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[PMID]:28334651
[Au] Autor:Chen D; Miao H; Zhao Y; Wu Y
[Ad] Endereço:Key Laboratory of Food Safety Risk Assessment, Ministry of Health, China National Center for Food Safety Risk Assessment, Beijing 100021, China.
[Ti] Título:Dispersive micro solid phase extraction of amantadine, rimantadine and memantine in chicken muscle with magnetic cation exchange polymer.
[So] Source:J Chromatogr B Analyt Technol Biomed Life Sci;1051:92-96, 2017 Apr 15.
[Is] ISSN:1873-376X
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:This study demonstrated a novel dispersive micro solid phase extraction (DMSPE) method for extraction of adamantane drugs (amantadine, rimantadine and memantine) in chicken muscle. The adamantane drugs were extracted from chicken muscle using 1% acidic acetonitrile as extraction solvent. The cleanup of fatty matrices from analytes was achieved by the DMSPE technique using magnetic cation exchange polymer as adsorbent. In this procedure, the experimental parameters and conditions were optimized in detail for the improvement of extraction efficiency. The method showed low limit of detection of 0.03µg/kg and recoveries of the analytes ranged from 87.2% to 109.3% for adamantane drugs. The proposed DMSPE method proved to be simple, effective and suitable for the treatment of adamantane drugs in chicken muscle with a relatively shorter extraction time.
[Mh] Termos MeSH primário: Amantadina/isolamento & purificação
Antivirais/isolamento & purificação
Dopaminérgicos/isolamento & purificação
Memantina/isolamento & purificação
Aves Domésticas
Rimantadina/isolamento & purificação
Extração em Fase Sólida/métodos
[Mh] Termos MeSH secundário: Adsorção
Animais
Cátions/química
Galinhas/metabolismo
Cromatografia Líquida de Alta Pressão/métodos
Contaminação de Alimentos/análise
Limite de Detecção
Imãs/química
Espectrometria de Massas/métodos
Músculos/química
Polímeros/química
Aves Domésticas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; VALIDATION STUDIES
[Nm] Nome de substância:
0 (Antiviral Agents); 0 (Cations); 0 (Dopamine Agents); 0 (Polymers); 0T2EF4JQTU (Rimantadine); BF4C9Z1J53 (Amantadine); W8O17SJF3T (Memantine)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170601
[Lr] Data última revisão:
170601
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170324
[St] Status:MEDLINE


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[PMID]:27856102
[Au] Autor:Peng D; Wei W; Pan Y; Wang Y; Chen D; Liu Z; Wang X; Dai M; Yuan Z
[Ad] Endereço:National Reference Laboratory of Veterinary Drug Residues (HZAU) and MAO Key Laboratory for Detection of Veterinary Drug Residues, MOA Laboratory for Risk Assessment of Quality and Safety of Livestock and Poultry Products, Hubei Collaborative Innovation Centre for Animal Nutrition and Feed Safety, H
[Ti] Título:Preparation of a monoclonal antibody against amantadine and rimantadine and development of an indirect competitive enzyme-linked immunosorbent assay for detecting the same in chicken muscle and liver.
[So] Source:J Pharm Biomed Anal;133:56-63, 2017 Jan 30.
[Is] ISSN:1873-264X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A monoclonal antibody (mAb) was produced in order to monitor the illegal use of amantadine and rimantadine in animals. The produced mAb 2G3 exhibited an IC value of 15.8µgL for amantadine and exhibited cross-reactivity to both amantadine (100%) and rimantadine (70.6%). Standard curves ranged from 5 to 80µgL for 2G3. The limits of detection of the developed indirect competitive enzyme-linked immunosorbent assay (ic-ELISA) ranged from 5.0µgkg to 5.4µgkg in chicken muscle and liver. The recoveries were 81.3% to 98.1% with a coefficient of variation less than 15.7%. Good correlations were observed between the results of the ic-ELISA and liquid chromatography-mass spectrometry in the incurred tissues. These results suggest that ic-ELISA is a sensitive, accurate, and low-cost method that could be a useful tool for screening the residues of amantadine and rimantadine in chicken muscle and liver.
[Mh] Termos MeSH primário: Amantadina/análise
Anticorpos Monoclonais/imunologia
Ensaio de Imunoadsorção Enzimática/métodos
Fígado/química
Músculos/química
Rimantadina/análise
[Mh] Termos MeSH secundário: Amantadina/imunologia
Animais
Galinhas
Resíduos de Drogas/análise
Limite de Detecção
Rimantadina/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0T2EF4JQTU (Rimantadine); BF4C9Z1J53 (Amantadine)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170508
[Lr] Data última revisão:
170508
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161119
[St] Status:MEDLINE


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[PMID]:27383164
[Au] Autor:Shibnev VA; Garaev TM; Deryabin PG; Finogenova MP; Botikov AG; Mishin DV
[Ad] Endereço:D. I. Ivanovsky Institute of Virology, N. F. Gamaleya Federal Research Center of Epidemiology and Microbiology, Ministry of Health of the Russian Federation, Moscow, Russia.
[Ti] Título:New Carbocyclic Amino Acid Derivatives Inhibit Infection Caused by Highly Pathogenic Influenza A Virus Strain (H5N1).
[So] Source:Bull Exp Biol Med;161(2):284-7, 2016 Jun.
[Is] ISSN:1573-8221
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:New amino acid derivatives with carbocycles of adamantine and quinaldic acid were synthesized and their in vitro antiviral activity against influenza A/H5N1 virus was evaluated. Experiments on cultured embryonic porcine kidney epithelial cells showed that amino acid derivatives suppressed viral replication. Tret-butyloxycarbonyl-DL-methionylsulfonyl-1-adamantayl ethylamine and benzyloxycarbonyl-L-trypthophanyl-1-adamantayl ethylamine compounds demonstrated high activity in all in vitro experiments. Moreover, some compounds showed virucidal activity against influenza A/H5N1 virus.
[Mh] Termos MeSH primário: Aminoácidos/farmacologia
Antivirais/farmacologia
Vírus da Influenza A Subtipo H5N1/efeitos dos fármacos
Rimantadina/farmacologia
Replicação Viral/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Avaliação Pré-Clínica de Medicamentos
Vírus da Influenza A Subtipo H5N1/fisiologia
Concentração Inibidora 50
Sus scrofa
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids); 0 (Antiviral Agents); 0T2EF4JQTU (Rimantadine)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170207
[Lr] Data última revisão:
170207
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160708
[St] Status:MEDLINE
[do] DOI:10.1007/s10517-016-3396-0


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[PMID]:27276260
[Au] Autor:Breitinger U; Farag NS; Ali NKM; Breitinger HA
[Ad] Endereço:Department of Biochemistry, German University in Cairo, New Cairo, Egypt.
[Ti] Título:Patch-Clamp Study of Hepatitis C p7 Channels Reveals Genotype-Specific Sensitivity to Inhibitors.
[So] Source:Biophys J;110(11):2419-2429, 2016 Jun 07.
[Is] ISSN:1542-0086
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hepatitis C is a major worldwide disease and health hazard, affecting ∼3% of the world population. The p7 protein of hepatitis C virus (HCV) is an intracellular ion channel and pH regulator that is involved in the viral replication cycle. It is targeted by various classical ion channel blockers. Here, we generated p7 constructs corresponding to HCV genotypes 1a, 2a, 3a, and 4a for recombinant expression in HEK293 cells, and studied p7 channels using patch-clamp recording techniques. The pH50 values for recombinant p7 channels were between 6.0 and 6.5, as expected for proton-activated channels, and current-voltage dependence did not show any differences between genotypes. Inhibition of p7-mediated currents by amantadine, however, exhibited significant, genotype-specific variation. The IC50 values of p7-1a and p7-4a were 0.7 ± 0.1 nM and 3.2 ± 1.2 nM, whereas p7-2a and p7-3a had 50- to 1000-fold lower sensitivity, with IC50 values of 2402 ± 334 nM and 344 ± 64 nM, respectively. The IC50 values for rimantadine were low across all genotypes, ranging from 0.7 ± 0.1 nM, 1.6 ± 0.6 nM, and 3.0 ± 0.8 nM for p7-1a, p7-3a, and p7-4a, respectively, to 24 ± 4 nM for p7-2a. Results from patch-clamp recordings agreed well with cellular assays of p7 activity, namely, measurements of intracellular pH and hemadsorption assays, which confirmed the much reduced amantadine sensitivity of genotypes 2a and 3a. Thus, our results establish patch-clamp studies of recombinant viroporins as a valid analytical tool that can provide quantitative information about viroporin channel properties, complementing established techniques.
[Mh] Termos MeSH primário: Antivirais/farmacologia
Hepacivirus/efeitos dos fármacos
Hepacivirus/genética
Técnicas de Patch-Clamp
Proteínas Virais/antagonistas & inibidores
Proteínas Virais/genética
[Mh] Termos MeSH secundário: Amantadina/farmacologia
Western Blotting
Genótipo
Células HEK293
Hemadsorção/efeitos dos fármacos
Hemadsorção/fisiologia
Seres Humanos
Concentração de Íons de Hidrogênio
Potenciais da Membrana/efeitos dos fármacos
Potenciais da Membrana/fisiologia
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Rimantadina/farmacologia
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antiviral Agents); 0 (Recombinant Proteins); 0 (Viral Proteins); 0 (p7 protein, Hepatitis C virus); 0T2EF4JQTU (Rimantadine); BF4C9Z1J53 (Amantadine)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170827
[Lr] Data última revisão:
170827
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160609
[St] Status:MEDLINE


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[PMID]:26954078
[Au] Autor:Zhirnov OP; Manykin AA; Rossman JS; Klenk HD
[Ad] Endereço:D.I. Ivanovsky Institute of Virology, Moscow 123098, Russia. Electronic address: zhirnov@inbox.ru.
[Ti] Título:Intravirion cohesion of matrix protein M1 with ribonucleocapsid is a prerequisite of influenza virus infectivity.
[So] Source:Virology;492:187-96, 2016 May.
[Is] ISSN:1096-0341
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Influenza virus has two major structural modules, an external lipid envelope and an internal ribonucleocapsid containing the genomic RNA in the form of the ribonucleoprotein (RNP) complex, both of which are interlinked by the matrix protein M1. Here we studied M1-RNP cohesion within virus exposed to acidic pH in vitro. The effect of acidification was dependent on the cleavage of the surface glycoprotein HA. Acidic pH caused a loss of intravirion RNP-M1 cohesion and activated RNP polymerase activity in virus with cleaved HA (HA1/2) but not in the uncleaved (HA0) virus. The in vitro acidified HA1/2 virus rapidly lost infectivity whereas the HA0 one retained infectivity, following activation by trypsin, suggesting that premature activation and release of the RNP is detrimental to viral infectivity. Rimantadine, an inhibitor of the M2 ion channel, was found to protect the HA1/2 virus interior against acidic disintegration, confirming that M2-dependent proton translocation is essential for the intravirion RNP release and suggesting that the M2 ion channel is only active in virions with cleaved HA. Acidic treatment of both HA0 and HA1/2 influenza viruses induces formation of spikeless bleb-like protrusion of ~ 25 nm in diameter on the surface of the virion, though only the HA1/2 virus was permeable to protons and permitted RNP release. It is likely that this bleb corresponds to the M2-enriched and M1-depleted focus arising from pinching off of the virus during the completion of budding. Cooperatively, the data suggest that the influenza virus has an asymmetric structure where the M1-mediated organization of the RNP inside the virion is a prerequisite for infectious entry into target cell.
[Mh] Termos MeSH primário: Glicoproteínas de Hemaglutininação de Vírus da Influenza/metabolismo
Vírus da Influenza A Subtipo H3N2/metabolismo
Nucleocapsídeo/metabolismo
Prótons
Proteínas da Matriz Viral/metabolismo
Vírion/metabolismo
[Mh] Termos MeSH secundário: Animais
Antivirais/farmacologia
Embrião de Galinha
Cães
Expressão Gênica
Glicoproteínas de Hemaglutininação de Vírus da Influenza/genética
Seres Humanos
Concentração de Íons de Hidrogênio
Vírus da Influenza A Subtipo H3N2/efeitos dos fármacos
Vírus da Influenza A Subtipo H3N2/patogenicidade
Vírus da Influenza A Subtipo H3N2/ultraestrutura
Células Madin Darby de Rim Canino
Nucleocapsídeo/química
Nucleocapsídeo/genética
Rimantadina/farmacologia
Tripsina/farmacologia
Proteínas da Matriz Viral/antagonistas & inibidores
Proteínas da Matriz Viral/química
Proteínas da Matriz Viral/genética
Vírion/efeitos dos fármacos
Vírion/patogenicidade
Vírion/ultraestrutura
Virulência
Internalização do Vírus/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antiviral Agents); 0 (Hemagglutinin Glycoproteins, Influenza Virus); 0 (M1 protein, Influenza A virus); 0 (M2 protein, Influenza A virus); 0 (Protons); 0 (Viral Matrix Proteins); 0 (hemagglutinin, human influenza A virus); 0T2EF4JQTU (Rimantadine); EC 3.4.21.4 (Trypsin)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160309
[St] Status:MEDLINE


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[PMID]:26949181
[Au] Autor:Tzeng JI; Wang JN; Wang JJ; Chen YW; Hung CH
[Ad] Endereço:Department of Anesthesiology, Chi-Mei Medical Center, Yong Kang, Tainan, Taiwan.
[Ti] Título:Intrathecal rimantadine induces motor, proprioceptive, and nociceptive blockades in rats.
[So] Source:Neurosci Lett;618:94-98, 2016 Apr 08.
[Is] ISSN:1872-7972
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:The purpose of the experiment was to evaluate the local anesthetic effect of rimantadine in spinal anesthesia. Rimantadine in a dose-dependent fashion was constructed after intrathecally injecting the rats with four different doses. The potency and duration of rimantadine were compared with that of the local anesthetic lidocaine at producing spinal motor, nociceptive, and proprioceptive blockades. We demonstrated that intrathecal rimantadine dose-dependently produced spinal motor, nociceptive, and proprioceptive blockades. On the 50% effective dose (ED50) basis, the ranks of potencies at inducing spinal motor, nociceptive, and proprioceptive blockades was lidocaine>rimantadine (P<0.01). Rimantadine exhibited more nociceptive block (ED50) than motor block (P<0.05). At equi-anesthetic doses (ED25, ED50, and ED75), the spinal block duration produced by rimantadine was longer than that produced by lidocaine (P<0.01). Furthermore, rimantadine (26.52µmol/kg) prolonged the nociceptive nerve block more than the motor block (P<0.001). Our preclinical data showed that rimantadine, with a more sensory-selective action over motor block, was less potent than lidocaine. Rimantadine produced longer duration in spinal anesthesia when compared with lidocaine.
[Mh] Termos MeSH primário: Anestésicos Locais/farmacologia
Atividade Motora/efeitos dos fármacos
Nociceptividade/efeitos dos fármacos
Propriocepção/efeitos dos fármacos
Rimantadina/farmacologia
[Mh] Termos MeSH secundário: Raquianestesia
Animais
Relação Dose-Resposta a Droga
Injeções Espinhais
Lidocaína/farmacologia
Masculino
Bloqueio Nervoso
Ratos Sprague-Dawley
Reflexo/efeitos dos fármacos
Vocalização Animal/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anesthetics, Local); 0T2EF4JQTU (Rimantadine); 98PI200987 (Lidocaine)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:170728
[Lr] Data última revisão:
170728
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160308
[St] Status:MEDLINE


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[PMID]:26872862
[Au] Autor:McKimm-Breschkin JL; Fry AM
[Ad] Endereço:CSIRO, 343 Royal Parade, Parkville, Australia. Electronic address: mck245@csiro.au.
[Ti] Título:Meeting report: 4th ISIRV antiviral group conference: Novel antiviral therapies for influenza and other respiratory viruses.
[So] Source:Antiviral Res;129:21-38, 2016 May.
[Is] ISSN:1872-9096
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The International Society for Influenza and other Respiratory Virus Diseases (isirv) held its 4th Antiviral Group Conference at the University of Texas on 2-4 June, 2015. With emerging resistance to the drugs currently licensed for treatment and prophylaxis of influenza viruses, primarily the neuraminidase inhibitor oseltamivir phosphate (Tamiflu) and the M2 inhibitors amantadine and rimantadine, and the lack of effective interventions against other respiratory viruses, the 3-day programme focused on the discovery and development of inhibitors of several virus targets and key host cell factors involved in virus replication or mediating the inflammatory response. Virus targets included the influenza haemagglutinin, neuraminidase and M2 proteins, and both the respiratory syncytial virus and influenza polymerases and nucleoproteins. Therapies for rhinoviruses and MERS and SARS coronaviruses were also discussed. With the emerging development of monoclonal antibodies as therapeutics, the potential implications of antibody-dependent enhancement of disease were also addressed. Topics covered all aspects from structural and molecular biology to preclinical and clinical studies. The importance of suitable clinical trial endpoints and regulatory issues were also discussed from the perspectives of both industry and government. This meeting summary provides an overview, not only for the conference participants, but also for those interested in the current status of antivirals for respiratory viruses.
[Mh] Termos MeSH primário: Antivirais/uso terapêutico
Influenza Humana/tratamento farmacológico
Infecções Respiratórias/tratamento farmacológico
Infecções Respiratórias/virologia
[Mh] Termos MeSH secundário: Amantadina/uso terapêutico
Anticorpos Facilitadores
Antivirais/administração & dosagem
Antivirais/efeitos adversos
Antivirais/farmacologia
Infecções por Coronavirus/tratamento farmacológico
Farmacorresistência Viral
Inibidores Enzimáticos/uso terapêutico
Seres Humanos
Influenza Humana/virologia
Neuraminidase/uso terapêutico
Orthomyxoviridae/efeitos dos fármacos
Oseltamivir/uso terapêutico
Infecções por Picornaviridae/tratamento farmacológico
Rimantadina/uso terapêutico
Síndrome Respiratória Aguda Grave/tratamento farmacológico
Texas
Replicação Viral/efeitos dos fármacos
[Pt] Tipo de publicação:CONGRESSES
[Nm] Nome de substância:
0 (Antiviral Agents); 0 (Enzyme Inhibitors); 0T2EF4JQTU (Rimantadine); 20O93L6F9H (Oseltamivir); BF4C9Z1J53 (Amantadine); EC 3.2.1.18 (Neuraminidase)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160214
[St] Status:MEDLINE


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[PMID]:26804976
[Au] Autor:Wright AK; Batsomboon P; Dai J; Hung I; Zhou HX; Dudley GB; Cross TA
[Ad] Endereço:National High Magnetic Field Laboratory, Florida State University , Tallahassee, Florida 32310, United States.
[Ti] Título:Differential Binding of Rimantadine Enantiomers to Influenza A M2 Proton Channel.
[So] Source:J Am Chem Soc;138(5):1506-9, 2016 Feb 10.
[Is] ISSN:1520-5126
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Rimantadine hydrochloride (α-methyl-1-adamantane-methalamine hydrochloride) is a chiral compound which exerts antiviral activity against the influenza A virus by inhibiting proton conductance of the M2 ion channel. In complex with M2, rimantadine has always been characterized as a racemic mixture. Here, we report the novel enantioselective synthesis of deuterium-labeled (R)- and (S)-rimantadine and the characterization of their protein-ligand interactions using solid-state NMR. Isotropic chemical shift changes strongly support differential binding of the enantiomers to the proton channel. Position restrained simulations satisfying distance restraints from (13)C-(2)H rotational-echo double-resonance NMR show marked differences in the hydrogen-bonding pattern of the two enantiomers at the binding site. Together these results suggest a complex set of interactions between (R)-rimantadine and the M2 proton channel, leading to a higher stability for this enantiomer of the drug in the channel pore.
[Mh] Termos MeSH primário: Antivirais/metabolismo
Rimantadina/metabolismo
Proteínas da Matriz Viral/metabolismo
[Mh] Termos MeSH secundário: Antivirais/química
Ligações de Hidrogênio
Espectroscopia de Ressonância Magnética
Ligação Proteica
Rimantadina/química
Estereoisomerismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Antiviral Agents); 0 (M2 protein, Influenza A virus); 0 (Viral Matrix Proteins); 0T2EF4JQTU (Rimantadine)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160126
[St] Status:MEDLINE
[do] DOI:10.1021/jacs.5b13129


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[PMID]:26574023
[Au] Autor:Fernandez MV; Miller E; Krammer F; Gopal R; Greenbaum BD; Bhardwaj N
[Ad] Endereço:Department of Pathology, New York University School of Medicine, New York, New York, USA;
[Ti] Título:Ion efflux and influenza infection trigger NLRP3 inflammasome signaling in human dendritic cells.
[So] Source:J Leukoc Biol;99(5):723-34, 2016 May.
[Is] ISSN:1938-3673
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The nucleotide-binding oligomerization domain-like receptor protein 3 inflammasome, a multiprotein complex, is an essential intracellular mediator of antiviral immunity. In murine dendritic cells, this complex responds to a wide array of signals, including ion efflux and influenza A virus infection, to activate caspase-1-mediated proteolysis of IL-1ß and IL-18 into biologically active cytokines. However, the presence and function of the nucleotide-binding oligomerization domain-like receptor protein 3 inflammasome in human dendritic cells, in response to various triggers, including viral infection, has not been defined clearly. Here, we delineate the contribution of the nucleotide-binding oligomerization domain-like receptor protein 3 inflammasome to the secretion of IL-1ß, IL-18, and IL-1α by human dendritic cells (monocyte-derived and primary conventional dendritic cells). Activation of the nucleotide-binding oligomerization domain-like receptor protein 3 inflammasome in human dendritic cells by various synthetic activators resulted in the secretion of bioactive IL-1ß, IL-18, and IL-1α and induction of pyroptotic cell death. Cellular IL-1ß release depended on potassium efflux and the activity of proteins nucleotide-binding oligomerization domain-like receptor protein 3 and caspase-1. Likewise, influenza A virus infection of dendritic cells resulted in priming and activation of the nucleotide-binding oligomerization domain-like receptor protein 3 inflammasome and secretion of IL-1ß and IL-18 in an M2- and nucleotide-binding oligomerization domain-like receptor protein 3-dependent manner. The magnitude of priming by influenza A virus varied among different strains and inversely corresponded to type I IFN production. To our knowledge, this is the first report describing the existence and function of the nucleotide-binding oligomerization domain-like receptor protein 3 inflammasome in human dendritic cells and the ability of influenza A virus to prime and activate this pathway in human dendritic cells, with important implications for antiviral immunity and pathogenesis.
[Mh] Termos MeSH primário: Células Dendríticas/imunologia
Células Dendríticas/virologia
Inflamassomos/metabolismo
Vírus da Influenza A/fisiologia
Proteína 3 que Contém Domínio de Pirina da Família NLR/metabolismo
Transdução de Sinais/imunologia
[Mh] Termos MeSH secundário: Amantadina/farmacologia
Apoptose/efeitos dos fármacos
Caspase 1/metabolismo
Seres Humanos
Imidazóis/farmacologia
Interferons/metabolismo
Interleucina-1/metabolismo
Transporte de Íons/efeitos dos fármacos
Íons/metabolismo
Monócitos/efeitos dos fármacos
Monócitos/patologia
Rimantadina/farmacologia
Receptores Toll-Like/metabolismo
Regulação para Cima/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Imidazoles); 0 (Inflammasomes); 0 (Interleukin-1); 0 (Ions); 0 (NLR Family, Pyrin Domain-Containing 3 Protein); 0 (NLRP3 protein, human); 0 (Toll-Like Receptors); 0T2EF4JQTU (Rimantadine); 9008-11-1 (Interferons); BF4C9Z1J53 (Amantadine); EC 3.4.22.36 (Caspase 1); V3DMU7PVXF (resiquimod)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170901
[Lr] Data última revisão:
170901
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151118
[St] Status:MEDLINE
[do] DOI:10.1189/jlb.3A0614-313RRR


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[PMID]:26391902
[Au] Autor:Van Nguyen H; Nguyen HT; Le LT
[Ad] Endereço:Life Science Laboratory, Institute for Computational Science and Technology, Ho Chi Minh City, Vietnam.
[Ti] Título:Investigation of the free energy profiles of amantadine and rimantadine in the AM2 binding pocket.
[So] Source:Eur Biophys J;45(1):63-70, 2016 Jan.
[Is] ISSN:1432-1017
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The purpose of this work was to study the mechanism of drug resistance of M2 channel proteins by analyzing the interactions between the drugs amantadine and rimantadine and M2 channel proteins (including the wild type and the three mutants V27A, S31N, and G34A) and the drug binding pathways, by use of a computational approach. Our results showed that multiple drug-binding sites were present in the M2 channel, and the trajectory of the drugs through the M2 channel was determined. A novel method was developed to investigate of free energy profiles of the ligand-protein complexes. Our work provides a new explanation of the large amount of experimental data on drug efficacy.
[Mh] Termos MeSH primário: Amantadina/farmacologia
Simulação de Acoplamento Molecular
Rimantadina/farmacologia
Proteínas da Matriz Viral/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Substituição de Aminoácidos
Sítios de Ligação
Dados de Sequência Molecular
Ligação Proteica
Proteínas da Matriz Viral/genética
Proteínas da Matriz Viral/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (M2 protein, Influenza A virus); 0 (Viral Matrix Proteins); 0T2EF4JQTU (Rimantadine); BF4C9Z1J53 (Amantadine)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150923
[St] Status:MEDLINE
[do] DOI:10.1007/s00249-015-1077-y



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