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  1 / 10706 MEDLINE  
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[PMID]:29360856
[Au] Autor:Yang Y; Xu H; Lu Y; Wang C; Lu Z
[Ad] Endereço:State Key Laboratory Breeding Base for Zhejiang Sustainable Pest and Disease Control, Institute of Plant Protection and Microbiology, Zhejiang Academy of Agricultural Sciences, Hangzhou, China.
[Ti] Título:Midgut transcriptomal response of the rice leaffolder, Cnaphalocrocis medinalis (Guenée) to Cry1C toxin.
[So] Source:PLoS One;13(1):e0191686, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cnaphalocrocis medinalis (Guenée) is one of the important insect pests in rice field. Bt agents were recommended in the C. medinalis control and Bt rice is bred as a tactic to control this insect. However, the tolerance or resistance of insect to Bt protein is a main threat to the application of Bt protein. In order to investigate the response of C. medinalis transcriptome in defending a Cry1C toxin, high-through RNA-sequencing was carried in the C. medinalis larvae treated with and without Cry1C toxin. A total of 35,586 high-quality unigenes was annotated in the transcriptome of C. medinalis midgut. The comparative analysis identified 6,966 differently expressed unigenes (DEGs) between the two treatments. GO analysis showed that these genes involved in proteolysis and extracellular region. Among these DEGs, carboxylesterase, glutathione S-transferase and P450 were differently expressed in the treated C. medinalis midgut. Furthermore, trypsin, chymotrypsin, and carboxypeptidase were identified in DEGs, and most of them up-regulated. In addition, thirteen ABC transporters were downregulated and three upregulated in Cry1C-treated C. medinalis midgut. Based on the pathway analysis, antigen processing and presentation pathway, and chronic myeloid leukemia pathway were significant in C. medinalis treated with Cry1C toxin. These results indicated that serine protease, detoxification enzymes and ABC transporter, antigen processing and presentation pathway, and chronic myeloid leukemia pathway may involved in the response of C. medinalis to Cry1C toxin. This study provides a transcriptomal foundation for the identification and functional characterization of genes involved in the toxicity of Bt Cry protein against C. medinalis, and provides potential clues to the studies on the tolerance or resistance of an agriculturally important insect pest C. medinalis to Cry1C toxin.
[Mh] Termos MeSH primário: Proteínas de Bactérias/toxicidade
Endotoxinas/toxicidade
Proteínas Hemolisinas/toxicidade
Mariposas/efeitos dos fármacos
Transcriptoma
[Mh] Termos MeSH secundário: Animais
Mariposas/genética
Análise de Sequência de RNA
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Endotoxins); 0 (Hemolysin Proteins); 0 (insecticidal crystal protein, Bacillus Thuringiensis)
[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:180124
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191686


  2 / 10706 MEDLINE  
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[PMID]:29080422
[Au] Autor:Sakata J; Yonekita T; Kawatsu K
[Ad] Endereço:Division of Microbiology Bacteriology Section, Osaka Institute of Public Health, 3-69, Nakamichi 1-chome, Higashinari-ku, Osaka 537-0025, Japan. Electronic address: sakata@iph.osaka.jp.
[Ti] Título:Development of a rapid immunochromatographic assay to detect contamination of raw oysters with enteropathogenic Vibrio parahaemolyticus.
[So] Source:Int J Food Microbiol;264:16-24, 2018 Jan 02.
[Is] ISSN:1879-3460
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Thermostable direct hemolysin (TDH) and TDH-related hemolysin (TRH) are major virulence factors of enteropathogenic Vibrio parahaemolyticus. TDH and TRH are bacterial exotoxins, and their presence in culture medium serves as a specific marker for detecting this significant pathogen. Here, we developed and evaluated an immunochromatographic assay (TDH/TRH-ICA) to simultaneously or individually detect TDH and TRH. The TDH/TRH-ICA detected TDH in all broth cultures of 47 V. parahaemolyticus strains carrying tdh. The genes encoding TRH are classified as variants trh1 and trh2, and TRH was detected in all broth cultures of 25 V. parahaemolyticus strains carrying trh1 and certain proportion (5/31) of broth cultures of V. parahaemolyticus strains carrying trh2. In contrast, TDH and TRH were not detected in broth cultures of 12 non-enteropathogenic V. parahaemolyticus strains without tdh and trh. It was difficult to detect TRH2 using the TDH/TRH-ICA. However, TRH2 may not serve as a suitable marker for detecting enteropathogenic V. parahaemolyticus, and evidence indicates that TRH2 may not contribute to enteropathogenesis. Further, a screening method using a combination of TDH/TRH-ICA and SPP medium supplemented with 1.5% NaCl (modified-SPP medium) detected oyster samples artificially spiked with 1.1-22 colony-forming units of enteropathogenic V. parahaemolyticus per 25g of oysters within approximately 8.5h, including the enrichment culture. The assay may serve as a method that facilitates the rapid and easy detection of raw oysters contaminated with enteropathogenic V. parahaemolyticus.
[Mh] Termos MeSH primário: Proteínas de Bactérias/análise
Proteínas Hemolisinas/análise
Imunocromatografia/métodos
Ostreidae/microbiologia
Vibrio parahaemolyticus/genética
[Mh] Termos MeSH secundário: Animais
Anticorpos Monoclonais/imunologia
Proteínas de Bactérias/genética
Proteínas de Bactérias/imunologia
Toxinas Bacterianas/análise
Toxinas Bacterianas/genética
Toxinas Bacterianas/imunologia
Proteínas Hemolisinas/genética
Proteínas Hemolisinas/imunologia
Camundongos
Camundongos Endogâmicos BALB C
Vibrio parahaemolyticus/classificação
Vibrio parahaemolyticus/isolamento & purificação
Fatores de Virulência/análise
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Bacterial Proteins); 0 (Bacterial Toxins); 0 (Hemolysin Proteins); 0 (Virulence Factors); 0 (thermostable direct hemolysin-related hemolysin protein, Vibrio parahaemolyticus); 135433-21-5 (thermostable direct hemolysin)
[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


  3 / 10706 MEDLINE  
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[PMID]:28926817
[Au] Autor:Chen Y; Yang Y; Zhu H; Romeis J; Li Y; Peng Y; Chen X
[Ad] Endereço:The State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing 100193, China.
[Ti] Título:Safety of Bacillus thuringiensis Cry1C protein for Daphnia magna based on different functional traits.
[So] Source:Ecotoxicol Environ Saf;147:631-636, 2018 Jan.
[Is] ISSN:1090-2414
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Cry1C is a Bacillus thuringiensis (Bt) insecticidal protein and it can be produced by transgenic rice lines developed in China. Cladocera species are common aquatic arthropods that may be exposed to insecticidal proteins produced in Bt-transgenic plants through ingestion of pollen or crop residues in water. As the cladoceran Daphnia magna plays an important role in the aquatic food chain, it is important to assess the possible effects of Bt crops to this species. To evaluate the safety of the Cry1C protein for D. magna, individuals were exposed to different concentrations of purified Cry1C protein in M4 medium for 21 days. Potassium dichromate (K Cr O ), a known toxicant to D. magna, was added to M4 medium as a positive control treatment, and pure M4 medium was used as a negative control. Our results show that developmental, reproductive, and biochemical parameters of D. magna were not significantly different between Cry1C and negative control treatments but were significantly inhibited by the positive control. We thus conclude that D. magna is insensitive to Cry1C.
[Mh] Termos MeSH primário: Proteínas de Bactérias/toxicidade
Daphnia/efeitos dos fármacos
Endotoxinas/toxicidade
Proteínas Hemolisinas/toxicidade
Poluentes Químicos da Água/toxicidade
[Mh] Termos MeSH secundário: Animais
Proteínas de Bactérias/genética
China
Relação Dose-Resposta a Droga
Endotoxinas/genética
Proteínas Hemolisinas/genética
Oryza/genética
Oryza/metabolismo
Plantas Geneticamente Modificadas/genética
Plantas Geneticamente Modificadas/metabolismo
Testes de Toxicidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Endotoxins); 0 (Hemolysin Proteins); 0 (Water Pollutants, Chemical); 0 (insecticidal crystal protein, Bacillus Thuringiensis)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180223
[Lr] Data última revisão:
180223
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170920
[St] Status:MEDLINE


  4 / 10706 MEDLINE  
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[PMID]:29293334
[Au] Autor:Qiu Y; Li P; Dong S; Zhang X; Yang Q; Wang Y; Ge J; Hammock BD; Zhang C; Liu X
[Ad] Endereço:Laboratory for Food Quality and Safety-State Key Laboratory Cultivation Base of Ministry of Science and Technology,Key Laboratory of Control Technology and Standard for Agro-product Safety and Quality (Ministry of Agriculture), Institute of Food Safety and Nutrition, Jiangsu Academy of Agricultural
[Ti] Título:Phage-Mediated Competitive Chemiluminescent Immunoassay for Detecting Cry1Ab Toxin by Using an Anti-Idiotypic Camel Nanobody.
[So] Source:J Agric Food Chem;66(4):950-956, 2018 Jan 31.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cry toxins have been widely used in genetically modified organisms for pest control, raising public concern regarding their effects on the natural environment and food safety. In this work, a phage-mediated competitive chemiluminescent immunoassay (c-CLIA) was developed for determination of Cry1Ab toxin using anti-idiotypic camel nanobodies. By extracting RNA from camels' peripheral blood lymphocytes, a naive phage-displayed nanobody library was established. Using anti-Cry1Ab toxin monoclonal antibodies (mAbs) against the library for anti-idiotypic antibody screening, four anti-idiotypic nanobodies were selected and confirmed to be specific for anti-Cry1Ab mAb binding. Thereafter, a c-CLIA was developed for detection of Cry1Ab toxin based on anti-idiotypic camel nanobodies and employed for sample testing. The results revealed a half-inhibition concentration of developed assay to be 42.68 ± 2.54 ng/mL, in the linear range of 10.49-307.1 ng/mL. The established method is highly specific for Cry1Ab recognition, with negligible cross-reactivity for other Cry toxins. For spiked cereal samples, the recoveries of Cry1Ab toxin ranged from 77.4% to 127%, with coefficient of variation of less than 9%. This study demonstrated that the competitive format based on phage-displayed anti-idiotypic nanobodies can provide an alternative strategy for Cry toxin detection.
[Mh] Termos MeSH primário: Anticorpos Anti-Idiotípicos
Proteínas de Bactérias/análise
Bacteriófagos
Camelus/imunologia
Endotoxinas/análise
Proteínas Hemolisinas/análise
Medições Luminescentes/métodos
Anticorpos de Domínio Único
[Mh] Termos MeSH secundário: Animais
Anticorpos Monoclonais
Proteínas de Bactérias/imunologia
Camelus/sangue
Grãos Comestíveis/química
Endotoxinas/imunologia
Contaminação de Alimentos/análise
Proteínas Hemolisinas/imunologia
Linfócitos/química
Biblioteca de Peptídeos
RNA/isolamento & purificação
Anticorpos de Domínio Único/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Anti-Idiotypic); 0 (Antibodies, Monoclonal); 0 (Bacterial Proteins); 0 (Endotoxins); 0 (Hemolysin Proteins); 0 (Peptide Library); 0 (Single-Domain Antibodies); 0 (insecticidal crystal protein, Bacillus Thuringiensis); 63231-63-0 (RNA)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180103
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b04923


  5 / 10706 MEDLINE  
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[PMID]:29324785
[Au] Autor:Joerling J; Barth SA; Schlez K; Willems H; Herbst W; Ewers C
[Ad] Endereço:Institute of Hygiene and Infectious Diseases of Animals, Justus Liebig University Giessen, Giessen, Germany.
[Ti] Título:Phylogenetic diversity, antimicrobial susceptibility and virulence gene profiles of Brachyspira hyodysenteriae isolates from pigs in Germany.
[So] Source:PLoS One;13(1):e0190928, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Swine dysentery (SD) is an economically important diarrheal disease in pigs caused by different strongly hemolytic Brachyspira (B.) species, such as B. hyodysenteriae, B. suanatina and B. hampsonii. Possible associations of epidemiologic data, such as multilocus sequence types (STs) to virulence gene profiles and antimicrobial susceptibility are rather scarce, particularly for B. hyodysenteriae isolates from Germany. In this study, B. hyodysenteriae (n = 116) isolated from diarrheic pigs between 1990 and 2016 in Germany were investigated for their STs, susceptibility to the major drugs used for treatment of SD (tiamulin and valnemulin) and genes that were previously linked with virulence and encode for hemolysins (tlyA, tlyB, tlyC, hlyA, BHWA1_RS02885, BHWA1_RS09085, BHWA1_RS04705, and BHWA1_RS02195), outer membrane proteins (OMPs) (bhlp16, bhlp17.6, bhlp29.7, bhmp39f, and bhmp39h) as well as iron acquisition factors (ftnA and bitC). Multilocus sequence typing (MLST) revealed that 79.4% of the isolates belonged to only three STs, namely ST52 (41.4%), ST8 (12.1%), and ST112 (25.9%) which have been observed in other European countries before. Another 24 isolates belonged to twelve new STs (ST113-118, ST120-123, ST131, and ST193). The temporal distribution of STs revealed the presence of new STs as well as the regular presence of ST52 over three decades (1990s-2000s). The proportion of strains that showed resistance to both tiamulin und valnemulin (39.1%) varied considerably among the most frequent STs ranging from 0% (0/14 isolates resistant) in ST8 isolates to 46.7% (14/30), 52.1% (25/48), and 85.7% (6/7) in isolates belonging to ST112, ST52, and ST114, respectively. All hemolysin genes as well as the iron-related gene ftnA and the OMP gene bhlp29.7 were regularly present in the isolates, while the OMP genes bhlp17.6 and bhmp39h could not be detected. Sequence analysis of hemolysin genes of selected isolates revealed co-evolution of tlyB, BHWA1_RS02885, BHWA1_RS09085, and BHWA1_RS02195 with the core genome and suggested independent evolution of tlyA, tlyC, and hlyA. Our data indicate that in Germany, swine dysentery might be caused by a limited number of B. hyodysenteriae clonal groups. Major STs (ST8, ST52, and ST112) are shared with other countries in Europe suggesting a possible role of the European intra-Community trade of pigs in the dissemination of certain clones. The identification of several novel STs, some of which are single or double locus variants of ST52, may on the other hand hint towards an ongoing diversification of the pathogen in the studied area. The linkage of pleuromutilin susceptibility and sequence type of an isolate might reflect a clonal expansion of the underlying resistance mechanism, namely mutations in the ribosomal RNA genes. A linkage between single virulence-associated genes (VAGs) or even VAG patterns and the phylogenetic background of the isolates could not be established, since almost all VAGs were regularly present in the isolates.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Brachyspira hyodysenteriae/efeitos dos fármacos
Brachyspira hyodysenteriae/patogenicidade
Farmacorresistência Bacteriana/genética
[Mh] Termos MeSH secundário: Animais
Proteínas de Bactérias/genética
Brachyspira hyodysenteriae/genética
Brachyspira hyodysenteriae/isolamento & purificação
Diterpenos/farmacologia
Disenteria/microbiologia
Disenteria/veterinária
Fezes/microbiologia
Alemanha
Infecções por Bactérias Gram-Negativas/microbiologia
Infecções por Bactérias Gram-Negativas/veterinária
Proteínas Hemolisinas/genética
Filogenia
Polimorfismo de Nucleotídeo Único
Proteínas Ribossômicas/genética
Sus scrofa
Suínos
Doenças dos Suínos/microbiologia
Virulência/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Bacterial Proteins); 0 (Diterpenes); 0 (Hemolysin Proteins); 0 (Ribosomal Proteins); 0 (ribosomal protein L3); 125-65-5 (pleuromutilin)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180206
[Lr] Data última revisão:
180206
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180112
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190928


  6 / 10706 MEDLINE  
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[PMID]:29215274
[Au] Autor:Zhang L; Zhao G; Hu X; Liu J; Li M; Batool K; Chen M; Wang J; Xu J; Huang T; Pan X; Xu L; Yu XQ; Guan X
[Ad] Endereço:Division of Cell Biology and Biophysics, University of Missouri-Kansas City , Kansas City, Missouri 64110, United States.
[Ti] Título:Cry11Aa Interacts with the ATP-Binding Protein from Culex quinquefasciatus To Improve the Toxicity.
[So] Source:J Agric Food Chem;65(50):10884-10890, 2017 Dec 20.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cry11Aa displays high toxicity to the larvae of several mosquito species, including Aedes, Culex, and Anopheles. To study its binding characterization against Culex quinquefasciatus, Cry11Aa was purified and western blot results showed that Cry11Aa could bind successfully to the brush border membrane vesicles. To identify Cry11Aa-binding proteins in C. quinquefasciatus, a biotin-based protein pull-down experiment was performed and seven Cry11Aa-binding proteins were isolated from the midgut of C. quinquefasciatus larvae. Analysis of liquid chromatography-tandem mass spectrometry showed that one of the Cry11Aa-binding proteins is the ATP-binding domain 1 family member B. To investigate its binding property and effect on the toxicity of Cry11Aa, western blot, far-western blot, enzyme-linked immunosorbent assay, and bioassays of Cry11Aa in the presence and absence of the recombinant ATP-binding protein were performed. Our results showed that the ATP-binding protein interacted with Cry11Aa and increased the toxicity of Cry11Aa against C. quinquefasciatus. Our study suggests that midgut proteins other than the toxin receptors may modulate the toxicity of Cry toxins against mosquitoes.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/metabolismo
Proteínas de Bactérias/metabolismo
Culex/metabolismo
Endotoxinas/metabolismo
Proteínas Hemolisinas/metabolismo
Proteínas de Insetos/metabolismo
[Mh] Termos MeSH secundário: Animais
Proteínas de Bactérias/toxicidade
Culex/química
Culex/efeitos dos fármacos
Culex/genética
Endotoxinas/toxicidade
Proteínas Hemolisinas/toxicidade
Proteínas de Insetos/química
Proteínas de Insetos/genética
Larva/efeitos dos fármacos
Larva/genética
Larva/crescimento & desenvolvimento
Larva/metabolismo
Ligação Proteica
Domínios Proteicos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Endotoxins); 0 (Hemolysin Proteins); 0 (Insect Proteins); 0 (insecticidal crystal protein, Bacillus Thuringiensis); 8L70Q75FXE (Adenosine Triphosphate)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180110
[Lr] Data última revisão:
180110
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171208
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b04427


  7 / 10706 MEDLINE  
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[PMID]:29190284
[Au] Autor:Kortebi M; Milohanic E; Mitchell G; Péchoux C; Prevost MC; Cossart P; Bierne H
[Ad] Endereço:Micalis Institute, Inra, AgroParisTech, Université Paris-Saclay, Equipe Epigénétique et Microbiologie Cellulaire, Jouy-en-Josas, France.
[Ti] Título:Listeria monocytogenes switches from dissemination to persistence by adopting a vacuolar lifestyle in epithelial cells.
[So] Source:PLoS Pathog;13(11):e1006734, 2017 Nov.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Listeria monocytogenes causes listeriosis, a foodborne disease that poses serious risks to fetuses, newborns and immunocompromised adults. This intracellular bacterial pathogen proliferates in the host cytosol and exploits the host actin polymerization machinery to spread from cell-to-cell and disseminate in the host. Here, we report that during several days of infection in human hepatocytes or trophoblast cells, L. monocytogenes switches from this active motile lifestyle to a stage of persistence in vacuoles. Upon intercellular spread, bacteria gradually stopped producing the actin-nucleating protein ActA and became trapped in lysosome-like vacuoles termed Listeria-Containing Vacuoles (LisCVs). Subpopulations of bacteria resisted degradation in LisCVs and entered a slow/non-replicative state. During the subculture of host cells harboring LisCVs, bacteria showed a capacity to cycle between the vacuolar and the actin-based motility stages. When ActA was absent, such as in ΔactA mutants, vacuolar bacteria parasitized host cells in the so-called "viable but non-culturable" state (VBNC), preventing their detection by conventional colony counting methods. The exposure of infected cells to high doses of gentamicin did not trigger the formation of LisCVs, but selected for vacuolar and VBNC bacteria. Together, these results reveal the ability of L. monocytogenes to enter a persistent state in a subset of epithelial cells, which may favor the asymptomatic carriage of this pathogen, lengthen the incubation period of listeriosis, and promote bacterial survival during antibiotic therapy.
[Mh] Termos MeSH primário: Células Epiteliais/metabolismo
Listeria monocytogenes
Listeriose/microbiologia
[Mh] Termos MeSH secundário: Proteínas de Bactérias/metabolismo
Linhagem Celular
Citoplasma/metabolismo
Proteínas de Choque Térmico/metabolismo
Proteínas Hemolisinas/metabolismo
Seres Humanos
Proteínas de Membrana/metabolismo
Vacúolos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Heat-Shock Proteins); 0 (Hemolysin Proteins); 0 (Membrane Proteins)
[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:171201
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006734


  8 / 10706 MEDLINE  
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[PMID]:28981636
[Au] Autor:Chang X; Lu Z; Shen Z; Peng Y; Ye G
[Ad] Endereço:State Key Laboratory of Rice Biology & Agricultural Entomology of Ministry of Agriculture, Institute of Insect Sciences, Zhejiang University, Hangzhou 310058, China.
[Ti] Título:Bitrophic and Tritrophic Effects of Transgenic cry1Ab/cry2Aj Maize on the Beneficial, Nontarget Harmonia axyridis (Coleoptera: Coccinellidae).
[So] Source:Environ Entomol;46(5):1171-1176, 2017 10 01.
[Is] ISSN:1938-2936
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Harmonia axyridis (Pallas) is a common and abundant predator in China and may be exposed to Cry toxins that are produced in Bt crops either by feeding on plant parts or by feeding on target or nontarget herbivorous insects. A new Bt maize line, expressing the Cry1Ab/Cry2Aj fused protein, has been developed and should be rigorously assessed for the ecological risks on the natural enemy. Laboratory experiments were carried out to study the effects of this Bt maize on nontarget predator H. axyridis via bitrophic interaction of adult H. axyridis feeding on Bt maize pollen and tritrophic interaction of H. axyridis consuming the lepidopteran prey. Spodoptera exigua (Hübner) neonate larvae were used to transfer Bt protein because they could survive after ingesting transgenic cry1Ab/cry2Aj maize kernels in the previous study. ELISA bioassays confirmed that the Bt protein could be transferred, but diluted through Bt maize-prey-predator. Life history parameters such as survival, development, weight, fecundity, and egg hatching rate were not significantly different when H. axyridis consumed prey that had been reared on Bt maize compared with prey reared on a nontransformed parental control. Furthermore, feeding directly on Bt maize pollen also had no detrimental effects on fitness, survival, and weight of female and male adults. In conclusion, our results indicate that transgenic cry1Ab/cry2Aj maize poses no ecological risks on the nontarget predator H. axyridis.
[Mh] Termos MeSH primário: Proteínas de Bactérias
Coleópteros/efeitos dos fármacos
Endotoxinas
Cadeia Alimentar
Proteínas Hemolisinas
Estágios do Ciclo de Vida/efeitos dos fármacos
Spodoptera
[Mh] Termos MeSH secundário: Animais
Proteínas de Bactérias/análise
Coleópteros/química
Endotoxinas/análise
Feminino
Proteínas Hemolisinas/análise
Larva/química
Masculino
Plantas Geneticamente Modificadas/química
Pólen
Reprodução/efeitos dos fármacos
Spodoptera/química
Zea mays/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Endotoxins); 0 (Hemolysin Proteins); 0 (insecticidal crystal protein, Bacillus Thuringiensis)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171126
[Lr] Data última revisão:
171126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171006
[St] Status:MEDLINE
[do] DOI:10.1093/ee/nvx113


  9 / 10706 MEDLINE  
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[PMID]:28911869
[Au] Autor:Li J; Lam WW; Lai TW; Au SW
[Ad] Endereço:Center for Protein Science and Crystallography, School of Life Sciences, The Chinese University of Hong Kong, Hong Kong, China.
[Ti] Título:Degradation of nuclear Ubc9 induced by listeriolysin O is dependent on K efflux.
[So] Source:Biochem Biophys Res Commun;493(2):1115-1121, 2017 Nov 18.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Listeriolysin O (LLO) is a pore-forming toxin produced by L. monocytogenes, and is belonged to a protein family of cholesterol-dependent cytolysins (CDCs). Previous studies have demonstrated that LLO triggers Ubc9 degradation and disrupts host SUMOylation to facilitate bacterial infection. However, the underlying mechanism of Ubc9 degradation is unclear. Here we show that LLO-induced down-regulation of Ubc9 is independent of Ubc9-SUMO interaction, however, it may involve phosphorylation signaling. Additionally, LLO exerts its effects primarily on nuclear Ubc9 and this process is mediated by K efflux. Interestingly, for intracellular CDCs such as pneumolysin and suilysin, blockage of K efflux enhances degradation of nuclear Ubc9, suggesting that extracellular and intracellular pathogens may exploit different mechanisms to modulate host SUMOylation system. Furthermore, up-regulation of SUMOylation by stable expression of SUMO-1 or SUMO-2 shows a delay in membrane perforation by LLO, indicating that SUMO modification of host proteins may act at the frontline for the defense response against LLO. Taken together, our study provides insights to the understanding of host-pathogen interactions.
[Mh] Termos MeSH primário: Toxinas Bacterianas/metabolismo
Proteínas de Choque Térmico/metabolismo
Proteínas Hemolisinas/metabolismo
Listeria monocytogenes/fisiologia
Listeriose/metabolismo
Potássio/metabolismo
Proteólise
Enzimas de Conjugação de Ubiquitina/metabolismo
[Mh] Termos MeSH secundário: Cátions Monovalentes/metabolismo
Células HeLa
Interações Hospedeiro-Patógeno
Seres Humanos
Listeriose/microbiologia
Fosforilação
Sumoilação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Toxins); 0 (Cations, Monovalent); 0 (Heat-Shock Proteins); 0 (Hemolysin Proteins); 72270-41-8 (hlyA protein, Listeria monocytogenes); EC 2.3.2.23 (Ubiquitin-Conjugating Enzymes); EC 6.3.2.- (ubiquitin-conjugating enzyme UBC9); RWP5GA015D (Potassium)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170916
[St] Status:MEDLINE


  10 / 10706 MEDLINE  
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[PMID]:28832671
[Au] Autor:Reboud E; Bouillot S; Patot S; Béganton B; Attrée I; Huber P
[Ad] Endereço:Université Grenoble Alpes, CNRS ERL5261, CEA BIG-BCI, INSERM UMR1036, Grenoble, France.
[Ti] Título:Pseudomonas aeruginosa ExlA and Serratia marcescens ShlA trigger cadherin cleavage by promoting calcium influx and ADAM10 activation.
[So] Source:PLoS Pathog;13(8):e1006579, 2017 Aug.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Pore-forming toxins are potent virulence factors secreted by a large array of bacteria. Here, we deciphered the action of ExlA from Pseudomonas aeruginosa and ShlA from Serratia marcescens on host cell-cell junctions. ExlA and ShlA are two members of a unique family of pore-forming toxins secreted by a two-component secretion system. Bacteria secreting either toxin induced an ExlA- or ShlA-dependent rapid cleavage of E-cadherin and VE-cadherin in epithelial and endothelial cells, respectively. Cadherin proteolysis was executed by ADAM10, a host cell transmembrane metalloprotease. ADAM10 activation is controlled in the host cell by cytosolic Ca2+ concentration. We show that Ca2+ influx, induced by ExlA or ShlA pore formation in the plasma membrane, triggered ADAM10 activation, thereby leading to cadherin cleavage. Our data suggest that ADAM10 is not a cellular receptor for ExlA and ShlA, further confirming that ADAM10 activation occurred via Ca2+ signalling. In conclusion, ExlA- and ShlA-secreting bacteria subvert a regulation mechanism of ADAM10 to activate cadherin shedding, inducing intercellular junction rupture, cell rounding and loss of tissue barrier integrity.
[Mh] Termos MeSH primário: Proteína ADAM10/metabolismo
Proteínas de Bactérias/metabolismo
Caderinas/metabolismo
Infecções por Bactérias Gram-Negativas/metabolismo
Proteínas Hemolisinas/metabolismo
[Mh] Termos MeSH secundário: Animais
Toxinas Bacterianas/metabolismo
Western Blotting
Cálcio/metabolismo
Ativação Enzimática
Feminino
Seres Humanos
Camundongos
Camundongos Endogâmicos BALB C
Microscopia Confocal
Pseudomonas aeruginosa/patogenicidade
Serratia marcescens/patogenicidade
Virulência/fisiologia
Fatores de Virulência/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Bacterial Toxins); 0 (Cadherins); 0 (Hemolysin Proteins); 0 (ShlA protein, Serratia marcescens); 0 (Virulence Factors); EC 3.4.24.81 (ADAM10 Protein); SY7Q814VUP (Calcium)
[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:170824
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006579



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