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  1 / 1625 MEDLINE  
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[PMID]:29196415
[Au] Autor:Peters BA; Wu J; Pei Z; Yang L; Purdue MP; Freedman ND; Jacobs EJ; Gapstur SM; Hayes RB; Ahn J
[Ad] Endereço:Division of Epidemiology, Department of Population Health, NYU School of Medicine, New York, New York.
[Ti] Título:Oral Microbiome Composition Reflects Prospective Risk for Esophageal Cancers.
[So] Source:Cancer Res;77(23):6777-6787, 2017 Dec 01.
[Is] ISSN:1538-7445
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bacteria may play a role in esophageal adenocarcinoma (EAC) and esophageal squamous cell carcinoma (ESCC), although evidence is limited to cross-sectional studies. In this study, we examined the relationship of oral microbiota with EAC and ESCC risk in a prospective study nested in two cohorts. Oral bacteria were assessed using 16S rRNA gene sequencing in prediagnostic mouthwash samples from = 81/160 EAC and = 25/50 ESCC cases/matched controls. Findings were largely consistent across both cohorts. Metagenome content was predicted using PiCRUST. We examined associations between centered log-ratio transformed taxon or functional pathway abundances and risk using conditional logistic regression adjusting for BMI, smoking, and alcohol. We found the periodontal pathogen to be associated with higher risk of EAC. Furthermore, we found that depletion of the commensal genus and the species was associated with lower EAC risk. Bacterial biosynthesis of carotenoids was also associated with protection against EAC. Finally, the abundance of the periodontal pathogen trended with higher risk of ESCC. Overall, our findings have potential implications for the early detection and prevention of EAC and ESCC. .
[Mh] Termos MeSH primário: Adenocarcinoma/microbiologia
Carcinoma de Células Escamosas/microbiologia
Neoplasias Esofágicas/microbiologia
Microbiota/genética
Boca/microbiologia
Neisseria/isolamento & purificação
Porphyromonas gingivalis/isolamento & purificação
Streptococcus pneumoniae/isolamento & purificação
Tannerella forsythia/isolamento & purificação
[Mh] Termos MeSH secundário: Adenocarcinoma/epidemiologia
Idoso
Carcinoma de Células Escamosas/epidemiologia
Estudos de Casos e Controles
Neoplasias Esofágicas/epidemiologia
Feminino
Seres Humanos
Masculino
Meia-Idade
Neisseria/classificação
Neisseria/genética
Porphyromonas gingivalis/classificação
Porphyromonas gingivalis/genética
Estudos Prospectivos
RNA Ribossômico 16S/genética
Streptococcus pneumoniae/classificação
Streptococcus pneumoniae/genética
Inquéritos e Questionários
Tannerella forsythia/classificação
Tannerella forsythia/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Ribosomal, 16S)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180105
[Lr] Data última revisão:
180105
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171203
[St] Status:MEDLINE
[do] DOI:10.1158/0008-5472.CAN-17-1296


  2 / 1625 MEDLINE  
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[PMID]:29220372
[Au] Autor:Huang MF; Lin SJ; Ko TP; Liao YT; Hsu KC; Wang HC
[Ad] Endereço:Graduate Institute of Translational Medicine, College of Medical Science and Technology, Taipei Medical University, Taipei, Taiwan.
[Ti] Título:The monomeric form of Neisseria DNA mimic protein DMP19 prevents DNA from binding to the histone-like HU protein.
[So] Source:PLoS One;12(12):e0189461, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:DNA mimicry is a direct and effective strategy by which the mimic competes with DNA for the DNA binding sites on other proteins. Until now, only about a dozen proteins have been shown to function via this strategy, including the DNA mimic protein DMP19 from Neisseria meningitides. We have shown previously that DMP19 dimer prevents the operator DNA from binding to the transcription factor NHTF. Here, we provide new evidence that DMP19 monomer can also interact with the Neisseria nucleoid-associated protein HU. Using BS3 crosslinking, gel filtration and isothermal titration calorimetry assays, we found that DMP19 uses its monomeric form to interact with the Neisseria HU dimer. Crosslinking conjugated mass spectrometry was used to investigate the binding mode of DMP19 monomer and HU dimer. Finally, an electrophoretic mobility shift assay (EMSA) confirmed that the DNA binding affinity of HU is affected by DMP19. These results showed that DMP19 is bifunctional in the gene regulation of Neisseria through its variable oligomeric forms.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Histonas/metabolismo
Mimetismo Molecular
Neisseria/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Dimerização
Ligação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Histones)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180104
[Lr] Data última revisão:
180104
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171209
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189461


  3 / 1625 MEDLINE  
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[PMID]:28760931
[Au] Autor:Shen P; Whelan FJ; Schenck LP; McGrath JJC; Vanderstocken G; Bowdish DME; Surette MG; Stämpfli MR
[Ad] Endereço:Medical Sciences Graduate Program, McMaster University, Hamilton, Ontario, Canada.
[Ti] Título:Streptococcus pneumoniae Colonization Is Required To Alter the Nasal Microbiota in Cigarette Smoke-Exposed Mice.
[So] Source:Infect Immun;85(10), 2017 Oct.
[Is] ISSN:1098-5522
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Smokers have nasal microbiota dysbiosis, with an increased frequency of colonizing bacterial pathogens. It is possible that cigarette smoke increases pathogen acquisition by perturbing the microbiota and decreasing colonization resistance. However, it is difficult to disentangle microbiota dysbiosis due to cigarette smoke exposure from microbiota changes caused by increased pathogen acquisition in human smokers. Using an experimental mouse model, we investigated the impact of cigarette smoke on the nasal microbiota in the absence and presence of nasal pneumococcal colonization. We observed that cigarette smoke exposure alone did not alter the nasal microbiota composition. The microbiota composition was also unchanged at 12 h following low-dose nasal pneumococcal inoculation, suggesting that the ability of the microbiota to resist initial nasal pneumococcal acquisition was not impaired in smoke-exposed mice. However, nasal microbiota dysbiosis occurred as a consequence of established high-dose nasal pneumococcal colonization at day 3 in smoke-exposed mice. Similar to clinical reports on human smokers, an enrichment of potentially pathogenic bacterial genera such as , , and was observed. Our findings suggest that cigarette smoke exposure predisposes to pneumococcal colonization independent of changes to the nasal microbiota and that microbiota dysbiosis observed in smokers may occur as a consequence of established pathogen colonization.
[Mh] Termos MeSH primário: Microbiota/efeitos dos fármacos
Nariz/microbiologia
Fumaça/efeitos adversos
Streptococcus pneumoniae/fisiologia
[Mh] Termos MeSH secundário: Animais
Modelos Animais de Doenças
Disbiose
Fusobacterium/isolamento & purificação
Gemella/isolamento & purificação
Seres Humanos
Pulmão/microbiologia
Camundongos
Neisseria/isolamento & purificação
Infecções Pneumocócicas/microbiologia
Pneumonia/microbiologia
Produtos do Tabaco/efeitos adversos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Smoke)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170802
[St] Status:MEDLINE


  4 / 1625 MEDLINE  
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[PMID]:28662181
[Au] Autor:Humbert MV; Awanye AM; Lian LY; Derrick JP; Christodoulides M
[Ad] Endereço:Neisseria Research, Molecular Microbiology, Academic Unit of Clinical and Experimental Sciences, Sir Henry Wellcome Laboratories, University of Southampton Faculty of Medicine, Southampton, United Kingdom.
[Ti] Título:Structure of the Neisseria Adhesin Complex Protein (ACP) and its role as a novel lysozyme inhibitor.
[So] Source:PLoS Pathog;13(6):e1006448, 2017 Jun.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Pathogenic and commensal Neisseria species produce an Adhesin Complex Protein, which was first characterised in Neisseria meningitidis (Nm) as a novel surface-exposed adhesin with vaccine potential. In the current study, the crystal structure of a recombinant (r)Nm-ACP Type I protein was determined to 1.4 Å resolution: the fold resembles an eight-stranded ß-barrel, stabilized by a disulphide bond between the first (Cys38) and last (Cys121) ß-strands. There are few main-chain hydrogen bonds linking ß4-ß5 and ß8-ß1, so the structure divides into two four-stranded anti-parallel ß-sheets (ß1-ß4 and ß5-ß8). The computed surface electrostatic charge distribution showed that the ß1-ß4 sheet face is predominantly basic, whereas the ß5-ß8 sheet is apolar, apart from the loop between ß4 and ß5. Concentrations of rNm-ACP and rNeisseria gonorrhoeae-ACP proteins ≥0.25 µg/ml significantly inhibited by ~80-100% (P<0.05) the in vitro activity of human lysozyme (HL) over 24 h. Specificity was demonstrated by the ability of murine anti-Neisseria ACP sera to block ACP inhibition and restore HL activity. ACP expression conferred tolerance to HL activity, as demonstrated by significant 3-9 fold reductions (P<0.05) in the growth of meningococcal and gonococcal acp gene knock-out mutants in the presence of lysozyme. In addition, wild-type Neisseria lactamica treated with purified ACP-specific rabbit IgG antibodies showed similar fold reductions in bacterial growth, compared with untreated bacteria (P<0.05). Nm-ACPI is structurally similar to the MliC/PliC protein family of lysozyme inhibitors. However, Neisseria ACP proteins show <20% primary sequence similarity with these inhibitors and do not share any conserved MliC/PliC sequence motifs associated with lysozyme recognition. These observations suggest that Neisseria ACP adopts a different mode of lysozyme inhibition and that the ability of ACP to inhibit lysozyme activity could be important for host colonization by both pathogenic and commensal Neisseria organisms. Thus, ACP represents a dual target for developing Neisseria vaccines and drugs to inhibit host-pathogen interactions.
[Mh] Termos MeSH primário: Adesinas Bacterianas/química
Proteínas de Bactérias/química
Interações Hospedeiro-Patógeno/imunologia
Vacinas Meningocócicas/metabolismo
Neisseria meningitidis/metabolismo
Neisseria/química
[Mh] Termos MeSH secundário: Adesinas Bacterianas/metabolismo
Animais
Proteínas de Bactérias/metabolismo
Seres Humanos
Muramidase/antagonistas & inibidores
Neisseria/metabolismo
Coelhos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adhesins, Bacterial); 0 (Bacterial Proteins); 0 (Meningococcal Vaccines); EC 3.2.1.17 (Muramidase)
[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:170630
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006448


  5 / 1625 MEDLINE  
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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


  6 / 1625 MEDLINE  
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[PMID]:28577993
[Au] Autor:Seo DH; Jung JH; Park CS
[Ad] Endereço:Research Group of Gut Microbiome, Korea Food Research Institute, Seongnam 13539, South Korea; Graduate School of Biotechnology and Institute of Life Science and Resources, Kyung Hee University, Yongin 17104, South Korea.
[Ti] Título:Fluorescence detection of the transglycosylation activity of amylosucrase.
[So] Source:Anal Biochem;532:19-25, 2017 Sep 01.
[Is] ISSN:1096-0309
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The purpose of this study was to investigate the novel fluorescence-based assay for the transglycosylation activity of amylosucrase (ASase). The transglycosylation activity of ASase from Deinococcus geothermalis (DGAS), ASase from Neisseria polysaccharea (NPAS), and DGAS-B (chimeric ASase wherein the B domain from DGAS was exchanged with the B domain of NPAS in a DGAS background) was applied to modify 4-methlylumberlliferone (MU) to 4-methylumberlliferone glucoside (MUG) using MU as an acceptor and sucrose as a glucoside donor. The result of HPLC (high performance liquid chromatography) show that the bioconversion of MUG with ASases was successfully accomplished using sucrose and MU. Kinetic studies of ASases were performed to determine kinetic parameter for sucrose and MU. The order of overall performance (k /K ) of transglycosylation activity for MU among DGAS, DGAS-B and NPAS was as follows: DGAS-B (8.1) > DGAS (5.0) > NPAS (0.4). The fluorescence-based transglycosylation assay using MU has a potential to be used as the detection of transglycosylation activity of ASase and to screen novel ASase variants, which may be improved in their transglycosylation activities.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Deinococcus/enzimologia
Glucosiltransferases/metabolismo
Neisseria/enzimologia
Sacarose/metabolismo
[Mh] Termos MeSH secundário: Cromatografia Líquida de Alta Pressão
Fluorescência
Glicosilação
Cinética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 57-50-1 (Sucrose); EC 2.4.1.- (Glucosyltransferases); EC 2.4.1.4 (amylosucrase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170912
[Lr] Data última revisão:
170912
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170605
[St] Status:MEDLINE


  7 / 1625 MEDLINE  
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[PMID]:28424521
[Au] Autor:Hirschi M; Johnson ZL; Lee SY
[Ad] Endereço:Department of Biochemistry, Duke University Medical Center, 303 Research Drive, Durham, North Carolina 27710, USA.
[Ti] Título:Visualizing multistep elevator-like transitions of a nucleoside transporter.
[So] Source:Nature;545(7652):66-70, 2017 05 04.
[Is] ISSN:1476-4687
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Membrane transporters move substrates across the membrane by alternating access of their binding sites between the opposite sides of the membrane. An emerging model of this process is the elevator mechanism, in which a substrate-binding transport domain moves a large distance across the membrane. This mechanism has been characterized by a transition between two states, but the conformational path that leads to the transition is not yet known, largely because the available structural information has been limited to the two end states. Here we present crystal structures of the inward-facing, intermediate, and outward-facing states of a concentrative nucleoside transporter from Neisseria wadsworthii. Notably, we determined the structures of multiple intermediate conformations, in which the transport domain is captured halfway through its elevator motion. Our structures present a trajectory of the conformational transition in the elevator model, revealing multiple intermediate steps and state-dependent conformational changes within the transport domain that are associated with the elevator-like motion.
[Mh] Termos MeSH primário: Modelos Biológicos
Movimento
Neisseria/química
Proteínas de Transporte de Nucleosídeos/química
Proteínas de Transporte de Nucleosídeos/metabolismo
[Mh] Termos MeSH secundário: Sítios de Ligação
Cristalização
Cristalografia por Raios X
Cisteína/química
Cisteína/metabolismo
Elevadores e Escadas Rolantes
Ligantes
Modelos Moleculares
Mutação
Domínios Proteicos
Uridina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Ligands); 0 (Nucleoside Transport Proteins); K848JZ4886 (Cysteine); WHI7HQ7H85 (Uridine)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170421
[St] Status:MEDLINE
[do] DOI:10.1038/nature22057


  8 / 1625 MEDLINE  
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[PMID]:28369241
[Au] Autor:Weyand NJ
[Ti] Título:Neisseria models of infection and persistence in the upper respiratory tract.
[So] Source:Pathog Dis;75(3), 2017 Apr 01.
[Is] ISSN:2049-632X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Gram-negative bacteria genus Neisseria includes both pathogenic and commensal species that are found primarily in the upper respiratory tract of humans and animals. The development of animal models to study neisserial pathogenesis has focused almost exclusively on two species that cause disease in humans. These include Neisseria meningitidis, an obligate commensal that can cause invasive disease, and N. gonorrhoeae, the causative agent of gonorrhea. Both pathogens can persist in the upper respiratory tract. This article will give a brief overview of the genus Neisseria. The anatomy of the upper respiratory tract and its use as a niche for bacteria will be discussed. Next, studies that provide insight about the first stage of upper respiratory tract infection, namely colonization, will be reviewed. Most studies of upper respiratory tract infection have focused on N. meningitidis infections of laboratory mice. This review will also discuss models of respiratory tract persistence by Neisseria species, including commensals, in mice, non-human primates and human volunteers. The article includes a section that discusses the future utility of upper respiratory tract models in informing the development of effective antimicrobial therapies. Such knowledge is needed to minimize the dissemination of antimicrobial resistance from respiratory reservoirs.
[Mh] Termos MeSH primário: Neisseria/fisiologia
Sistema Respiratório/microbiologia
Infecções Respiratórias/microbiologia
[Mh] Termos MeSH secundário: Animais
Animais Geneticamente Modificados
Antibacterianos/farmacologia
Antibacterianos/uso terapêutico
Modelos Animais de Doenças
Farmacorresistência Bacteriana
Interações Hospedeiro-Patógeno/genética
Interações Hospedeiro-Patógeno/imunologia
Seres Humanos
Imunidade
Neisseria/efeitos dos fármacos
Sistema Respiratório/anatomia & histologia
Sistema Respiratório/imunologia
Sistema Respiratório/patologia
Infecções Respiratórias/diagnóstico
Infecções Respiratórias/tratamento farmacológico
Infecções Respiratórias/imunologia
Fatores de Risco
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Anti-Bacterial Agents)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170504
[Lr] Data última revisão:
170504
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170404
[St] Status:MEDLINE
[do] DOI:10.1093/femspd/ftx031


  9 / 1625 MEDLINE  
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[PMID]:28158534
[Au] Autor:Hooda Y; Shin HE; Bateman TJ; Moraes TF
[Ti] Título:Neisserial surface lipoproteins: structure, function and biogenesis.
[So] Source:Pathog Dis;75(2), 2017 Mar 01.
[Is] ISSN:2049-632X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The surface of many Gram-negative bacteria contains lipidated protein molecules referred to as surface lipoproteins or SLPs. SLPs play critical roles in host immune evasion, nutrient acquisition and regulation of the bacterial stress response. The focus of this review is on the SLPs present in Neisseria, a genus of bacteria that colonise the mucosal surfaces of animals. Neisseria contains two pathogens of medical interest, namely Neisseria meningitidis and N. gonorrhoeae. Several SLPs have been identified in Neisseria and their study has elucidated key strategies used by these pathogens to survive inside the human body. Herein, we focus on the identification, structure and function of SLPs that have been identified in Neisseria. We also survey the translocation pathways used by these SLPs to reach the cell surface. Specifically, we elaborate on the strategies used by neisserial SLPs to translocate across the outer membrane with an emphasis on Slam, a novel outer membrane protein that has been implicated in SLP biogenesis. Taken together, the study of SLPs in Neisseria illustrates the widespread roles played by this family of proteins in Gram-negative bacteria.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Proteínas de Bactérias/metabolismo
Lipoproteínas/química
Lipoproteínas/metabolismo
Neisseria/metabolismo
[Mh] Termos MeSH secundário: Animais
Proteínas de Bactérias/classificação
Proteínas de Bactérias/genética
Membrana Celular/metabolismo
Seres Humanos
Lipoproteínas/classificação
Lipoproteínas/genética
Neisseria/genética
Transporte Proteico
Transdução de Sinais
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Lipoproteins)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170504
[Lr] Data última revisão:
170504
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170204
[St] Status:MEDLINE
[do] DOI:10.1093/femspd/ftx010


  10 / 1625 MEDLINE  
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[PMID]:28090057
[Au] Autor:Uwamino Y; Sugita K; Iwasaki E; Fujiwara H; Nishimura T; Hasegawa N; Iwata S
[Ad] Endereço:Center for Infectious Diseases and Infection Control, Keio University School of Medicine, Japan.
[Ti] Título:The First Case Report of Acute Cholangitis and Bacteremia Due to Neisseria subflava.
[So] Source:Intern Med;56(2):221-223, 2017.
[Is] ISSN:1349-7235
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:We herein report a case of acute cholangitis and bacteremia caused by a commensal Neisseria species, Neisseria subflava, in an 82-year-old man with cholangiocarcinoma. Emergency endoscopic nasobiliary drainage and cefoperazone/sulbactam therapy were effective. Gram negative coccobacilli were isolated from both blood and bile cultures on 5% sheep blood agar. The isolate was identified as N.subflava biovar perflava by mass spectrometry, a sequence analysis of the 16S rRNA, and biochemical testing. Although biliary infections due to commensal Neisseria are extremely rare, this case demonstrates the possibility of its occurrence in patients undergoing bile duct treatment.
[Mh] Termos MeSH primário: Bacteriemia/diagnóstico
Colangiocarcinoma
Colangite/diagnóstico
Neisseria/isolamento & purificação
[Mh] Termos MeSH secundário: Doença Aguda
Idoso de 80 Anos ou mais
Antibacterianos/administração & dosagem
Antibacterianos/uso terapêutico
Bacteriemia/complicações
Bacteriemia/diagnóstico por imagem
Bacteriemia/terapia
Cefoperazona/administração & dosagem
Cefoperazona/uso terapêutico
Colangite/complicações
Colangite/diagnóstico por imagem
Colangite/terapia
Diagnóstico Diferencial
Drenagem
Quimioterapia Combinada
Seres Humanos
Masculino
Pancreaticoduodenectomia
Sulbactam/administração & dosagem
Sulbactam/uso terapêutico
Tomografia Computadorizada por Raios X
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 7U75I1278D (Cefoperazone); S4TF6I2330 (Sulbactam)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170117
[St] Status:MEDLINE
[do] DOI:10.2169/internalmedicine.56.7482



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