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Pesquisa : B03.353.750.737.500.400 [Categoria DeCS]
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  1 / 3924 MEDLINE  
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[PMID]:29220366
[Au] Autor:Suzuki C; Aoki-Yoshida A; Aoki R; Sasaki K; Takayama Y; Mizumachi K
[Ad] Endereço:Institute of Livestock and Grassland Science, National Agriculture and Food Research Organization (NARO), Tsukuba, Ibaraki, Japan.
[Ti] Título:The distinct effects of orally administered Lactobacillus rhamnosus GG and Lactococcus lactis subsp. lactis C59 on gene expression in the murine small intestine.
[So] Source:PLoS One;12(12):e0188985, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The molecular mechanisms of strain-specific probiotic effects and the impact of the oral administration of probiotic strains on the host's gene expression are not yet well understood. The aim of this study was to investigate the strain-specific effects of probiotic strain intake on gene expression in the murine small intestine. Two distinct strains of lactic acid bacteria, Lactobacillus rhamnosus GG (GG) and Lactococcus lactis subsp. lactis C59 (C59), were orally administered to BALB/c mice, daily for 2 weeks. The total RNA was isolated from the upper (including the duodenum) and lower (the terminal ileum) small intestine, and gene expression was assessed by microarray analysis. The data revealed (1) oral administration of C59 and GG markedly down-regulated the expression of genes encoding fibrinogen subunits and plasminogen in the upper small intestine; (2) administration of more than 1 × 107 CFU/day of GG changed the gene expression of the host ileum. (3) strain- and dose-related effects on various GO biological processes; and (4) enrichment for B cell-related Gene Ontology terms among up-regulated genes in the terminal ileum of mice administered the 1 × 109 CFU/day of GG. The distinct effects of GG and C59 on gene expression in the intact small intestine provide clues to understand how the health beneficial effects of specific strains of probiotic bacteria are mediated by interactions with intestinal cells.
[Mh] Termos MeSH primário: Expressão Gênica
Intestino Delgado/metabolismo
Lactobacillus rhamnosus
Lactococcus lactis
[Mh] Termos MeSH secundário: Administração Oral
Animais
Masculino
Camundongos
Camundongos Endogâmicos BALB C
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180104
[Lr] Data última revisão:
180104
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171209
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0188985


  2 / 3924 MEDLINE  
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[PMID]:28960943
[Au] Autor:Monjas L; Swier LJYM; Setyawati I; Slotboom DJ; Hirsch AKH
[Ad] Endereço:Stratingh Institute for Chemistry, University of Groningen, Nijenborgh 7, 9747, AG, Groningen, The Netherlands.
[Ti] Título:Dynamic Combinatorial Chemistry to Identify Binders of ThiT, an S-Component of the Energy-Coupling Factor Transporter for Thiamine.
[So] Source:ChemMedChem;12(20):1693-1696, 2017 Oct 20.
[Is] ISSN:1860-7187
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:We applied dynamic combinatorial chemistry (DCC) to identify ligands of ThiT, the S-component of the energy-coupling factor (ECF) transporter for thiamine in Lactococcus lactis. We used a pre-equilibrated dynamic combinatorial library (DCL) and saturation-transfer difference (STD) NMR spectroscopy to identify ligands of ThiT. This is the first report in which DCC is used for fragment growing to an ill-defined pocket, and one of the first reports for its application with an integral membrane protein as target.
[Mh] Termos MeSH primário: Tiamina/metabolismo
[Mh] Termos MeSH secundário: Transportadores de Cassetes de Ligação de ATP/metabolismo
Proteínas de Bactérias/metabolismo
Transporte Biológico
Proteínas de Transporte
Técnicas de Química Combinatória
Desenho de Drogas
Lactococcus lactis
Modelos Moleculares
Estrutura Molecular
Subunidades Proteicas
Bibliotecas de Moléculas Pequenas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Carrier Proteins); 0 (Protein Subunits); 0 (Small Molecule Libraries); X66NSO3N35 (Thiamine)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171106
[Lr] Data última revisão:
171106
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170930
[St] Status:MEDLINE
[do] DOI:10.1002/cmdc.201700440


  3 / 3924 MEDLINE  
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[PMID]:28873396
[Au] Autor:Camperio C; Armas F; Biasibetti E; Frassanito P; Giovannelli C; Spuria L; D'Agostino C; Tait S; Capucchio MT; Marianelli C
[Ad] Endereço:Department of Food Safety and Veterinary Public Health, Istituto Superiore di Sanità, Rome, Italy.
[Ti] Título:A mouse mastitis model to study the effects of the intramammary infusion of a food-grade Lactococcus lactis strain.
[So] Source:PLoS One;12(9):e0184218, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lactococcus lactis is one of the most important microorganisms in the dairy industry and has "generally recognized as safe" (GRAS) status. L. lactis belongs to the group of lactic acid bacteria (LAB) and is encountered in a wide range of environments. Recently, the use of the intramammary infusion of a live culture of LAB has been investigated as a new antibiotic alternative for treating mastitis in dairy ruminants. Controversial results are described in literature regarding its efficacy and safety. In this study we conducted in-depth investigation of the mammary gland immune response induced by intramammary inoculum of a live culture of L. lactis LMG 7930 using the mouse mastitis model. Overnight cultures either of L. lactis (≈ 107 CFU) or of the mastitis pathogens Staphylococcus chromogenes (≈ 105 CFU) or S. aureus (≈ 102 CFU/ml) were injected into the mouse inguinal glands. A double injection, consisting of S. chromogenes first and then L. lactis, was also investigated. Bacterial recovery from the gland and inflammatory cell infiltration were assessed. L. lactis-treated and control glands were analysed for proinflammatory cytokine production. Microbiological results showed that L. lactis was able to survive in the mammary gland 24 h post infection, as were the mastitis pathogens S. chromogenes and S. aureus. L. lactis reduced S. chromogenes survival in the glands and increased its own survival ability by coexisting with the pathogen. Histology showed that L. lactis-treated glands presented variable histological features, ranging from undamaged tissue with no inflammatory cell infiltrate to severe PMN infiltrate with focal areas of tissue damage. S. aureus-treated glands showed the most severe histological grade of inflammation despite the fact that the inoculum size was the smallest. In contrast, most S. chromogenes-treated glands showed normal structures with no infiltration or lesions. Significant increases in IL-1ß and TNF-α levels were also found in L. lactis-inoculated glands. The above findings seem to suggest that food-grade L. lactis at a high-inoculum dose such as an overnight culture may elicit a suppurative inflammatory response in the mammary gland, thus becoming a potential mastitis-causing pathogen. Because of the unpredictable potential of L. lactis in acting as a potential mastitis pathogen, this organism cannot be considered a safe treatment for bovine mastitis.
[Mh] Termos MeSH primário: Lactococcus lactis/fisiologia
Glândulas Mamárias Animais/microbiologia
Glândulas Mamárias Animais/patologia
Mastite/microbiologia
[Mh] Termos MeSH secundário: Animais
Citocinas/biossíntese
Modelos Animais de Doenças
Feminino
Mediadores da Inflamação/metabolismo
Mastite/patologia
Camundongos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytokines); 0 (Inflammation Mediators)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170906
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184218


  4 / 3924 MEDLINE  
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[PMID]:28802003
[Au] Autor:Gandini C; Tarraran L; Kalemasi D; Pessione E; Mazzoli R
[Ad] Endereço:Department of Life Sciences and Systems Biology, Structural and Functional Biochemistry, Laboratory of Proteomics and Metabolic Engineering of Prokaryotes, University of Turin, Torino, Italy.
[Ti] Título:Recombinant Lactococcus lactis for efficient conversion of cellodextrins into L-lactic acid.
[So] Source:Biotechnol Bioeng;114(12):2807-2817, 2017 Dec.
[Is] ISSN:1097-0290
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lactic acid bacteria (LAB) are among the most interesting organisms for industrial processes with a long history of application as food starters and biocontrol agents, and an underexploited potential for biorefineries converting biomass into high-value compounds. Lactic acid (LA), their main fermentation product, is among the most requested chemicals owing to its broad range of applications. Notably, LA polymers, that is, polylactides, have high potential as biodegradable substitutes of fossil-derived plastics. However, LA production by LAB fermentation is currently too expensive for polylactide to be cost-competitive with traditional plastics. LAB have complex nutritional requirements and cannot ferment inexpensive substrates such as cellulose. Metabolic engineering could help reduce such nutritional requirements and enable LAB to directly ferment low-cost polysaccharides. Here, we engineered a Lactococcus lactis strain which constitutively secretes a ß-glucosidase and an endoglucanase. The recombinant strain can grow on cellooligosaccharides up to at least cellooctaose and efficiently metabolizes them to L-LA in single-step fermentation. This is the first report of a LAB able to directly metabolize cellooligosaccharides longer that cellohexaose and a significant step toward cost-sustainable consolidated bioprocessing of cellulose into optically pure LA.
[Mh] Termos MeSH primário: Celulose/análogos & derivados
Dextrinas/metabolismo
Melhoramento Genético/métodos
Ácido Láctico/biossíntese
Lactococcus lactis/genética
Lactococcus lactis/metabolismo
Proteínas Recombinantes/metabolismo
Recombinação Genética/genética
[Mh] Termos MeSH secundário: Celulose/genética
Celulose/metabolismo
Dextrinas/genética
Ácido Láctico/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Dextrins); 0 (Recombinant Proteins); 33X04XA5AT (Lactic Acid); 9004-34-6 (Cellulose); 9061-30-7 (cellodextrin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170813
[St] Status:MEDLINE
[do] DOI:10.1002/bit.26400


  5 / 3924 MEDLINE  
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[PMID]:28800826
[Au] Autor:Siroli L; Patrignani F; Serrazanetti DI; Vernocchi P; Del Chierico F; Russo A; Torriani S; Putignani L; Gardini F; Lanciotti R
[Ad] Endereço:Department of Agricultural and Food Sciences, Alma Mater Studiorum, University of Bologna, Campus of Food Science, Piazza Goidanich 60, 47521 Cesena, Italy.
[Ti] Título:Effect of thyme essential oil and Lactococcus lactis CBM21 on the microbiota composition and quality of minimally processed lamb's lettuce.
[So] Source:Food Microbiol;68:61-70, 2017 Dec.
[Is] ISSN:1095-9998
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The main aim of this work was to evaluate, at pilot scale in an industrial environment, the effects of the biocontrol agent Lactococcus lactis CBM21 and thyme essential oil compared to chlorine, used in the washing step of fresh-cut lamb's lettuce, on the microbiota and its changes in relation to the time of storage. The modification of the microbial population was studied through pyrosequencing in addition to the traditional plate counts. In addition, the volatile molecule and sensory profiles were evaluated during the storage. The results showed no significant differences in terms of total aerobic mesophilic cell loads in relation to the washing solution adopted. However, the pyrosequencing data permitted to identify the genera and species able to dominate the spoilage associations over storage in relation to the treatment applied. Also, the analyses of the volatile molecule profiles of the samples during storage allowed the identification of specific molecules as markers of the spoilage for each different treatment. The sensory analyses after 3 and 5 days of storage showed the preference of the panelists for samples washed with the combination thyme EO and the biocontrol agent. These samples were preferred for attributes such as flavor, acceptability and overall quality. These results highlighted the effect of the innovative washing solutions on the quality of lettuce through the shift of microbiota towards genera and species with lower potential in decreasing the sensory properties of the product.
[Mh] Termos MeSH primário: Bactérias/efeitos dos fármacos
Lactococcus lactis/fisiologia
Alface/microbiologia
Óleos Voláteis/farmacologia
Extratos Vegetais/farmacologia
Thymus (Planta)/química
Verduras/microbiologia
[Mh] Termos MeSH secundário: Bactérias/classificação
Bactérias/crescimento & desenvolvimento
Bactérias/isolamento & purificação
Biodiversidade
Contaminação de Alimentos/prevenção & controle
Óleos Voláteis/isolamento & purificação
Extratos Vegetais/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Oils, Volatile); 0 (Plant Extracts)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170813
[St] Status:MEDLINE


  6 / 3924 MEDLINE  
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[PMID]:28786717
[Au] Autor:Zhou LH; Wang YL; Qiu M; Shi Q; Sun LJ; Liao JM; Xu DF; Liu Y; Fang ZJ; Gooneratne R
[Ad] Endereço:1 College of Food Science and Technology, Guangdong Provincial Key Laboratory of Aquatic Product Processing and Safety, Key Laboratory of Advanced Processing of Aquatic Products of Guangdong Higher Education Institution, Guangdong Ocean University, Zhanjiang 524088, People's Republic of China.
[Ti] Título:Analysis of T-2 Toxin Removal Factors in a Lactococcus Fermentation System.
[So] Source:J Food Prot;80(9):1471-1477, 2017 Sep.
[Is] ISSN:1944-9097
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The objective of this work was to determine the bacterial strains and factors that most efficiently degrade T-2 toxin in foods or animal feed. To determine the most efficient strain and optimal incubation times for degradation of T-2, the rate of T-2 removal by three lactic acid bacteria strains was quantified by liquid chromatography plus tandem mass spectrometry after incubation in de Man Rogosa Sharpe broth with 50 ng mL T-2 at 37°C for 96 h. Various components of the most efficient degradation strain fermentation systems were extracted, and the ability to remove T-2 was assayed. Lactococcus lactis CAMT22361 was the most efficient degradation strain for removing T-2. Yeast extract powder interfered with L. lactis CAMT22361 in the degradation process. T-2 toxin was removed by various components of the L. lactis CAMT22361 cells in the following order: nonprotein material of the extracellular fraction > protein in the extracellular fraction > whole cell ≈ cell wall > cell intracellular matrix fluid. T-2 removal rates were 54.08% ± 0.79%, 43.65% ± 0.84%, 43.09% ± 0.87%, 41.98% ± 0.8%, and 23.45% ± 0.66%, respectively. The nonprotein fraction in the extracellular fluid was most likely the key component in L. lactis CAMT22361 and hence would be the most desirable cellular component to be used to remove T-2 from food or feed.
[Mh] Termos MeSH primário: Fermentação
Manipulação de Alimentos/métodos
Toxina T-2/análise
[Mh] Termos MeSH secundário: Animais
Lactococcus lactis
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
I3FL5NM3MO (T-2 Toxin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170809
[St] Status:MEDLINE
[do] DOI:10.4315/0362-028X.JFP-17-051


  7 / 3924 MEDLINE  
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[PMID]:28675292
[Au] Autor:Lagedroste M; Smits SHJ; Schmitt L
[Ad] Endereço:Institute of Biochemistry, Heinrich-Heine-University Duesseldorf , Universitaetsstrasse 1, 40225 Duesseldorf, Germany.
[Ti] Título:Substrate Specificity of the Secreted Nisin Leader Peptidase NisP.
[So] Source:Biochemistry;56(30):4005-4014, 2017 Aug 01.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nisin (NisA) is an antimicrobial peptide produced by Lactococcus lactis and belongs to the class of lanthipeptides, more specifically to the class of lantibiotics. They are ribosomally synthesized as a precursor peptide and are comprised of an N-terminal leader peptide and a C-terminal core peptide. The core peptide is post-translationally modified and contains dehydrated amino acids in addition to five (methyl)-lanthionine rings, which are crucial for its activity. The leader peptide serves as a signal sequence and ensures that NisA remains inactive but secretion-competent within the cell. After translocation into the extracellular space, the leader peptide is cleaved by the leader peptidase NisP, resulting in active nisin. NisP is an extracellular subtilisin-like serine protease, which recognizes the cleavage site GASPR|IT located at the C-terminal end of the leader peptide. Here, we present the biochemical characterization of secreted and purified NisP (NisP ) with its natural substrate, the fully modified NisA (mNisA). Furthermore, we determined the kinetic parameters of NisP in the presence of NisA containing different modification states. Additionally, in vitro data revealed that NisP can efficiently cleave the leader peptide of mNisA. However, it is strictly dependent on the modification state of the core peptide. Thus, NisP has a sequence-based cleavage activity, and the presence of at least one lanthionine ring is crucial for optimal substrate recognition and subsequent cleavage.
[Mh] Termos MeSH primário: Antibacterianos/metabolismo
Proteínas de Bactérias/metabolismo
Lactococcus lactis/metabolismo
Proteínas de Membrana/metabolismo
Nisina/metabolismo
Processamento de Proteína Pós-Traducional
Subtilisinas/metabolismo
[Mh] Termos MeSH secundário: Alanina/análogos & derivados
Alanina/química
Alanina/metabolismo
Motivos de Aminoácidos
Substituição de Aminoácidos
Antibacterianos/química
Proteínas de Bactérias/genética
Proteínas de Bactérias/secreção
Biocatálise
Ativação Enzimática
Lactococcus lactis/enzimologia
Proteínas de Membrana/genética
Proteínas de Membrana/secreção
Metilação
Peso Molecular
Mutagênese Sítio-Dirigida
Mutação
Nisina/química
Nisina/genética
Nisina/secreção
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Fragmentos de Peptídeos/secreção
Sinais Direcionadores de Proteínas
Proteólise
Proteínas Recombinantes/metabolismo
Especificidade por Substrato
Subtilisinas/genética
Subtilisinas/secreção
Sulfetos/química
Sulfetos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Bacterial Proteins); 0 (Membrane Proteins); 0 (Peptide Fragments); 0 (Protein Sorting Signals); 0 (Recombinant Proteins); 0 (Sulfides); 1414-45-5 (Nisin); 42849-28-5 (beta-methyllanthionine); EC 3.4.21.- (NisP protein, Lactococcus lactis); EC 3.4.21.- (Subtilisins); JO78O46X3K (lanthionine); OF5P57N2ZX (Alanine)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170811
[Lr] Data última revisão:
170811
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170705
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00524


  8 / 3924 MEDLINE  
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[PMID]:28583849
[Au] Autor:García-Cayuela T; Requena T; Martínez-Cuesta MC; Peláez C
[Ad] Endereço:Departamento de Biotecnología y Microbiología de Alimentos, Instituto de Investigación en Ciencias de la Alimentación CIAL (CSIC), Madrid, Spain. Electronic address: tomas.garcia@csic.es.
[Ti] Título:Rapid detection of Lactococcuslactis isolates producing the lantibiotics nisin, lacticin 481 and lacticin 3147 using MALDI-TOF MS.
[So] Source:J Microbiol Methods;139:138-142, 2017 Aug.
[Is] ISSN:1872-8359
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The aim of the study was to evaluate the potential use of Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry (MALDI-TOF MS) for fast and reliable detection of strains producing the lantibiotics nisin, lacticin 481 and lacticin 3147 in a large collection of lactococci. A total of one hundred lactococcal isolates from traditional ewe's and goat's raw milk cheeses were identified to the species level as Lactococcuslactis by MALDI-TOF MS based on comparison with lactococcal entries in the BioTyper database. Mass spectra in the range 2000-4000Da of the identified isolates were compared to reference spectra of three lactococcal strains producing lacticin 481 (IFPL 330), lacticin 3147 (IFPL 105) and nisin (IFPL 503). Only eight isolates had mass spectra with peaks that could be unequivocally identified as lacticin 481 (2900.47Da) or nisin (3330.31Da). None of the assayed isolates matched the mass spectra corresponding to the two-peptide lacticin 3147 (2847.97 and 3306.29Da). The results obtained by MALDI-TOF MS were genetically validated by amplification of the corresponding structural gene coding for lacticin 481, nisin and lacticin 3147. MALDI-TOF MS can be used as a fast and reliable technique to screen a large number of lactococcal isolates for the ability to produce the lantibiotics nisin, lacticin 481 and lacticin 3147.
[Mh] Termos MeSH primário: Bacteriocinas/análise
Lactococcus lactis/isolamento & purificação
Lactococcus lactis/metabolismo
Leite/microbiologia
Nisina/análise
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz/métodos
[Mh] Termos MeSH secundário: Animais
Técnicas de Tipagem Bacteriana
Bacteriocinas/biossíntese
Cabras
Seres Humanos
Nisina/biossíntese
Ovinos
Fatores de Tempo
[Pt] Tipo de publicação:EVALUATION STUDIES; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacteriocins); 0 (nisin A); 136959-47-2 (lacticin 481); 1414-45-5 (Nisin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170607
[St] Status:MEDLINE


  9 / 3924 MEDLINE  
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[PMID]:28569168
[Au] Autor:Singh SK; Roeffen W; Mistarz UH; Chourasia BK; Yang F; Rand KD; Sauerwein RW; Theisen M
[Ad] Endereço:Department for Congenital Disorders, Statens Serum Institut, Artillerivej 5, 2300, Copenhagen, Denmark.
[Ti] Título:Construct design, production, and characterization of Plasmodium falciparum 48/45 R0.6C subunit protein produced in Lactococcus lactis as candidate vaccine.
[So] Source:Microb Cell Fact;16(1):97, 2017 May 31.
[Is] ISSN:1475-2859
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The sexual stages of Plasmodium falciparum are responsible for the spread of the parasite in malaria endemic areas. The cysteine-rich Pfs48/45 protein, exposed on the surface of sexual stages, is one of the most advanced antigens for inclusion into a vaccine that will block transmission. However, clinical Pfs48/45 sub-unit vaccine development has been hampered by the inability to produce high yields of recombinant protein as the native structure is required for the induction of functional transmission-blocking (TB) antibodies. We have investigated a downstream purification process of a sub-unit (R0.6C) fragment representing the C-terminal 6-Cys domain of Pfs48/45 (6C) genetically fused to the R0 region (R0) of asexual stage Glutamate Rich Protein expressed in Lactococcus lactis. RESULTS: A series of R0.6C fusion proteins containing features, which aim to increase expression levels or to facilitate protein purification, were evaluated at small scale. None of these modifications affected the overall yield of recombinant protein. Consequently, R0.6C with a C-terminal his tag was used for upstream and downstream process development. A simple work-flow was developed consisting of batch fermentation followed by two purification steps. As such, the recombinant protein was purified to homogeneity. The composition of the final product was verified by HPLC, mass spectrometry, SDS-PAGE and Western blotting with conformation dependent antibodies against Pfs48/45. The recombinant protein induced high levels of functional TB antibodies in rats. CONCLUSIONS: The established production and purification process of the R0.6C fusion protein provide a strong basis for further clinical development of this candidate transmission blocking malaria vaccine.
[Mh] Termos MeSH primário: Vacinas Bacterianas/biossíntese
Vacinas Bacterianas/imunologia
Imunogenicidade da Vacina/imunologia
Lactococcus lactis/metabolismo
Plasmodium falciparum/metabolismo
Proteínas Recombinantes de Fusão/biossíntese
[Mh] Termos MeSH secundário: Animais
Vacinas Bacterianas/isolamento & purificação
Reatores Biológicos
Lactococcus lactis/genética
Plasmodium falciparum/química
Plasmodium falciparum/imunologia
Subunidades Proteicas/biossíntese
Subunidades Proteicas/química
Subunidades Proteicas/isolamento & purificação
Ratos
Proteínas Recombinantes de Fusão/imunologia
Proteínas Recombinantes de Fusão/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Vaccines); 0 (Protein Subunits); 0 (Recombinant Fusion Proteins)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171108
[Lr] Data última revisão:
171108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170602
[St] Status:MEDLINE
[do] DOI:10.1186/s12934-017-0710-0


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[PMID]:28537141
[Au] Autor:Taguchi Y; Saburi W; Imai R; Mori H
[Ad] Endereço:a Research Faculty of Agriculture , Hokkaido University , Sapporo , Japan.
[Ti] Título:Evaluation of acceptor selectivity of Lactococcus lactis ssp. lactis trehalose 6-phosphate phosphorylase in the reverse phosphorolysis and synthesis of a new sugar phosphate.
[So] Source:Biosci Biotechnol Biochem;81(8):1512-1519, 2017 Aug.
[Is] ISSN:1347-6947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Trehalose 6-phosphate phosphorylase (TrePP), a member of glycoside hydrolase family 65, catalyzes the reversible phosphorolysis of trehalose 6-phosphate (Tre6P) with inversion of the anomeric configuration to produce ß-d-glucose 1-phosphate (ß-Glc1P) and d-glucose 6-phosphate (Glc6P). TrePP in Lactococcus lactis ssp. lactis (LlTrePP) is, alongside the phosphotransferase system, involved in the metabolism of trehalose. In this study, recombinant LlTrePP was produced and characterized. It showed its highest reverse phosphorolytic activity at pH 4.8 and 40°C, and was stable in the pH range 5.0-8.0 and at up to 30°C. Kinetic analyses indicated that reverse phosphorolysis of Tre6P proceeded through a sequential bi bi mechanism involving the formation of a ternary complex of the enzyme, ß-Glc1P, and Glc6P. Suitable acceptor substrates were Glc6P, and, at a low level, d-mannose 6-phosphate (Man6P). From ß-Glc1P and Man6P, a novel sugar phosphate, α-d-Glcp-(1↔1)-α-d-Manp6P, was synthesized with 51% yield.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Glucosiltransferases/metabolismo
Lactococcus lactis/enzimologia
Fosfatos Açúcares/biossíntese
Trealose/análogos & derivados
Trealose/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Clonagem Molecular
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Glucofosfatos/metabolismo
Glucosiltransferases/genética
Concentração de Íons de Hidrogênio
Hidrólise
Cinética
Lactococcus lactis/química
Manosefosfatos/metabolismo
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Especificidade por Substrato
Fosfatos Açúcares/metabolismo
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Glucosephosphates); 0 (Mannosephosphates); 0 (Recombinant Proteins); 0 (Sugar Phosphates); 3672-15-9 (mannose-6-phosphate); 4484-88-2 (trehalose-6-phosphate); 54482-78-9 (2-deoxyglucose-1-phosphate); B8WCK70T7I (Trehalose); EC 2.4.1.- (Glucosyltransferases); EC 2.4.1.- (trehalose-6-phosphate phosphorylase)
[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:170525
[St] Status:MEDLINE
[do] DOI:10.1080/09168451.2017.1329620



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