encoded type IV secretion system in pro-inflammatory signalling by the Helicobacter pylori Ser/Thr kinase, CtkA.
[So] Source:PLoS One;12(7):e0182144, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Two distinct type IV secretion systems (T4SSs) can be identified in certain Helicobacter pylori strains, encoded on mobile genetic elements termed tfs3 and tfs4. Although their function remains unknown, both have been implicated in clinical outcomes of H. pylori infection. Here we provide evidence that the Tfs3 T4SS is required for activity of the pro-inflammatory Ser/Thr kinase protein, CtkA, in a gastric epithelial cell infection model. Previously, purified recombinant CtkA protein has been shown to upregulate NF-kappaB signalling and induce TNF-alpha and IL-8 cytokine secretion from cultured macrophages suggesting that it may potentiate the H. pylori-mediated inflammatory response. In this study, we show that CtkA expressed from its native host, H. pylori has a similar capacity for stimulation of a pro-inflammatory response from gastric epithelial cells. CtkA interaction was found to be dependent upon a complement of tfs3 T4SS genes, but independent of the T4SSs encoded by either tfs4 or the cag pathogenicity island. Moreover, the availability of CtkA for host cell interaction was shown to be conditional upon the carboxyl-terminus of CtkA, encoding a putative conserved secretion signal common to other variably encoded Tfs3 proteins. Collectively, our observations indicate a role for the Tfs3 T4SS in CtkA-mediated pro-inflammatory signalling by H. pylori and identify CtkA as a likely Tfs3 T4SS secretion substrate.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Helicobacter pylori/metabolismo
Proteínas Serina-Treonina Quinases/metabolismo
Transdução de Sinais
Sistemas de Secreção Tipo IV/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Linhagem Celular
Citocinas/genética
Citocinas/metabolismo
Células Epiteliais/metabolismo
Células Epiteliais/microbiologia
Helicobacter pylori/genética
Helicobacter pylori/patogenicidade
Seres Humanos
Domínios Proteicos
Proteínas Serina-Treonina Quinases/química
Proteínas Serina-Treonina Quinases/genética
Sistemas de Secreção Tipo IV/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Cytokines); 0 (Type IV Secretion Systems); EC 2.7.11.1 (CtkA protein, Helicobacter pylori); EC 2.7.11.1 (Protein-Serine-Threonine Kinases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170920
[Lr] Data última revisão:
170920
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170801
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0182144


  10 / 98 MEDLINE  
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[PMID]:28713154
[Au] Autor:Qiu J; Luo ZQ
[Ad] Endereço:Center of Infection and Immunity, The First Hospital, Jilin University, Changchun 130001, China.
[Ti] Título:Legionella and Coxiella effectors: strength in diversity and activity.
[So] Source:Nat Rev Microbiol;15(10):591-605, 2017 Oct.
[Is] ISSN:1740-1534
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Legionella pneumophila and Coxiella burnetii are two evolutionarily related intracellular pathogens that use the Dot/Icm type IV secretion system to translocate effectors into host cells. These effectors are essential for the establishment of membrane-bound compartments known as replication vacuoles, which enable the survival and replication of bacteria inside host cells. The effectors interfere with diverse signalling pathways to co-opt host processes, such as vesicle trafficking, ubiquitylation, gene expression and lipid metabolism, to promote pathogen survival. In this Review, we explore Dot/Icm effectors from L. pneumophila and C. burnetii as key virulence factors, and we examine the biochemical and cell biological functions of these effectors and their roles in our understanding of bacterial virulence.
[Mh] Termos MeSH primário: Coxiella burnetii/patogenicidade
Legionella pneumophila/patogenicidade
Sistemas de Secreção Tipo IV/fisiologia
Vacúolos/microbiologia
[Mh] Termos MeSH secundário: Transporte Biológico/fisiologia
Coxiella burnetii/genética
Coxiella burnetii/metabolismo
Expressão Gênica/genética
Legionella pneumophila/genética
Legionella pneumophila/metabolismo
Metabolismo dos Lipídeos/fisiologia
Ubiquitina-Proteína Ligases/metabolismo
Ubiquitinação
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Type IV Secretion Systems); EC 2.3.2.27 (Ubiquitin-Protein Ligases)
[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:170718
[St] Status:MEDLINE
[do] DOI:10.1038/nrmicro.2017.67



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