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[PMID]:29458526
[Au] Autor:Ma J; Wei Y; Zhang L; Wang X; Yao D; Liu D; Liu W; Yu S; Yu Y; Wu Z; Yu L; Zhu Z; Cui Y
[Ad] Endereço:College of Life Science and Technology, Heilongjiang Bayi Agricultural University, Daqing 163319, PR China.
[Ti] Título:Identification of a novel linear B-cell epitope as a vaccine candidate in the N2N3 subdomain of Staphylococcus aureus fibronectin-binding protein A.
[So] Source:J Med Microbiol;67(3):423-431, 2018 Mar.
[Is] ISSN:1473-5644
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:PURPOSE: To explore an epitope-based vaccine against Staphylococcus aureus, we screened the epitopes in the N2N3 subdomain of fibronectin-binding protein A (FnBPA) as a surface component of S. aureus. METHODOLOGY: We expressed N2N3 proteins and prepared monoclonal antibodies (mAbs) against N2N3 by the hybridoma technique, before screening the B-cell epitopes in N2N3 using a phage-displayed random 12-mer peptide library with these mAbs against N2N3. Finally, we analysed the characters of the screened epitopes using immunofluorescence and an S. aureus infection assay. RESULTS: In this paper, we identified a linear B-cell epitope in N2N3 through screening a phage-displayed peptide library with a 3C3 mAb against the N2N3. The 3C3 mAb recognized the 159IETFNKANNRFSH171 sequence of the N2N3 subdomain. Subsequently, site-directed mutagenic analysis demonstrated that residues F162, K164, N167, R168 and F169 formed the core of 159IETFNKANNRFSH171, and this core motif was the minimal determinant of the B-cell epitope recognized by the 3C3 mAb. The epitope 159IETFNKANNRFSH171 showed high homology among different S. aureus strains. Moreover, this epitope was exposed on the surface of the S. aureus by using an enzyme-linked immunosorbent assay (ELISA) assay and an indirect immunofluorescence assay. As expected, the epitope peptide evoked a protective immune response against S. aureus infection in immunized mice. CONCLUSION: We identified a novel linear B-cell epitope, 159IETFNKANNRFSH171, in the N2N3 subdomain of S. aureus fibronectin-binding protein A that is recognized by 3C3 mAb, which will contribute to the further study of an epitope-based vaccine candidate against S. aureus.
[Mh] Termos MeSH primário: Adesinas Bacterianas/imunologia
Epitopos de Linfócito B/imunologia
Infecções Estafilocócicas/prevenção & controle
Vacinas Antiestafilocócicas/imunologia
Staphylococcus aureus/imunologia
[Mh] Termos MeSH secundário: Adesinas Bacterianas/química
Adesinas Bacterianas/genética
Animais
Anticorpos Monoclonais/imunologia
Anticorpos Monoclonais/isolamento & purificação
Ensaio de Imunoadsorção Enzimática
Mapeamento de Epitopos
Epitopos de Linfócito B/química
Epitopos de Linfócito B/genética
Imunização
Camundongos
Biblioteca de Peptídeos
Ligação Proteica
Infecções Estafilocócicas/imunologia
Staphylococcus aureus/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adhesins, Bacterial); 0 (Antibodies, Monoclonal); 0 (Epitopes, B-Lymphocyte); 0 (Peptide Library); 0 (Staphylococcal Vaccines); 0 (fibronectin-binding proteins, bacterial)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180221
[St] Status:MEDLINE
[do] DOI:10.1099/jmm.0.000633


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[PMID]:28448633
[Au] Autor:Scoffield JA; Duan D; Zhu F; Wu H
[Ad] Endereço:Department of Pediatric Dentistry, School of Dentistry, University of Alabama at Birmingham, Birmingham, Alabama, United States of America.
[Ti] Título:A commensal streptococcus hijacks a Pseudomonas aeruginosa exopolysaccharide to promote biofilm formation.
[So] Source:PLoS Pathog;13(4):e1006300, 2017 Apr.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Pseudomonas aeruginosa causes devastating chronic pulmonary infections in cystic fibrosis (CF) patients. Although the CF airway is inhabited by diverse species of microorganisms interlaced within a biofilm, many studies focus on the sole contribution of P. aeruginosa pathogenesis in CF morbidity. More recently, oral commensal streptococci have been identified as cohabitants of the CF lung, but few studies have explored the role these bacteria play within the CF biofilm. We examined the interaction between P. aeruginosa and oral commensal streptococci within a dual species biofilm. Here we report that the CF P. aeruginosa isolate, FRD1, enhances biofilm formation and colonization of Drosophila melanogaster by the oral commensal Streptococcus parasanguinis. Moreover, production of the P. aeruginosa exopolysaccharide, alginate, is required for the promotion of S. parasanguinis biofilm formation and colonization. However, P. aeruginosa is not promoted in the dual species biofilm. Furthermore, we show that the streptococcal adhesin, BapA1, mediates alginate-dependent enhancement of the S. parasanguinis biofilm in vitro, and BapA1 along with another adhesin, Fap1, are required for the in vivo colonization of S. parasanguinis in the presence of FRD1. Taken together, our study highlights a new association between streptococcal adhesins and P. aeruginosa alginate, and reveals a mechanism by which S. parasanguinis potentially colonizes the CF lung and interferes with the pathogenesis of P. aeruginosa.
[Mh] Termos MeSH primário: Biofilmes
Fibrose Cística/microbiologia
Polissacarídeos Bacterianos/metabolismo
Infecções por Pseudomonas/microbiologia
Pseudomonas aeruginosa/fisiologia
[Mh] Termos MeSH secundário: Adesinas Bacterianas/genética
Adesinas Bacterianas/metabolismo
Animais
Drosophila melanogaster
Seres Humanos
Pseudomonas aeruginosa/genética
Pseudomonas aeruginosa/crescimento & desenvolvimento
Pseudomonas aeruginosa/isolamento & purificação
Sistema Respiratório/microbiologia
Simbiose
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adhesins, Bacterial); 0 (Polysaccharides, Bacterial); 128531-82-8 (exopolysaccharide, Pseudomonas)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:180306
[Lr] Data última revisão:
180306
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170428
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006300


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[PMID]:29329335
[Au] Autor:Kyrklund M; Kummu O; Kankaanpää J; Akhi R; Nissinen A; Turunen SP; Pussinen P; Wang C; Hörkkö S
[Ad] Endereço:Medical Microbiology and Immunology, Research Unit of Biomedicine, Faculty of Medicine, University of Oulu, Oulu, Finland.
[Ti] Título:Immunization with gingipain A hemagglutinin domain of Porphyromonas gingivalis induces IgM antibodies binding to malondialdehyde-acetaldehyde modified low-density lipoprotein.
[So] Source:PLoS One;13(1):e0191216, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Treatment of periodontitis has beneficial effects on systemic inflammation markers that relate to progression of atherosclerosis. We aimed to investigate whether immunization with A hemagglutinin domain (Rgp44) of Porphyromonas gingivalis (Pg), a major etiologic agent of periodontitis, would lead to an antibody response cross-reacting with oxidized low-density lipoprotein (OxLDL) and how it would affect the progression of atherosclerosis in low-density lipoprotein receptor-deficient (LDLR-/-) mice. The data revealed a prominent IgM but not IgG response to malondialdehyde-acetaldehyde modified LDL (MAA-LDL) after Rgp44 and Pg immunizations, implying that Rgp44/Pg and MAA adducts may share cross-reactive epitopes that prompt IgM antibody production and consequently confer atheroprotection. A significant negative association was observed between atherosclerotic lesion and plasma IgA to Rgp44 in Rgp44 immunized mice, supporting further the anti-atherogenic effect of Rgp44 immunization. Plasma IgA levels to Rgp44 and to Pg in both Rgp44- and Pg-immunized mice were significantly higher than those in saline control, suggesting that IgA to Rgp44 could be a surrogate marker of immunization in Pg-immunized mice. Distinct antibody responses in plasma IgA levels to MAA-LDL, to Pg lipopolysaccharides (Pg-LPS), and to phosphocholine (PCho) were observed after Rgp44 and Pg immunizations, indicating that different immunogenic components between Rpg44 and Pg may behave differently in regard of their roles in the development of atherosclerosis. Immunization with Rgp44 also displayed atheroprotective features in modulation of plaque size through association with plasma levels of IL-1α whereas whole Pg bacteria achieved through regulation of anti-inflammatory cytokine levels of IL-5 and IL-10. The present study may contribute to refining therapeutic approaches aiming to modulate immune responses and inflammatory/anti-inflammatory processes in atherosclerosis.
[Mh] Termos MeSH primário: Adesinas Bacterianas/imunologia
Anticorpos Antibacterianos/biossíntese
Proteínas de Bactérias/imunologia
Cisteína Endopeptidases/imunologia
Imunoglobulina M/biossíntese
Lipoproteínas LDL/imunologia
Porphyromonas gingivalis/imunologia
[Mh] Termos MeSH secundário: Acetaldeído/análogos & derivados
Adesinas Bacterianas/química
Animais
Anticorpos Antibacterianos/metabolismo
Aterosclerose/etiologia
Aterosclerose/imunologia
Aterosclerose/prevenção & controle
Proteínas de Bactérias/química
Infecções por Bacteroidaceae/complicações
Infecções por Bacteroidaceae/imunologia
Infecções por Bacteroidaceae/microbiologia
Reações Cruzadas
Cisteína Endopeptidases/química
Modelos Animais de Doenças
Feminino
Seres Humanos
Imunização
Imunoglobulina M/metabolismo
Lectinas/química
Lectinas/imunologia
Lipoproteínas LDL/química
Malondialdeído/análogos & derivados
Malondialdeído/imunologia
Camundongos
Camundongos Knockout
Periodontite/complicações
Periodontite/imunologia
Periodontite/microbiologia
Domínios Proteicos
Receptores de LDL/deficiência
Receptores de LDL/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adhesins, Bacterial); 0 (Antibodies, Bacterial); 0 (Bacterial Proteins); 0 (Immunoglobulin M); 0 (Lectins); 0 (Lipoproteins, LDL); 0 (Receptors, LDL); 0 (hemagglutinin A, Porphyromonas gingivalis); 0 (malondialdehyde-low density lipoprotein, mouse); 4Y8F71G49Q (Malondialdehyde); EC 3.4.22.- (Cysteine Endopeptidases); EC 3.4.22.37 (argingipain, Porphyromonas gingivalis); GO1N1ZPR3B (Acetaldehyde)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180113
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191216


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[PMID]:29080423
[Au] Autor:Cha W; Fratamico PM; Ruth LE; Bowman AS; Nolting JM; Manning SD; Funk JA
[Ad] Endereço:Department of Microbiology and Molecular Genetics, Michigan State University, East Lansing, MI 48824, USA.
[Ti] Título:Prevalence and characteristics of Shiga toxin-producing Escherichia coli in finishing pigs: Implications on public health.
[So] Source:Int J Food Microbiol;264:8-15, 2018 Jan 02.
[Is] ISSN:1879-3460
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Shiga toxin-producing Escherichia coli (STEC) are important food-borne pathogens, which can cause serious illnesses, including hemorrhagic colitis and hemolytic uremic syndrome. To study the epidemiology of STEC in finishing pigs and examine the potential risks they pose for human STEC infections, we conducted a longitudinal cohort study in three finishing sites. Six cohorts of pigs (2 cohorts/site, 20 pigs/cohort) were randomly selected, and fecal samples (n=898) were collected every two weeks through their finishing period. Eighty-two pigs (68.3%) shed STEC at least once, and the proportion of STEC-positive pigs varied across sites (50-97.5%) and cohorts (15-100%). Clinically important serotypes, O157:H7 (stx , eae) and O26:H11 (stx , eae), were recovered from two pigs at sites C and A, respectively. The most common serotype isolated was O59:H21 (stx ), which was particularly prevalent in site B as it was recovered from all STEC positive pigs (n=39). Each cohort showed different patterns of STEC shedding, which were associated with the prevalent serotype. The median shedding duration of STEC in pigs was 28days, consistent with our prior study. However, among pigs shedding O59:H21 at least once, pigs in cohort B2 had a significantly longer shedding duration of 42days (P<0.05) compared to other cohorts. Stx2e was the most commonly observed stx variant in finishing pigs (93.9%), in accordance with the previous studies. Stx2e has been reported to be significantly associated with edema disease in pigs, however, the pathogenicity in humans warrants further investigations. Nonetheless, our findings affirm that pigs are an important reservoir for human STEC infections, and that the circulating serotypes in a cohort and site management factors may significantly affect the prevalence of STEC. Molecular characterization of STEC isolates and epidemiological studies to identify risk factors for shedding in pigs are strongly warranted to further address the significance to public health and to develop mitigation strategies.
[Mh] Termos MeSH primário: Adesinas Bacterianas/genética
Proteínas de Escherichia coli/genética
Doenças Transmitidas por Alimentos/microbiologia
Escherichia coli Shiga Toxigênica/classificação
Escherichia coli Shiga Toxigênica/genética
Sus scrofa/microbiologia
[Mh] Termos MeSH secundário: Animais
Infecções por Escherichia coli
Fezes/microbiologia
Seres Humanos
Estudos Longitudinais
Prevalência
Saúde Pública
Sorogrupo
Escherichia coli Shiga Toxigênica/isolamento & purificação
Escherichia coli Shiga Toxigênica/patogenicidade
Suínos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adhesins, Bacterial); 0 (Escherichia coli Proteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171029
[St] Status:MEDLINE


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[PMID]:28469996
[Au] Autor:Cendra MDM; Christodoulides M; Hossain P
[Ad] Endereço:Division of Clinical and Experimental Sciences, Department of Molecular Microbiology, Faculty of Medicine, University of SouthamptonSouthampton, UK.
[Ti] Título:Signaling Mediated by Toll- Receptor 5 Sensing of Flagellin Influences IL-1ß and IL-18 Production by Primary Fibroblasts Derived from the Human Cornea.
[So] Source:Front Cell Infect Microbiol;7:130, 2017.
[Is] ISSN:2235-2988
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:is the principal cause of bacterial keratitis worldwide and overstimulation of the innate immune system by this organism is believed to contribute significantly to sight loss. In the current study, we have used primary human corneal fibroblast (hCF) cells as an model of corneal infection to examine the role of flagellum and type three secretion system (TTSS) in inducing inflammasome-associated molecules that trigger IL-1ß and IL-18 production during the early stages of the infection. Our results show that infection stimulated the non-canonical pathway for IL-1ß and IL-18 expression and pathway stimulation was influenced predominantly by the flagellum. Both IL-1ß and IL-18 cytokines were expressed intracellularly during bacterial infection, but only the former was released and detected in the extracellular environment. We also investigated the signaling pathways in hCFs mediated by Toll- Receptor (TLR)4 and TLR5 sensing of , and our data show that the signal triggered by TLR5-flagellin sensing significantly contributed to IL-1ß and IL-18 cytokine production in our model. Our study suggests that IL-18 expression is wholly dependent on extracellular flagellin sensing by TLR5, whereas IL-1ß expression is also influenced by lipopolysacharide. Additionally, we demonstrate that IL-1ß and IL-18 production by hCFs can be triggered by both MyD88-dependent and -independent pathways. Overall, our study provides a rationale for the development of targeted therapies, by proposing an inhibition of flagellin-PRR-signaling interactions, in order to ameliorate the inflammatory response characteristic of keratitis.
[Mh] Termos MeSH primário: Epitélio Anterior/efeitos dos fármacos
Fibroblastos/metabolismo
Flagelina/farmacologia
Interleucina-18/metabolismo
Interleucina-1beta/metabolismo
Pseudomonas aeruginosa/química
Transdução de Sinais/imunologia
Receptor 5 Toll-Like/metabolismo
[Mh] Termos MeSH secundário: Adesinas Bacterianas
Proteínas de Bactérias/genética
Proteínas de Bactérias/farmacologia
Células Cultivadas
Citocinas/metabolismo
Epitélio Anterior/imunologia
Flagelina/genética
Flagelina/imunologia
Flagelina/isolamento & purificação
Seres Humanos
Inflamassomos/metabolismo
Lipopolissacarídeos/imunologia
Pseudomonas aeruginosa/patogenicidade
Proteínas Recombinantes
Receptor 4 Toll-Like/metabolismo
Sistemas de Secreção Tipo III/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adhesins, Bacterial); 0 (Bacterial Proteins); 0 (Cytokines); 0 (FlgK protein, Bacteria); 0 (Inflammasomes); 0 (Interleukin-18); 0 (Interleukin-1beta); 0 (Lipopolysaccharides); 0 (Recombinant Proteins); 0 (TLR4 protein, human); 0 (TLR5 protein, human); 0 (Toll-Like Receptor 4); 0 (Toll-Like Receptor 5); 0 (Type III Secretion Systems); 12777-81-0 (Flagellin)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180216
[Lr] Data última revisão:
180216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.3389/fcimb.2017.00130


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[PMID]:29211991
[Au] Autor:Koutsioubas A
[Ad] Endereço:Jülich Centre for Neutron Science (JCNS) at Heinz Maier-Leibnitz Zentrum (MLZ), Forschungszentrum Jülich, Garching, Germany. Electronic address: a.koutsioumpas@fz-juelich.de.
[Ti] Título:Low-Resolution Structure of Detergent-Solubilized Membrane Proteins from Small-Angle Scattering Data.
[So] Source:Biophys J;113(11):2373-2382, 2017 Dec 05.
[Is] ISSN:1542-0086
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Despite the ever-increasing usage of small-angle scattering as a valuable complementary method in the field of structural biology, applications concerning membrane proteins remain elusive mainly due to experimental challenges and the relative lack of theoretical tools for the treatment of scattering data. This fact adds up to general difficulties encountered also by other established methods (crystallography, NMR) for the study of membrane proteins. Following the general paradigm of ab initio methods for low-resolution restoration of soluble protein structure from small-angle scattering data, we construct a general multiphase model with a set of physical constraints, which, together with an appropriate minimization procedure, gives direct structural information concerning the different components (protein, detergent molecules) of detergent-solubilized membrane protein complexes. Assessment of the method's precision and robustness is evaluated by performing shape restorations from simulated data of a tetrameric α-helical membrane channel (Aquaporin-0) solubilized by n-Dodecyl ß-D-Maltoside and from previously published small-angle neutron scattering experimental data of the filamentous hemagglutinin adhesin ß-barrel protein transporter solubilized by n-Octyl ß-D-glucopyranoside. It is shown that the acquisition of small-angle neutron scattering data at two different solvent contrasts, together with an estimation of detergent aggregation number around the protein, permits the reliable reconstruction of the shape of membrane proteins without the need for any prior structural information.
[Mh] Termos MeSH primário: Adesinas Bacterianas/química
Aquaporinas/química
Detergentes/química
Proteínas do Olho/química
Espalhamento a Baixo Ângulo
[Mh] Termos MeSH secundário: Simulação de Dinâmica Molecular
Conformação Proteica em alfa-Hélice
Conformação Proteica em Folha beta
Solubilidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adhesins, Bacterial); 0 (Aquaporins); 0 (Detergents); 0 (Eye Proteins); 0 (aquaporin 0)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180119
[Lr] Data última revisão:
180119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171207
[St] Status:MEDLINE


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[PMID]:29211241
[Au] Autor:Cunha CEPD; Moreira C; Rocha ADSR; Finger PF; Magalhães CG; Ferreira MRA; Dellagostin OA; Moreira ÂN; Conceição FR
[Ad] Endereço:Universidade Federal de Pelotas, Centro de Desenvolvimento Tecnológico, Biotecnologia, Pelotas, RS, Brasil.
[Ti] Título:Parenteral adjuvant potential of recombinant B subunit of Escherichia coli heat-labile enterotoxin.
[So] Source:Mem Inst Oswaldo Cruz;112(12):812-816, 2017 Dec.
[Is] ISSN:1678-8060
[Cp] País de publicação:Brazil
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The B subunit of Escherichia coli heat-labile enterotoxin (LTB) is a potent mucosal immune adjuvant. However, there is little information about LTB's potential as a parenteral adjuvant. OBJECTIVES: We aimed at evaluating and better understanding rLTB's potential as a parenteral adjuvant using the fused R1 repeat of Mycoplasma hyopneumoniae P97 adhesin as an antigen to characterise the humoral immune response induced by this construct and comparing it to that generated when aluminium hydroxide is used as adjuvant instead. METHODS: BALB/c mice were immunised intraperitoneally with either rLTBR1 or recombinant R1 adsorbed onto aluminium hydroxide. The levels of systemic anti-rR1 antibodies (total Ig, IgG1, IgG2a, and IgA) were assessed by enzyme-linked immunosorbent assay (ELISA). The ratio of IgG1 and IgG2a was used to characterise a Th1, Th2, or mixed Th1/Th2 immune response. FINDINGS: Western blot confirmed rR1, either alone or fused to LTB, remained antigenic; anti-cholera toxin ELISA confirmed that LTB retained its activity when expressed in a heterologous system. Mice immunised with the rLTBR1 fusion protein produced approximately twice as much anti-rR1 immunoglobulins as mice vaccinated with rR1 adsorbed onto aluminium hydroxide. Animals vaccinated with either rLTBR1 or rR1 adsorbed onto aluminium hydroxide presented a mixed Th1/Th2 immune response. We speculate this might be a result of rR1 immune modulation rather than adjuvant modulation. Mice immunised with rLTBR1 produced approximately 1.5-fold more serum IgA than animals immunised with rR1 and aluminium hydroxide. MAIN CONCLUSIONS: The results suggest that rLTB is a more powerful parenteral adjuvant than aluminium hydroxide when administered intraperitoneally as it induced higher antibody titres. Therefore, we recommend that rLTB be considered an alternative adjuvant, even if different administration routes are employed.
[Mh] Termos MeSH primário: Adesinas Bacterianas/imunologia
Adjuvantes Imunológicos/administração & dosagem
Toxinas Bacterianas/administração & dosagem
Enterotoxinas/administração & dosagem
Proteínas de Escherichia coli/administração & dosagem
Mycoplasma hyopneumoniae/imunologia
Pneumonia Suína Micoplasmática/prevenção & controle
[Mh] Termos MeSH secundário: Hidróxido de Alumínio
Animais
Toxinas Bacterianas/imunologia
Enterotoxinas/imunologia
Ensaio de Imunoadsorção Enzimática
Proteínas de Escherichia coli/imunologia
Feminino
Camundongos
Camundongos Endogâmicos BALB C
Pneumonia Suína Micoplasmática/imunologia
Suínos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adhesins, Bacterial); 0 (Adjuvants, Immunologic); 0 (Bacterial Toxins); 0 (Enterotoxins); 0 (Escherichia coli Proteins); 0 (P97 protein, Mycoplasma); 0 (heat-labile enterotoxin, E coli); 5QB0T2IUN0 (Aluminum Hydroxide)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171227
[Lr] Data última revisão:
171227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171207
[St] Status:MEDLINE


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Campos, Leila Carvalho
Texto completo
[PMID]:28931058
[Au] Autor:Moura ARSS; Kretz CB; Ferreira IE; Nunes AMPB; de Moraes JC; Reis MG; McBride AJA; Wang X; Campos LC
[Ad] Endereço:Laboratório de Patologia e Biologia Molecular, Instituto Gonçalo Moniz, FIOCRUZ-BA, Salvador, Bahia, Brazil.
[Ti] Título:Molecular characterization of Neisseria meningitidis isolates recovered from 11-19-year-old meningococcal carriers in Salvador, Brazil.
[So] Source:PLoS One;12(9):e0185038, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Characterization of meningococci isolated from the pharynx is essential towards understanding the dynamics of meningococcal carriage and disease. Meningococcal isolates, collected from adolescents resident in Salvador, Brazil during 2014, were characterized by multilocus sequence typing, genotyping or whole-genome sequencing. Most were nongroupable (61.0%), followed by genogroups B (11.9%) and Y (8.5%). We identified 34 different sequence types (STs), eight were new STs, distributed among 14 clonal complexes (cc), cc1136 represented 20.3% of the nongroupable isolates. The porA and fetA genotypes included P1.18,25-37 (11.9%), P1.18-1,3 (10.2%); F5-5 (23.7%), F4-66 (16.9%) and F1-7 (13.6%). The porB class 3 protein and the fHbp subfamily A (variants 2 and 3) genotypes were found in 93.0 and 71.0% of the isolates, respectively. NHBA was present in all isolates, and while most lacked NadA (94.9%), we detected the hyperinvasive lineages B:P1.19,15:F5-1:ST-639 (cc32); C:P1.22,14-6:F3-9:ST-3780 (cc103) and W:P1.5,2:F1-1:ST-11 (cc11). This is the first report on the genetic diversity and vaccine antigen prevalence among N. meningitidis carriage isolates in the Northeast of Brazil. This study highlights the need for ongoing characterization of meningococcal isolates following the introduction of vaccines and for determining public health intervention strategies.
[Mh] Termos MeSH primário: Neisseria meningitidis/genética
Neisseria meningitidis/isolamento & purificação
Filogenia
[Mh] Termos MeSH secundário: Adesinas Bacterianas/genética
Adolescente
Antígenos de Bactérias/genética
Proteínas da Membrana Bacteriana Externa/genética
Proteínas de Bactérias/genética
Brasil
Proteínas de Transporte/genética
Portador Sadio
Criança
Variação Genética
Genótipo
Seres Humanos
Tipagem de Sequências Multilocus
Porinas/genética
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adhesins, Bacterial); 0 (Antigens, Bacterial); 0 (Bacterial Outer Membrane Proteins); 0 (Bacterial Proteins); 0 (Carrier Proteins); 0 (FrpB protein, bacteria); 0 (NHBA protein, Neisseria meningitidis); 0 (NadA protein, Neisseria meningitidis); 0 (Porins); 0 (factor H-binding protein, Neisseria meningitidis); 0 (porin protein, Neisseria)
[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:170921
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185038


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[PMID]:28874408
[Au] Autor:Kern BK; Porsch EA; St Geme JW
[Ad] Endereço:Cell and Molecular Biology Graduate Group, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, USA.
[Ti] Título:Defining the Mechanical Determinants of Kingella kingae Adherence to Host Cells.
[So] Source:J Bacteriol;199(23), 2017 Dec 01.
[Is] ISSN:1098-5530
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:is an important pathogen in young children and initiates infection by colonizing the posterior pharynx. Adherence to pharyngeal epithelial cells is an important first step in the process of colonization. In the present study, we sought to elucidate the interplay of type IV pili (T4P), a trimeric autotransporter adhesin called Knh, and the polysaccharide capsule in adherence to host cells. Using adherence assays performed under shear stress, we observed that a strain expressing only Knh was capable of higher levels of adherence than a strain expressing only T4P. Using atomic force microscopy and transmission electron microscopy (TEM), we established that the capsule had a mean depth of 700 nm and that Knh was approximately 110 nm long. Using cationic ferritin capsule staining and thin-section transmission electron microscopy, we found that when bacteria expressing retractile T4P were in close contact with host cells, the capsule was absent at the point of contact between the bacterium and the host cell membrane. In a T4P retraction-deficient mutant, the capsule depth remained intact and adherence levels were markedly reduced. These results support the following model: T4P make initial contact with the host cell and mediate low-strength adherence. T4P retract, pulling the organism closer to the host cell and displacing the capsule, allowing Knh to be exposed and mediate high-strength, tight adherence to the host cell surface. This report provides the first description of the mechanical displacement of capsule enabling intimate bacterial adherence to host cells. Adherence to host cells is an important first step in bacterial colonization and pathogenicity. has three surface factors that are involved in adherence: type IV pili (T4P), a trimeric autotransporter adhesin called Knh, and a polysaccharide capsule. Our results suggest that T4P mediate initial contact and low-strength adherence to host cells. T4P retraction draws the bacterium closer to the host cell and causes the displacement of capsule. This displacement exposes Knh and allows Knh to mediate high-strength adherence to the host cell. This work provides new insight into the interplay of T4P, a nonpilus adhesin, and a capsule and their effects on bacterial adherence to host cells.
[Mh] Termos MeSH primário: Aderência Bacteriana/fisiologia
Proteínas de Bactérias/metabolismo
Interações Hospedeiro-Patógeno/fisiologia
Kingella kingae/metabolismo
[Mh] Termos MeSH secundário: Células A549
Adesinas Bacterianas/metabolismo
Linhagem Celular Tumoral
Células Epiteliais/microbiologia
Seres Humanos
Microscopia Eletrônica de Transmissão/métodos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adhesins, Bacterial); 0 (Bacterial Proteins)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171119
[Lr] Data última revisão:
171119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170907
[St] Status:MEDLINE


  10 / 5741 MEDLINE  
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[PMID]:28864445
[Au] Autor:Cuthbert BJ; Ross W; Rohlfing AE; Dove SL; Gourse RL; Brennan RG; Schumacher MA
[Ad] Endereço:Department of Biochemistry, Duke University School of Medicine, Durham, North Carolina 27710, USA.
[Ti] Título:Dissection of the molecular circuitry controlling virulence in .
[So] Source:Genes Dev;31(15):1549-1560, 2017 Aug 01.
[Is] ISSN:1549-5477
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:the etiological agent of tularemia, is one of the most infectious bacteria known. Because of its extreme pathogenicity, is classified as a category A bioweapon by the US government. virulence stems from genes encoded on the pathogenicity island (FPI). An unusual set of regulators-the heteromeric macrophage growth locus protein A (MglA)-stringent starvation protein A (SspA) complex and the DNA-binding protein pathogenicity island gene regulator (PigR)-activates FPI transcription and thus is essential for virulence. Intriguingly, the second messenger, guanosine-tetraphosphate (ppGpp), which is produced during infection, is also involved in coordinating virulence; however, its role has been unclear. Here we identify MglA-SspA as a novel ppGpp-binding complex and describe structures of apo- and ppGpp-bound MglA-SspA. We demonstrate that MglA-SspA, which binds RNA polymerase (RNAP), also interacts with the C-terminal domain of PigR, thus anchoring the (MglA-SspA)-RNAP complex to the FPI promoter. Furthermore, we show that MglA-SspA must be bound to ppGpp to mediate high-affinity interactions with PigR. Thus, these studies unveil a novel pathway different from those described previously for regulation of transcription by ppGpp. The data also indicate that pathogenesis is controlled by a highly interconnected molecular circuitry in which the virulence machinery directly senses infection via a small molecule stress signal.
[Mh] Termos MeSH primário: Adesinas Bacterianas/metabolismo
Proteínas de Ligação a DNA/metabolismo
Francisella tularensis/patogenicidade
Ilhas Genômicas/genética
Guanosina Tetrafosfato/metabolismo
Tularemia/microbiologia
[Mh] Termos MeSH secundário: Adesinas Bacterianas/química
Adesinas Bacterianas/genética
Bioterrorismo/prevenção & controle
Células Cultivadas
Cristalografia
Proteínas de Ligação a DNA/química
Proteínas de Ligação a DNA/genética
RNA Polimerases Dirigidas por DNA/metabolismo
Regulação Bacteriana da Expressão Gênica
Guanosina Tetrafosfato/genética
Seres Humanos
Macrófagos/metabolismo
Conformação Proteica
Transcrição Genética
Virulência/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adhesins, Bacterial); 0 (DNA-Binding Proteins); 0 (SspA protein, bacteria); 33503-72-9 (Guanosine Tetraphosphate); EC 2.7.7.6 (DNA-Directed RNA Polymerases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170903
[St] Status:MEDLINE
[do] DOI:10.1101/gad.303701.117



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