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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


  2 / 3191 MEDLINE  
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[PMID]:29176760
[Au] Autor:Bruxelle JF; Mizrahi A; Hoÿs S; Collignon A; Janoir C; Péchiné S
[Ad] Endereço:EA4043 Unité Bactéries Pathogènes et Santé (UBaPS), Univ. Paris-Sud, Université Paris-Saclay, Châtenay-Malabry Cedex, France.
[Ti] Título:Clostridium difficile flagellin FliC: Evaluation as adjuvant and use in a mucosal vaccine against Clostridium difficile.
[So] Source:PLoS One;12(11):e0187212, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The immunogenicity of bacterial flagellin has been reported in different studies. By its close interaction with the immune system, the flagellin represents an interesting adjuvant and vaccine candidate. Salmonella Typhimurium flagellin has already been tested as adjuvant to stimulate mucosal immunity. Here, we assessed the ability of Clostridium difficile flagellin FliC to act as a mucosal adjuvant, first combined with ovalbumin as antigen and second with a C. difficile surface protein, the precursor of the S-layer proteins SlpA. Using ovalbumin as antigen, we compared the gut mucosal adjuvanticity of FliC to Salmonella Typhimurium flagellin and cholera toxin. Two routes of immunization were tested in a mouse model: intra-rectal and intra-peritoneal, following which, gut mucosal and systemic antibody responses against ovalbumin (Immunoglobulins G and Immunoglobulins A) were analyzed by Enzyme-Linked Immuno Assay in intestinal contents and in sera. In addition, ovalbumin-specific immunoglobulin producing cells were detected in the intestinal lamina propria by Enzyme-Linked Immunospot. Results showed that FliC as adjuvant for immunization targeting ovalbumin was able to stimulate a gut mucosal and systemic antibody response independently of the immunization route. In order to develop a mucosal vaccine to prevent C. difficile intestinal colonization, we assessed in a mouse model the efficacy of FliC as adjuvant compared with cholera toxin co-administrated with the C. difficile S-layer precursor SlpA as antigen. After challenge, a significant decrease of C. difficile intestinal colonization was observed in immunized groups compared to the control group. Our results showed that C. difficile FliC could be used as adjuvant in mucosal vaccination strategy against C. difficile infections.
[Mh] Termos MeSH primário: Adjuvantes Imunológicos/farmacologia
Proteínas de Bactérias/imunologia
Vacinas Bacterianas/imunologia
Clostridium difficile/imunologia
Flagelina/metabolismo
Imunidade nas Mucosas/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Anticorpos Antibacterianos/imunologia
Contagem de Células
Clostridium difficile/efeitos dos fármacos
Clostridium difficile/metabolismo
Contagem de Colônia Microbiana
Enterocolite Pseudomembranosa/sangue
Enterocolite Pseudomembranosa/imunologia
Enterocolite Pseudomembranosa/microbiologia
Feminino
Imunidade/efeitos dos fármacos
Imunização
Imunoglobulina G/sangue
Mucosa Intestinal/efeitos dos fármacos
Mucosa Intestinal/imunologia
Mucosa Intestinal/microbiologia
Glicoproteínas de Membrana/imunologia
Camundongos Endogâmicos C57BL
Ovalbumina/imunologia
Reto/imunologia
Vacinação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adjuvants, Immunologic); 0 (Antibodies, Bacterial); 0 (Bacterial Proteins); 0 (Bacterial Vaccines); 0 (Immunoglobulin G); 0 (Membrane Glycoproteins); 0 (S-layer proteins); 12777-81-0 (Flagellin); 9006-59-1 (Ovalbumin)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171219
[Lr] Data última revisão:
171219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0187212


  3 / 3191 MEDLINE  
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[PMID]:28973025
[Au] Autor:Poncini L; Wyrsch I; Dénervaud Tendon V; Vorley T; Boller T; Geldner N; Métraux JP; Lehmann S
[Ad] Endereço:Department of Biology, University of Fribourg, Fribourg, Switzerland.
[Ti] Título:In roots of Arabidopsis thaliana, the damage-associated molecular pattern AtPep1 is a stronger elicitor of immune signalling than flg22 or the chitin heptamer.
[So] Source:PLoS One;12(10):e0185808, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Plants interpret their immediate environment through perception of small molecules. Microbe-associated molecular patterns (MAMPs) such as flagellin and chitin are likely to be more abundant in the rhizosphere than plant-derived damage-associated molecular patterns (DAMPs). We investigated how the Arabidopsis thaliana root interprets MAMPs and DAMPs as danger signals. We monitored root development during exposure to increasing concentrations of the MAMPs flg22 and the chitin heptamer as well as of the DAMP AtPep1. The tissue-specific expression of defence-related genes in roots was analysed using a toolkit of promoter::YFPN lines reporting jasmonic acid (JA)-, salicylic acid (SA)-, ethylene (ET)- and reactive oxygen species (ROS)- dependent signalling. Finally, marker responses were analysed during invasion by the root pathogen Fusarium oxysporum. The DAMP AtPep1 triggered a stronger activation of the defence markers compared to flg22 and the chitin heptamer. In contrast to the tested MAMPs, AtPep1 induced SA- and JA-signalling markers in the root and caused a severe inhibition of root growth. Fungal attack resulted in a strong activation of defence genes in tissues close to the invading fungal hyphae. The results collectively suggest that AtPep1 presents a stronger danger signal to the Arabidopsis root than the MAMPs flg22 and chitin heptamer.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Quitina/metabolismo
Flagelina/metabolismo
Raízes de Plantas/metabolismo
Transdução de Sinais/fisiologia
Transativadores/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Arabidopsis/genética
Quitina/genética
Ciclopentanos/metabolismo
Etilenos/metabolismo
Flagelina/genética
Regulação da Expressão Gênica de Plantas
Oxilipinas/metabolismo
Raízes de Plantas/crescimento & desenvolvimento
Espécies Reativas de Oxigênio/metabolismo
Ácido Salicílico/metabolismo
Transativadores/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Cyclopentanes); 0 (Ethylenes); 0 (Oxylipins); 0 (Pep1 protein, Arabidopsis); 0 (Reactive Oxygen Species); 0 (Trans-Activators); 12777-81-0 (Flagellin); 1398-61-4 (Chitin); 6RI5N05OWW (jasmonic acid); 91GW059KN7 (ethylene); O414PZ4LPZ (Salicylic Acid)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171004
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185808


  4 / 3191 MEDLINE  
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[PMID]:28874019
[Au] Autor:Khoo JJ; Lim FS; Tan KK; Chen FS; Phoon WH; Khor CS; Pike BL; Chang LY; AbuBakar S
[Ad] Endereço:Tropical Infectious Diseases Research and Education Centre (TIDREC), University of Malaya, Kuala Lumpur, 50603, Malaysia.
[Ti] Título:Detection in Malaysia of a Borrelia sp. From Haemaphysalis hystricis (Ixodida: Ixodidae).
[So] Source:J Med Entomol;54(5):1444-1448, 2017 Sep 01.
[Is] ISSN:1938-2928
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Spirochetes from the Borrelia genus are known to cause diseases in humans, namely Lyme disease and relapsing fever. These organisms are commonly transmitted to humans by arthropod vectors including ticks, mite, and lice. Here, we report the molecular detection of a Borrelia sp. from a Haemaphysalis hystricis Supino tick collected from wildlife in an Orang Asli settlement in Selangor, Malaysia. Phylogenetic analyses of partial 16s rRNA and flaB gene sequences revealed that the Borrelia sp. is closely related to the relapsing fever group borreliae, Borrelia lonestari, Borrelia miyamotoi, and Borrelia theileri, as well as a number of uncharacterized Borrelia sp. from ticks in Portugal and Japan. To our knowledge, this is the first report of a Borrelia sp. detected in H. hystricis, and in Malaysia. The zoonotic potential of this Borrelia sp. merits further investigation.
[Mh] Termos MeSH primário: Borrelia/classificação
Borrelia/isolamento & purificação
Ixodidae/microbiologia
[Mh] Termos MeSH secundário: Animais
Borrelia/genética
Flagelina/genética
Malásia
Filogenia
RNA Bacteriano/genética
RNA Ribossômico 16S/genética
Análise de Sequência de RNA
Sus scrofa/parasitologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Bacterial); 0 (RNA, Ribosomal, 16S); 12777-81-0 (Flagellin); 140470-87-7 (flaB flagellin)
[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:170907
[St] Status:MEDLINE
[do] DOI:10.1093/jme/tjx131


  5 / 3191 MEDLINE  
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[PMID]:28827825
[Au] Autor:Forstneric V; Ivicak-Kocjan K; Plaper T; Jerala R; Bencina M
[Ad] Endereço:Department of Synthetic Biology and Immunology, National Institute of Chemistry, Ljubljana, Slovenia.
[Ti] Título:The role of the C-terminal D0 domain of flagellin in activation of Toll like receptor 5.
[So] Source:PLoS Pathog;13(8):e1006574, 2017 Aug.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Flagellin is a wide-spread bacterial virulence factor sensed by the membrane-bound Toll-like receptor 5 (TLR5) and by the intracellular NAIP5/NLRC4 inflammasome receptor. TLR5 recognizes a conserved region within the D1 domain of flagellin, crucial for the interaction between subunits in the flagellum and for bacterial motility. While it is known that a deletion of the D0 domain of flagellin, which lines the interior of flagella, also completely abrogates activation of TLR5, its functional role remains unknown. Using a protein fusion strategy, we propose a role for the D0 domain in the stabilization of an active dimeric signaling complex of flagellin-TLR5 at a 2:2 stoichiometric ratio. Alanine-scanning mutagenesis of flagellin revealed a previously unidentified region of flagellin, the C-terminal D0 domain, to play a crucial role in TLR5 activation. Interestingly, we show that TLR5 recognizes the same hydrophobic motif of the D0 domain of flagellin as the intracellular NAIP5/NLRC4 inflammasome receptor. Further, we show that residues within the D0 domain play a previously unrecognized role in the evasion of TLR5 recognition by Helicobacter pylori. These findings demonstrate that TLR5 is able to simultaneously sense several spatially separated sites of flagellin that are essential for its functionality, hindering bacterial evasion of immune recognition. Our findings significantly contribute to the understanding of the mechanism of TLR5 activation, which plays an important role in host defense against several pathogens, but also in several diseases, such as Crohn's disease, cystic fibrosis and rheumatoid arthritis.
[Mh] Termos MeSH primário: Infecções Bacterianas/imunologia
Flagelina/imunologia
Imunidade Inata/imunologia
Receptor 5 Toll-Like/imunologia
[Mh] Termos MeSH secundário: Animais
Western Blotting
Linhagem Celular
Flagelina/metabolismo
Seres Humanos
Imunoprecipitação
Camundongos
Receptor 5 Toll-Like/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Toll-Like Receptor 5); 12777-81-0 (Flagellin)
[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:170823
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006574


  6 / 3191 MEDLINE  
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[PMID]:28750075
[Au] Autor:Alexander KL; Katz J; Elson CO
[Ad] Endereço:Department of Medicine, University of Alabama at Birmingham, Birmingham, AL, United States of America.
[Ti] Título:CBirTox is a selective antigen-specific agonist of the Treg-IgA-microbiota homeostatic pathway.
[So] Source:PLoS One;12(7):e0181866, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cultivating an environment of mutualism between host cells and the microbiota is vital, and dysregulation of this relationship is associated with multiple immune disorders including metabolic and skin diseases, asthma, allergy, and Inflammatory Bowel Disease (IBD). One prominent mechanism for maintaining homeostasis is the protective regulatory T cell (Treg)- Immunoglobulin A (IgA) pathway toward microbiota antigens, in which Tregs maintain homeostasis and provide critical survival factors to IgA+ B cells. In order to amplify the Treg-IgA pathway, we have generated a fusion protein, CBirTox, comprised of a portion of the carboxy terminus of CBir1, a microbiota flagellin, genetically coupled to Cholera Toxin B subunit (CTB) via the A2 linker of CT. Both dendritic cells (DCs) and B cells pulsed with CBirTox selectively induced functional CD4+Foxp3+ Tregs in vitro, and CBirTox augmented CD4+Foxp3+ cell numbers in vivo. The induced Foxp3 expression was independent of retinoic acid (RA) signaling but was inhibited by neutralization of TGF-ß. CBirTox treatment of B cells downregulated mammalian target of rapamycin (mTOR) signaling. Furthermore, CBirTox-pulsed DCs induced substantial production of IgA from naïve B cells. Collectively these data demonstrate that CBirTox represents a novel approach to bolstering the Treg-IgA pathway at the host-microbiota interface.
[Mh] Termos MeSH primário: Epitopos/imunologia
Flagelina/agonistas
Homeostase
Imunoglobulina A/imunologia
Microbiota
Linfócitos T Reguladores/imunologia
[Mh] Termos MeSH secundário: Animais
Células Apresentadoras de Antígenos/metabolismo
Linfócitos B/imunologia
Linhagem Celular
Toxina da Cólera/metabolismo
Células Dendríticas/imunologia
Fatores de Transcrição Forkhead/metabolismo
Genômica
Intestinos
Camundongos Endogâmicos C57BL
Proteínas Recombinantes de Fusão/metabolismo
Transdução de Sinais
Serina-Treonina Quinases TOR/metabolismo
Fator de Crescimento Transformador beta/metabolismo
Tretinoína/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CBir1 flagellin); 0 (Epitopes); 0 (Forkhead Transcription Factors); 0 (Foxp3 protein, mouse); 0 (Immunoglobulin A); 0 (Recombinant Fusion Proteins); 0 (Transforming Growth Factor beta); 12777-81-0 (Flagellin); 5688UTC01R (Tretinoin); 9012-63-9 (Cholera Toxin); EC 2.7.1.1 (TOR Serine-Threonine Kinases)
[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:170728
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0181866


  7 / 3191 MEDLINE  
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[PMID]:28710253
[Au] Autor:Lee SJ; Benoun J; Sheridan BS; Fogassy Z; Pham O; Pham QM; Puddington L; McSorley SJ
[Ad] Endereço:Center for Comparative Medicine, School of Veterinary Medicine, University of California, Davis, Davis, CA 95616.
[Ti] Título:Dual Immunization with SseB/Flagellin Provides Enhanced Protection against Infection Mediated by Circulating Memory Cells.
[So] Source:J Immunol;199(4):1353-1361, 2017 Aug 15.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The development of a subunit vaccine has been hindered by the absence of detailed information about antigenic targets of protective -specific T and B cells. Recent studies have identified SseB as a modestly protective Ag in susceptible C57BL/6 mice, but the mechanism of protective immunity remains undefined. In this article, we report that simply combining SseB with flagellin substantially enhances protective immunity, allowing immunized C57BL/6 mice to survive for up to 30 d following challenge with virulent bacteria. Surprisingly, the enhancing effect of flagellin did not require flagellin Ag targeting during secondary responses or recognition of flagellin by TLR5. Although coimmunization with flagellin did not affect SseB-specific Ab responses, it modestly boosted CD4 responses. In addition, protective immunity was effectively transferred in circulation to parabionts of immunized mice, demonstrating that tissue-resident memory is not required for vaccine-induced protection. Finally, protective immunity required host expression of IFN-γR but was independent of induced NO synthase expression. Taken together, these data indicate that flagellin has unique adjuvant properties that improve SseB-mediated protective immunity provided by circulating memory.
[Mh] Termos MeSH primário: Proteínas de Bactérias/imunologia
Flagelina/imunologia
Memória Imunológica
Chaperonas Moleculares/imunologia
Salmonelose Animal/prevenção & controle
Vacinas contra Salmonella/imunologia
[Mh] Termos MeSH secundário: Adjuvantes Imunológicos
Animais
Anticorpos Antibacterianos/sangue
Linfócitos T CD4-Positivos/imunologia
Feminino
Imunização
Camundongos
Camundongos Endogâmicos C57BL
Óxido Nítrico Sintase/genética
Óxido Nítrico Sintase/metabolismo
Receptores de Interferon/genética
Receptores de Interferon/imunologia
Vacinas contra Salmonella/administração & dosagem
Salmonella typhimurium/imunologia
Receptor 5 Toll-Like/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adjuvants, Immunologic); 0 (Antibodies, Bacterial); 0 (Bacterial Proteins); 0 (Molecular Chaperones); 0 (Receptors, Interferon); 0 (Salmonella Vaccines); 0 (SseB protein, Salmonella typhimurium); 0 (Toll-Like Receptor 5); 0 (interferon gamma receptor); 12777-81-0 (Flagellin); EC 1.14.13.39 (Nitric Oxide Synthase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170716
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1601357


  8 / 3191 MEDLINE  
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[PMID]:28665716
[Au] Autor:Thomrongsuwannakij T; Blackall PJ; Chansiripornchai N
[Ad] Endereço:A Avian Health Research Unit, Department of Veterinary Medicine, Faculty of Veterinary Science, Chulalongkorn University, Bangkok 10330, Thailand.
[Ti] Título:A Study on Campylobacter jejuni and Campylobacter coli through Commercial Broiler Production Chains in Thailand: Antimicrobial Resistance, the Characterization of DNA Gyrase Subunit A Mutation, and Genetic Diversity by Flagellin A Gene Restriction Fragment Length Polymorphism.
[So] Source:Avian Dis;61(2):186-197, 2017 Jun.
[Is] ISSN:1938-4351
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Contaminated poultry meat is regarded as the main source of human campylobacteriosis. During September 2014 and February 2015, breeder flocks, hatcheries, and broiler farms from two chicken production chains were investigated chronologically. Five commercial breeder flocks (Breeder Flocks 1-5), two hatcheries (Hatcheries A and B), and five broiler flocks (Broiler Flocks 1-5) were sampled in this study. Campylobacter colonization of both breeder and broiler flocks was determined from cloacal swabs and environmental samples (pan feeders, footwear, darkling beetles, flies, feed, and water). The eggs from the breeder flocks were followed to hatcheries. At the hatcheries, early embryonic deaths, egg trays, eggshells, hatchers, and water were investigated. Cloacal swabs were taken from broilers at Days 1, 14, and 28 (all broiler flocks), and either 35 (Broiler Flocks 1 and 2) or 43 (Broiler Flocks 3-5). Thirty-six Campylobacter jejuni and 94 Campylobacter coli isolates collected through two broiler production chains were tested by twofold agar dilution for their susceptibility to antimicrobial agents. Most Campylobacter isolates were multidrug resistant (MDR), defined as being resistant to three or more antimicrobial classes ( C. jejuni : 100%; C. coli : 98.9%), and exhibited high resistance to enrofloxacin ( C. jejuni : 100%; C. coli : 98.9%). The vast majority of C. coli were resistant to tetracycline (97.9%), trimethoprim-sulfamethoxazole (81.9%), and doxycycline (79.8%), but only 55.6%, 36.1%, and 50% of C. jejuni isolates revealed resistance to these antimicrobial agents, respectively. A selected subset of 24 C. jejuni and 24 C. coli were characterized for their mutations in the quinolone resistance determining region of the DNA gyrase subunit A gene by nucleotide sequence analysis. The Thr-86-Ile substitution (ACA-ATA in C. jejuni or ACT-ATT in C. coli ) was found in all isolates. Moreover, a total of 130 Campylobacter isolates were typed with the use of polymerase chain reaction-restriction fragment length polymorphism of the flagellin A gene (flaA-RFLP) to determine their genetic relationships. Ten distinct clusters were recognized by flaA-RFLP typing. The results showed that horizontal transmission was the major route of Campylobacter transmission in this study. In conclusion, the emergence of MDR and high resistance rates to several antimicrobials are major concerns identified in this study. The prudent use of these agents and active surveillance of resistance at the farm level are essential steps to reduce the public health risks identified in this work.
[Mh] Termos MeSH primário: Proteínas de Bactérias/genética
Infecções por Campylobacter/veterinária
Campylobacter coli/genética
Campylobacter jejuni/genética
DNA Girase/genética
Farmacorresistência Bacteriana
Flagelina/genética
Doenças das Aves Domésticas/microbiologia
[Mh] Termos MeSH secundário: Animais
Antibacterianos/farmacologia
Proteínas de Bactérias/metabolismo
Infecções por Campylobacter/microbiologia
Campylobacter coli/efeitos dos fármacos
Campylobacter coli/enzimologia
Campylobacter coli/isolamento & purificação
Campylobacter jejuni/efeitos dos fármacos
Campylobacter jejuni/enzimologia
Campylobacter jejuni/isolamento & purificação
Galinhas
DNA Girase/metabolismo
Flagelina/metabolismo
Mutação
Filogenia
Polimorfismo de Fragmento de Restrição
Tailândia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Bacterial Proteins); 12777-81-0 (Flagellin); EC 5.99.1.3 (DNA Gyrase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170823
[Lr] Data última revisão:
170823
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170701
[St] Status:MEDLINE
[do] DOI:10.1637/11546-120116-Reg.1


  9 / 3191 MEDLINE  
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[PMID]:28622575
[Au] Autor:Deng L; Kim JR; Chang TZ; Zhang H; Mohan T; Champion JA; Wang BZ
[Ad] Endereço:Center for Inflammation, Immunity & Infection, Georgia State University Institute for Biomedical Sciences, Atlanta, GA, USA.
[Ti] Título:Protein nanoparticle vaccine based on flagellin carrier fused to influenza conserved epitopes confers full protection against influenza A virus challenge.
[So] Source:Virology;509:82-89, 2017 Sep.
[Is] ISSN:1096-0341
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Currently marketed influenza vaccines only confer protection against matching influenza virus strains. The influenza A composition of these vaccines needs to be annually updated. Vaccines that target conserved epitopes of influenza viruses would in principle offer broad cross-protection against influenza A viruses. In our study, we investigated the specific immune responses and protective efficacy of protein nanoparticles based on fusion proteins of flagellin carrier linked to conserved influenza epitopes. We designed fusion proteins by replacing the hyperimmunogenic region of flagellin (FliC) with four tandem copies of the ectodomain of matrix protein 2 (f4M2e), H1 HA2 domain (fHApr8) or H3 HA2 domain (fHAaichi). Protein nanoparticles fabricated from these fusion proteins by using DTSSP crosslinking retained Toll-like receptor 5 agonist activity of FliC. Intranasal immunization with f4M2e, f4M2e/fHApr8 or f4M2e/fHAaichi nanoparticles induced vaccine antigen-specific humoral immune responses. It was also found that the incorporation of the H1 HA2 domain into f4M2e/fHApr8 nanoparticles boosted M2e specific antibody responses. Immunized mice were fully protected against lethal doses of virus challenge.
[Mh] Termos MeSH primário: Portadores de Fármacos/metabolismo
Epitopos/imunologia
Flagelina/metabolismo
Vacinas contra Influenza/imunologia
Nanopartículas
[Mh] Termos MeSH secundário: Administração Intranasal
Animais
Anticorpos Antivirais/sangue
Modelos Animais de Doenças
Epitopos/genética
Flagelina/genética
Glicoproteínas de Hemaglutininação de Vírus da Influenza/genética
Glicoproteínas de Hemaglutininação de Vírus da Influenza/imunologia
Vacinas contra Influenza/administração & dosagem
Vacinas contra Influenza/genética
Camundongos
Infecções por Orthomyxoviridae/prevenção & controle
Ligação Proteica
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/imunologia
Análise de Sobrevida
Receptor 5 Toll-Like/metabolismo
Vacinas de Subunidades/administração & dosagem
Vacinas de Subunidades/genética
Vacinas de Subunidades/imunologia
Vacinas Sintéticas/administração & dosagem
Vacinas Sintéticas/genética
Vacinas Sintéticas/imunologia
Proteínas da Matriz Viral/genética
Proteínas da Matriz Viral/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Viral); 0 (Drug Carriers); 0 (Epitopes); 0 (Hemagglutinin Glycoproteins, Influenza Virus); 0 (Influenza Vaccines); 0 (M2 protein, Influenza A virus); 0 (Recombinant Fusion Proteins); 0 (Toll-Like Receptor 5); 0 (Vaccines, Subunit); 0 (Vaccines, Synthetic); 0 (Viral Matrix Proteins); 12777-81-0 (Flagellin)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170726
[Lr] Data última revisão:
170726
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170617
[St] Status:MEDLINE


  10 / 3191 MEDLINE  
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[PMID]:28586664
[Au] Autor:Hughes KT
[Ad] Endereço:Department of Biology, University of Utah, Salt Lake City, UT 84112, USA. Electronic address: Kelly.Hughes@utah.edu.
[Ti] Título:Flagellum Length Control: How Long Is Long Enough?
[So] Source:Curr Biol;27(11):R413-R415, 2017 Jun 05.
[Is] ISSN:1879-0445
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The bacterial flagellum is an organelle that self-assembles outside the cell body. Recent work has uncovered the mechanism for length control of this self-assembly process.
[Mh] Termos MeSH primário: Bactérias/citologia
Fenômenos Fisiológicos Bacterianos
Flagelos/fisiologia
[Mh] Termos MeSH secundário: Bactérias/classificação
Flagelos/química
Flagelina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
12777-81-0 (Flagellin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170607
[St] Status:MEDLINE



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