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[PMID]:28736824
[Au] Autor:Wei Y; Wahome N; VanSlyke G; Whitaker N; Kumar P; Barta ML; Picking WL; Volkin DB; Mantis NJ; Middaugh CR
[Ad] Endereço:Macromolecule and Vaccine Stabilization Center, Department of Pharmaceutical Chemistry, University of Kansas, Lawrence, Kansas, 66047.
[Ti] Título:Evaluation of lumazine synthase from Bacillus anthracis as a presentation platform for polyvalent antigen display.
[So] Source:Protein Sci;26(10):2059-2072, 2017 Oct.
[Is] ISSN:1469-896X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Polyvalent antigen display is an effective strategy to enhance the immunogenicity of subunit vaccines by clustering them in an array-like manner on a scaffold system. This strategy results in a higher local density of antigens, increased high avidity interactions with B cells and other antigen presenting cells, and therefore a more effective presentation of vaccine antigens. In this study, we used lumazine synthase (LS), an icosahedral symmetry capsid derived from Bacillus anthracis, as a scaffold to present 60 copies of a linear B cell epitope (PB10) from the ricin toxin fused to the C terminus of LS via four different linkers. We then investigated the effects of linker length, linker rigidity and formaldehyde crosslinking on the protein assembly, conformational integrity, thermal stability, in vitro antibody binding, and immunogenicity in mice. Fusion of the PB10 peptide onto LS, with varying linker lengths, did not affect protein assembly, thermal stability or exposure of the epitope, but had a minor impact on protein conformation. Formaldehyde crosslinking considerably improved protein thermal stability with only minor impact on protein conformation. All LS_PB10 constructs, when administered to mice by injection without adjuvant, elicited measurable anti-ricin serum IgG titers, although the titers were not sufficient to confer protection against a 10× lethal dose ricin challenge. This work sheds light on the biophysical properties, immunogenicity and potential feasibility of LS from B. anthracis as a scaffold system for polyvalent antigen display.
[Mh] Termos MeSH primário: Vacinas contra Antraz
Antígenos de Bactérias
Bacillus anthracis
Epitopos de Linfócito B
Complexos Multienzimáticos
Vacinas de Subunidades
[Mh] Termos MeSH secundário: Animais
Vacinas contra Antraz/química
Vacinas contra Antraz/genética
Vacinas contra Antraz/imunologia
Vacinas contra Antraz/metabolismo
Anticorpos Antibacterianos/sangue
Anticorpos Antibacterianos/imunologia
Antígenos de Bactérias/química
Antígenos de Bactérias/genética
Antígenos de Bactérias/imunologia
Antígenos de Bactérias/metabolismo
Bacillus anthracis/enzimologia
Bacillus anthracis/imunologia
Epitopos de Linfócito B/química
Epitopos de Linfócito B/genética
Epitopos de Linfócito B/imunologia
Epitopos de Linfócito B/metabolismo
Feminino
Imunoglobulina G/sangue
Imunoglobulina G/imunologia
Camundongos
Modelos Moleculares
Complexos Multienzimáticos/química
Complexos Multienzimáticos/genética
Complexos Multienzimáticos/imunologia
Complexos Multienzimáticos/metabolismo
Estabilidade Proteica
Ricina/química
Ricina/genética
Ricina/imunologia
Ricina/metabolismo
Vacinas de Subunidades/química
Vacinas de Subunidades/genética
Vacinas de Subunidades/imunologia
Vacinas de Subunidades/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anthrax Vaccines); 0 (Antibodies, Bacterial); 0 (Antigens, Bacterial); 0 (Epitopes, B-Lymphocyte); 0 (Immunoglobulin G); 0 (Multienzyme Complexes); 0 (Vaccines, Subunit); 89287-46-7 (6,7-dimethyl-8-ribityllumazine synthase); 9009-86-3 (Ricin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170725
[St] Status:MEDLINE
[do] DOI:10.1002/pro.3243


  2 / 2697 MEDLINE  
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[PMID]:28718923
[Au] Autor:Bazzoli A; Vance DJ; Rudolph MJ; Rong Y; Angalakurthi SK; Toth RT; Middaugh CR; Volkin DB; Weis DD; Karanicolas J; Mantis NJ
[Ad] Endereço:Center for Computational Biology, University of Kansas, Lawrence, Kansas, 66045.
[Ti] Título:Using homology modeling to interrogate binding affinity in neutralization of ricin toxin by a family of single domain antibodies.
[So] Source:Proteins;85(11):1994-2008, 2017 Nov.
[Is] ISSN:1097-0134
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In this report we investigated, within a group of closely related single domain camelid antibodies (V Hs), the relationship between binding affinity and neutralizing activity as it pertains to ricin, a fast-acting toxin and biothreat agent. The V1C7-like V Hs (V1C7, V2B9, V2E8, and V5C1) are similar in amino acid sequence, but differ in their binding affinities and toxin-neutralizing activities. Using the X-ray crystal structure of V1C7 in complex with ricin's enzymatic subunit (RTA) as a template, Rosetta-based homology modeling coupled with energetic decomposition led us to predict that a single pairwise interaction between Arg29 on V5C1 and Glu67 on RTA was responsible for the difference in ricin toxin binding affinity between V1C7, a weak neutralizer, and V5C1, a moderate neutralizer. This prediction was borne out experimentally: substitution of Arg for Gly at position 29 enhanced V1C7's binding affinity for ricin, whereas the reverse (ie, Gly for Arg at position 29) diminished V5C1's binding affinity by >10 fold. As expected, the V5C1 mutant was largely devoid of toxin-neutralizing activity (TNA). However, the TNA of the V1C7 mutant was not correspondingly improved, indicating that in the V1C7 family binding affinity alone does not account for differences in antibody function. V1C7 and V5C1, as well as their respective point mutants, recognized indistinguishable epitopes on RTA, at least at the level of sensitivity afforded by hydrogen-deuterium mass spectrometry. The results of this study have implications for engineering therapeutic antibodies because they demonstrate that even subtle differences in epitope specificity can account for important differences in antibody function.
[Mh] Termos MeSH primário: Anticorpos Neutralizantes
Mapeamento de Epitopos/métodos
Modelos Moleculares
Engenharia de Proteínas/métodos
Ricina
Anticorpos de Domínio Único
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Anticorpos Neutralizantes/química
Anticorpos Neutralizantes/metabolismo
Camelidae
Ligação Proteica
Ricina/química
Ricina/isolamento & purificação
Ricina/metabolismo
Alinhamento de Sequência
Anticorpos de Domínio Único/química
Anticorpos de Domínio Único/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Neutralizing); 0 (Single-Domain Antibodies); 9009-86-3 (Ricin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170719
[St] Status:MEDLINE
[do] DOI:10.1002/prot.25353


  3 / 2697 MEDLINE  
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[PMID]:28700745
[Au] Autor:Rong Y; Van Slyke G; Vance DJ; Westfall J; Ehrbar D; Mantis NJ
[Ad] Endereço:Division of Infectious Disease, Wadsworth Center, New York State Department of Health, Albany, New York, United States of America.
[Ti] Título:Spatial location of neutralizing and non-neutralizing B cell epitopes on domain 1 of ricin toxin's binding subunit.
[So] Source:PLoS One;12(7):e0180999, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ricin toxin's binding subunit (RTB) is a galactose-/N-acetylgalactosamine (Gal/GalNac)-specific lectin that mediates uptake and intracellular trafficking of ricin within mammalian cells. Structurally, RTB consists of two globular domains, each divided into three homologous sub-domains (α, ß, γ). In this report, we describe five new murine IgG monoclonal antibodies (mAbs) against RTB: MH3, 8A1, 8B3, LF1, and LC5. The mAbs have similar binding affinities (KD) for ricin holotoxin, but displayed a wide range of in vitro toxin-neutralizing activities. Competition ELISAs indicate that the two most potent toxin-neutralizing mAbs (MH3, 8A1), as well as one of the moderate toxin-neutralizing mAbs (LF1), recognize distinct epitopes near the low affinity Gal recognition domain in RTB subdomain 1α. Evaluated in a mouse model of systemic ricin challenge, all five mAbs afforded some benefit against intoxication, but only MH3 was protective. However, neither MH3 nor 24B11, another well-characterized mAb against RTB subdomain 1α, could passively protect mice against a mucosal (intranasal) ricin challenge. This is in contrast to SylH3, a previously characterized mAb directed against an epitope near RTB's high affinity Gal/GalNac recognition element in sub-domain 2γ, which protected animals against systemic and mucosal ricin exposure. SylH3 was significantly more effective than MH3 and 24B11 at blocking ricin attachment to host cell receptors, suggesting that mucosal immunity to ricin is best imparted by antibodies that target RTB's high affinity Gal/GalNac recognition element in subdomain 2γ, not the low affinity Gal recognition domain in subdomain 1α.
[Mh] Termos MeSH primário: Anticorpos Neutralizantes/imunologia
Epitopos de Linfócito B/química
Ricina/química
Ricina/imunologia
[Mh] Termos MeSH secundário: Animais
Anticorpos Monoclonais/imunologia
Cercopithecus aethiops
Ensaio de Imunoadsorção Enzimática
Mapeamento de Epitopos/métodos
Epitopos de Linfócito B/imunologia
Feminino
Camundongos
Camundongos Endogâmicos BALB C
Estrutura Secundária de Proteína
Ressonância de Plasmônio de Superfície
Células Vero
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Antibodies, Neutralizing); 0 (Epitopes, B-Lymphocyte); 9009-86-3 (Ricin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170927
[Lr] Data última revisão:
170927
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170713
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0180999


  4 / 2697 MEDLINE  
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[PMID]:28398250
[Au] Autor:Li XP; Tumer NE
[Ad] Endereço:Department of Plant Biology, Rutgers, The State University of New Jersey, New Brunswick, NJ 08901, USA. xpli@aesop.rutgers.edu.
[Ti] Título:Differences in Ribosome Binding and Sarcin/Ricin Loop Depurination by Shiga and Ricin Holotoxins.
[So] Source:Toxins (Basel);9(4), 2017 Apr 11.
[Is] ISSN:2072-6651
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Both ricin and Shiga holotoxins display no ribosomal activity in their native forms and need to be activated to inhibit translation in a cell-free translation inhibition assay. This is because the ribosome binding site of the ricin A chain (RTA) is blocked by the B subunit in ricin holotoxin. However, it is not clear why Shiga toxin 1 (Stx1) or Shiga toxin 2 (Stx2) holotoxin is not active in a cell-free system. Here, we compare the ribosome binding and depurination activity of Stx1 and Stx2 holotoxins with the A1 subunits of Stx1 and Stx2 using either the ribosome or a 10-mer RNA mimic of the sarcin/ricin loop as substrates. Our results demonstrate that the active sites of Stx1 and Stx2 holotoxins are blocked by the A2 chain and the B subunit, while the ribosome binding sites are exposed to the solvent. Unlike ricin, which is enzymatically active, but cannot interact with the ribosome, Stx1 and Stx2 holotoxins are enzymatically inactive but can interact with the ribosome.
[Mh] Termos MeSH primário: Ribossomos/metabolismo
Ricina/metabolismo
Toxina Shiga I/metabolismo
Toxina Shiga II/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Shiga Toxin 1); 0 (Shiga Toxin 2); 9009-86-3 (Ricin)
[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:170412
[St] Status:MEDLINE


  5 / 2697 MEDLINE  
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[PMID]:28232091
[Au] Autor:Landi N; Pacifico S; Ragucci S; Iglesias R; Piccolella S; Amici A; Di Giuseppe AMA; Di Maro A
[Ad] Endereço:Department of Environmental, Biological and Pharmaceutical Sciences and Technologies, University of Campania "Luigi Vanvitelli", I-81100 Caserta, Italy.
[Ti] Título:Purification, characterization and cytotoxicity assessment of Ageritin: The first ribotoxin from the basidiomycete mushroom Agrocybe aegerita.
[So] Source:Biochim Biophys Acta;1861(5 Pt A):1113-1121, 2017 05.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Several species belonging to Ascomycota phylum produce extracellular ribonucleases, known as ribotoxins, which exhibit RNase activity through the cleavage of a single phosphodiester bond, located at the universally conserved sarcin/ricin loop of the large rRNA leading to inhibition of protein biosynthesis. Clarifying the structure-function relationship in ribotoxins is interesting for their use in human tumour therapy and in construction of pest resistant transgenic plants. RESULTS: The ribotoxin Ageritin has been isolated for the first time from the Basidiomycetes class. The enzyme, characterized by means of its amino acid composition, N-terminal sequence and a circular dichroism, structurally differs from Ascomycota ribotoxin prototype, although it was able, as α-sarcin, to release a specific α-fragment. However, it does not display aspecific ribonucleolytic activity. Ageritin exerts cytotoxicity and cell death promoting effects towards CNS model cell lines (SK-N-BE(2)-C, U-251 and C6), as vinblastine, a plant alkaloid used in cancer therapy. Moreover, our results indicate that Ageritin initially activates caspase-8, whereas caspase-9 cleavage was not detected, demonstrating the involvement of an extrinsic apoptotic pathway. CONCLUSIONS: Our findings show that Ageritin is the earliest diverging member of the Ascomycota ribotoxin family, suggesting that ribotoxins are more widely distributed among fungi than previously believed. GENERAL SIGNIFICANCE: Ageritin, structurally different from the widely known Ascomycota ribotoxins, with promising anti-cancer properties vs. aggressive brain tumours, has been found from the basidiomycete fungus Agrocybe aegerita. Finally, this finding highlights that the ribotoxin family has divergent members in Basidiomycota phylum, whose structural and functional characterization can give new information on ribotoxin or ribonuclease superfamilies.
[Mh] Termos MeSH primário: Agaricales/química
Agrocybe/química
Antineoplásicos/química
Antineoplásicos/farmacologia
Basidiomycota/química
Ribonucleases/química
Ribonucleases/farmacologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Apoptose/efeitos dos fármacos
Caspase 8/metabolismo
Caspase 9/metabolismo
Linhagem Celular Tumoral
Endorribonucleases/metabolismo
Proteínas Fúngicas/metabolismo
Seres Humanos
Biossíntese de Proteínas/efeitos dos fármacos
RNA Ribossômico/metabolismo
Ribossomos/química
Ribossomos/metabolismo
Ricina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Fungal Proteins); 0 (RNA, Ribosomal); 1407-48-3 (alpha-sarcin); 9009-86-3 (Ricin); EC 3.1.- (Endoribonucleases); EC 3.1.- (Ribonucleases); EC 3.4.22.- (Caspase 8); EC 3.4.22.- (Caspase 9)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170225
[St] Status:MEDLINE


  6 / 2697 MEDLINE  
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[PMID]:28192054
[Au] Autor:Bartholomew RA; Ozanich RM; Arce JS; Engelmann HE; Heredia-Langner A; Hofstad BA; Hutchison JR; Jarman K; Melville AM; Victry KD; Bruckner-Lea CJ
[Ti] Título:Evaluation of Immunoassays and General Biological Indicator Tests for Field Screening of Bacillus anthracis and Ricin.
[So] Source:Health Secur;15(1):81-96, 2017 Jan/Feb.
[Is] ISSN:2326-5108
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:There is little published data on the performance of biological indicator tests and immunoassays that could be used by first responders to determine if a suspicious powder contains a potential biothreat agent. We evaluated a range of biological indicator tests, including 3 protein tests, 2 ATP tests, 1 DNA test, and 1 FTIR spectroscopy instrument for their ability to screen suspicious powders for Bacillus anthracis (B. anthracis) spores and ricin. We also evaluated 12 immunoassays (mostly lateral flow immunoassays) for their ability to screen for B. anthracis and ricin. We used a cost-effective, statistically based test plan that allows instruments to be evaluated at performance levels ranging from 0.85 to 0.95 lower confidence bound of the probability of detection at confidence levels of 80% to 95%. We also assessed interference with 22 common suspicious powders encountered in the field. The detection reproducibility for the biological indicators was evaluated at 10 B. anthracis spores and 62.5 µg ricin, and the immunoassay detection reproducibility was evaluated at 10 spores/mL (B. anthracis) and 0.1 µg/mL (ricin). Seven out of 12 immunoassays met our most stringent criteria for B. anthracis detection, while 9 out of 12 met our most stringent test criteria for ricin detection. Most of the immunoassays also detected ricin in 3 different crude castor seed preparations. Our testing results varied across products and sample preparations, indicating the importance of reviewing performance data for specific instruments and sample types of interest for the application in order to make informed decisions regarding the selection of biodetection equipment for field use.
[Mh] Termos MeSH primário: Bacillus anthracis
Imunoensaio/métodos
Ricina
Manejo de Espécimes
[Mh] Termos MeSH secundário: Pós
Reprodutibilidade dos Testes
Esporos Bacterianos/isolamento & purificação
[Pt] Tipo de publicação:EVALUATION STUDIES; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Powders); 9009-86-3 (Ricin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170912
[Lr] Data última revisão:
170912
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170214
[St] Status:MEDLINE
[do] DOI:10.1089/hs.2016.0044


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[PMID]:28134797
[Au] Autor:Bolognesi A; Bortolotti M; Battelli MG; Polito L
[Ad] Endereço:Department of Experimental, Diagnostic and Specialty Medicine-DIMES, Alma Mater Studiorum, University of Bologna, Via San Giacomo 14, 40126 Bologna, Italy. andrea.bolognesi@unibo.it.
[Ti] Título:Hyperuricaemia, Xanthine Oxidoreductase and Ribosome-Inactivating Proteins from Plants: The Contributions of Fiorenzo Stirpe to Frontline Research.
[So] Source:Molecules;22(2), 2017 Jan 27.
[Is] ISSN:1420-3049
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:The enzymes called ribosome-inactivating proteins (RIPs) that are able to depurinate  nucleic acids and arrest vital cellular functions, including protein synthesis, are still a frontline  research field, mostly because of their promising medical applications. The contributions of Stirpe  to the development of these studies has been one of the most relevant. After a short biographical  introduction, an overview is offered of the main results obtained by his investigations during last  55 years on his main research lines: hyperuricaemia, xanthine oxidoreductase and RIPs.
[Mh] Termos MeSH primário: Hiperuricemia/tratamento farmacológico
Hiperuricemia/metabolismo
Proteínas de Plantas/farmacologia
Pesquisa
Proteínas Inativadoras de Ribossomos/farmacologia
Xantina Desidrogenase/metabolismo
[Mh] Termos MeSH secundário: Animais
Pessoas Famosas
Frutose/metabolismo
História do Século XX
Seres Humanos
Hiperuricemia/diagnóstico
Hiperuricemia/etiologia
Itália
Pesquisa/história
Ricina/farmacologia
Pesquisa Médica Translacional/história
[Pt] Tipo de publicação:BIOGRAPHY; HISTORICAL ARTICLE; JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Plant Proteins); 30237-26-4 (Fructose); 9009-86-3 (Ricin); EC 1.17.1.4 (Xanthine Dehydrogenase); EC 3.2.2.22 (Ribosome Inactivating Proteins)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170509
[Lr] Data última revisão:
170509
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170131
[St] Status:MEDLINE


  8 / 2697 MEDLINE  
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[PMID]:28094539
[Au] Autor:Wang ML; Dzievit M; Chen Z; Morris JB; Norris JE; Barkley NA; Tonnis B; Pederson GA; Yu J
[Ad] Endereço:a USDA-ARS, Plant Genetic Resources Conservation Unit, 1109 Experiment Street, Griffin, GA 30223, USA.
[Ti] Título:Genetic diversity and population structure of castor (Ricinus communis L.) germplasm within the US collection assessed with EST-SSR markers.
[So] Source:Genome;60(3):193-200, 2017 Mar.
[Is] ISSN:1480-3321
[Cp] País de publicação:Canada
[La] Idioma:eng
[Ab] Resumo:Castor is an important oilseed crop and although its oil is inedible, it has multiple industrial and pharmaceutical applications. The entire US castor germplasm collection was previously screened for oil content and fatty acid composition, but its genetic diversity and population structure has not been determined. Based on the screening results of oil content, fatty acid composition, and country origins, 574 accessions were selected and genotyped with 22 polymorphic EST-SSR markers. The results from cluster analysis, population structure, and principal component analysis were consistent, and partitioned accessions into four subpopulations. Although there were certain levels of admixtures among groups, these clusters and subpopulations aligned with geographic origins. Both divergent and redundant accessions were identified in this study. The US castor germplasm collection encompasses a moderately high level of genetic diversity (pairwise dissimilarity coefficient = 0.53). The results obtained here will be useful for choosing accessions as parents to make crosses in breeding programs and prioritizing accessions for regeneration to improve germplasm management. A subset of 230 accessions was selected and will be planted in the field for establishing a core collection of the US castor germplasm. Further evaluation of the US castor germplasm collection is also discussed.
[Mh] Termos MeSH primário: Variação Genética
Genética Populacional
Ricinus/genética
[Mh] Termos MeSH secundário: Alelos
Análise por Conglomerados
Etiquetas de Sequências Expressas
Ácidos Graxos/química
Marcadores Genéticos
Genótipo
Geografia
Repetições de Microssatélites
Polimorfismo Genético
Análise de Componente Principal
Ricina/genética
Estados Unidos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fatty Acids); 0 (Genetic Markers); 9009-86-3 (Ricin)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170320
[Lr] Data última revisão:
170320
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170118
[St] Status:MEDLINE
[do] DOI:10.1139/gen-2016-0116


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[PMID]:28089771
[Au] Autor:Noy-Porat T; Alcalay R; Epstein E; Sabo T; Kronman C; Mazor O
[Ad] Endereço:Department of Biochemistry and Molecular Genetics, Israel Institute for Biological Research, Ness-Ziona, Israel.
[Ti] Título:Extended therapeutic window for post-exposure treatment of ricin intoxication conferred by the use of high-affinity antibodies.
[So] Source:Toxicon;127:100-105, 2017 Mar 01.
[Is] ISSN:1879-3150
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The plant toxin ricin is considered a potential bioterror agent against which there is no available antidote. To date, neutralizing antibodies are the most promising post-exposure treatment for ricin intoxication, yet so far they were shown to be effective only when given within several hours post exposure. As part of an ongoing effort to develop efficient ricin-countermeasures, we tested whether high-affinity antibodies that were previously isolated from immunized non-human primates, may confer effective post-exposure therapy for ricin-intoxicated mice treated at late time-points after exposure. While each antibody is capable of providing high protection rate by itself, a formulation consisting of three neutralizing antibodies that target different epitopes was tested to provide therapeutic coverage against different variants of the malicious pathogen. Indeed, the tri-antibody based cocktail was highly effective, its administration resulting in very high survival rates (>70%) when animals were treated as late as 48 h post exposure and significant protection (>30%) even at 72 h. This study establishes for the first time that anti-ricin antibodies can serve as a highly effective antidote at such late time-points after exposure. From the clinical point of view, the extended therapeutic window documented here is of high importance allowing adequate time to accurately identify the causative agent and may permit initiation of life-saving treatment with these antibodies even after the onset of clinical signs.
[Mh] Termos MeSH primário: Anticorpos Neutralizantes/farmacologia
Ricina/imunologia
[Mh] Termos MeSH secundário: Animais
Anticorpos Neutralizantes/imunologia
Afinidade de Anticorpos
Epitopos
Feminino
Células HeLa
Seres Humanos
Camundongos Endogâmicos ICR
Ricina/toxicidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Neutralizing); 0 (Epitopes); 9009-86-3 (Ricin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170117
[St] Status:MEDLINE


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[PMID]:28006682
[Au] Autor:Li CH; Xiao X; Tao J; Wang DM; Huang CZ; Zhen SJ
[Ad] Endereço:Key Laboratory of Luminescent and Real-Time Analytical Chemistry (Southwest University), Ministry of Education, College of Chemistry and Chemical Engineering, Southwest University, 400715 Chongqing, PR China.
[Ti] Título:A graphene oxide-based strand displacement amplification platform for ricin detection using aptamer as recognition element.
[So] Source:Biosens Bioelectron;91:149-154, 2017 May 15.
[Is] ISSN:1873-4235
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The toxic plant protein ricin is a potential agent for criminal or bioterrorist attacks due to the wide availability and relative ease of preparation. Herein, we developed a novel strategy for the detection of ricin B-chain (RTB) based on isothermal strand-displacement polymerase reaction (ISDPR) by using aptamer as a recognition element and graphene oxide (GO) as a low background platform. In this method, ricin-binding aptamer (RBA) hybridized with a short blocker firstly, and then was immobilized on the surface of streptavidin-coated magnetic beads (MBs). The addition of RTB could release the blocker, which could hybridize with the dye-modified hairpin probe and trigger the ISDPR, resulting in high fluorescence intensity. In the absence of RTB, however, the fluorescence of the dye could be quenched strongly by GO, resulting in the extremely low background signal. Thus, RTB could be sensitively detected by the significantly increased fluorescence signal. The linear range of the current analytical system was from 0.75µg/mL to 100µg/mL and the limit of detection (3σ) was 0.6µg/mL. This method has been successfully utilized for the detection of both the RTB and the entire ricin toxin in real samples, and it could be generalized to any kind of target detection based on an appropriate aptamer.
[Mh] Termos MeSH primário: Aptâmeros de Nucleotídeos/química
Técnicas Biossensoriais/métodos
Substâncias para a Guerra Química/análise
Substâncias para a Guerra Química/farmacocinética
Sucos de Frutas e Vegetais/análise
Ricina/análise
Ricina/urina
[Mh] Termos MeSH secundário: Semente de Rícino/química
Corantes Fluorescentes/química
Grafite/química
Seres Humanos
Limite de Detecção
Hibridização de Ácido Nucleico/métodos
Óxidos/química
Espectrometria de Fluorescência/métodos
[Pt] Tipo de publicação:EVALUATION STUDIES; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aptamers, Nucleotide); 0 (Chemical Warfare Agents); 0 (Fluorescent Dyes); 0 (Oxides); 7782-42-5 (Graphite); 9009-86-3 (Ricin)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170531
[Lr] Data última revisão:
170531
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161223
[St] Status:MEDLINE



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