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  1 / 1213 MEDLINE  
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[PMID]:28592143
[Au] Autor:Pang X; Lin X; Tian Y; Liang R; Wang J; Yang B; Zhou X; Kaliyaperumal K; Luo X; Tu Z; Liu Y
[Ad] Endereço:a CAS Key Laboratory of Tropical Marine Bio-resources and Ecology/Guangdong Key Laboratory of Marine Materia Medica/RNAM Center for Marine Microbiology , South China Sea Institute of Oceanology, Chinese Academy of Sciences , Guangzhou , China.
[Ti] Título:Three new polyketides from the marine sponge-derived fungus Trichoderma sp. SCSIO41004.
[So] Source:Nat Prod Res;32(1):105-111, 2018 Jan.
[Is] ISSN:1478-6427
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Three new polyketides named trichbenzoisochromen A (1), 5,7-dihydroxy-3-methyl -2-(2-oxopropyl)naphthalene-1,4-dione (2) and 7-acetyl-1,3,6-trihydroxyanthracene-9,10- dione (3) together with six known compounds (4-9) were isolated from a sponge-derived fungus Trichoderma sp. SCSIO41004. The structures of three new polyketides (1-3) were determined by the extensive spectroscopic analysis, including 1D, 2D NMR and HRESIMS data. The absolute configuration of compound 1 was confirmed by the specific optical rotation value and CD spectra analyses. Compound 4 exhibited significant inhibitory activity against EV71 with the IC value of 25.7 µM.
[Mh] Termos MeSH primário: Antracenos/química
Antivirais/química
Antivirais/farmacologia
Naftalenos/química
Policetídeos/química
Trichoderma/química
[Mh] Termos MeSH secundário: Animais
Antracenos/farmacologia
Organismos Aquáticos/química
Dicroísmo Circular
Enterovirus Humano A/efeitos dos fármacos
Fermentação
Seres Humanos
Vírus da Influenza A Subtipo H3N2/efeitos dos fármacos
Células K562
Células MCF-7
Espectroscopia de Ressonância Magnética/métodos
Estrutura Molecular
Naftalenos/farmacologia
Policetídeos/farmacologia
Poríferos/microbiologia
Espectrometria de Massas por Ionização por Electrospray
Trichoderma/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anthracenes); 0 (Antiviral Agents); 0 (Naphthalenes); 0 (Polyketides)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180301
[Lr] Data última revisão:
180301
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170609
[St] Status:MEDLINE
[do] DOI:10.1080/14786419.2017.1338286


  2 / 1213 MEDLINE  
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[PMID]:28469998
[Au] Autor:Yang X; Xie J; Jia L; Liu N; Liang Y; Wu F; Liang B; Li Y; Wang J; Sheng C; Li H; Liu H; Ma Q; Yang C; Du X; Qiu S; Song H
[Ad] Endereço:Center for Infectious Disease Control, Institute of Disease Control and Prevention, Academy of Military Medical SciencesBeijing, China.
[Ti] Título:Analysis of miRNAs Involved in Mouse Brain Damage upon Enterovirus 71 Infection.
[So] Source:Front Cell Infect Microbiol;7:133, 2017.
[Is] ISSN:2235-2988
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Enterovirus 71 (EV71) infects the central nervous system (CNS) and causes brainstem encephalitis in children. MiRNAs have been found to play various functions in EV71 infection in human cell lines. To identify potential miRNAs involved in the inflammatory injury in CNS, our study, for the first time, performed a miRNA microarray assay using EV71 infected mice brains. Twenty differentially expressed miRNAs were identified (four up- and 16 down-regulated) and confirmed by qRT-PCR. The target genes of these miRNAs were analyzed using KEGG (Kyoto Encyclopedia of Genes and Genomes) analysis, revealing that the miRNAs were mainly involved in the regulation of inflammation and neural system function. MiR-150-5p, -3082-5p, -3473a, -468-3p, -669n, -721, -709, and -5107-5p that regulate MAPK and chemokine signaling were all down-regulated, which might result in increased cytokine production. In addition, miR-3473a could also regulate focal adhesion and leukocyte trans-endothelial migration, suggesting a role in virus-induced blood-brain barrier disruption. The miRNAs and pathways identified in this study could help to understand the intricate interactions between EV71 and the brain injury, offering new insight for the future research of the molecular mechanism of EV71 induced brainstem encephalitis.
[Mh] Termos MeSH primário: Lesões Encefálicas/patologia
Encéfalo/virologia
Enterovirus Humano A/patogenicidade
MicroRNAs/metabolismo
MicroRNAs/farmacologia
[Mh] Termos MeSH secundário: Animais
Barreira Hematoencefálica
Encéfalo/patologia
Lesões Encefálicas/virologia
Linhagem Celular
Sistema Nervoso Central/patologia
Sistema Nervoso Central/virologia
Quimiocinas/metabolismo
Citocinas/metabolismo
Regulação para Baixo
Enterovirus Humano A/genética
Infecções por Enterovirus
Perfilação da Expressão Gênica
Seres Humanos
Inflamação
Camundongos
MicroRNAs/genética
Quinases de Proteína Quinase Ativadas por Mitógeno/metabolismo
Reação em Cadeia da Polimerase em Tempo Real
Taxa de Sobrevida
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Chemokines); 0 (Cytokines); 0 (MicroRNAs); EC 2.7.12.2 (Mitogen-Activated Protein Kinase Kinases)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180216
[Lr] Data última revisão:
180216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.3389/fcimb.2017.00133


  3 / 1213 MEDLINE  
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[PMID]:27771182
[Au] Autor:Yang L; Liu Y; Li S; Zhao H; Lin Q; Yu H; Huang X; Zheng Q; Cheng T; Xia N
[Ad] Endereço:State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, National Institute of Diagnostics and Vaccine Development in Infectious Diseases, School of Life Science & School of Public Health, Xiamen University, Xiamen, China.
[Ti] Título:A novel inactivated enterovirus 71 vaccine can elicit cross-protective immunity against coxsackievirus A16 in mice.
[So] Source:Vaccine;34(48):5938-5945, 2016 11 21.
[Is] ISSN:1873-2518
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Hand, foot, and mouth disease (HFMD) is a highly contagious disease that mainly affects infants and children. Enterovirus 71 (EV71) and coxsackievirus A16 (CA16) are the major pathogens of HFMD. Two EV71 vaccines were recently licensed in China and the administration of the EV71 vaccines is believed to significantly reduce the number of HFMD-related severe or fatal cases. However, a monovalent EV71 vaccine cannot cross-protect against CA16 infection, this may result in that it cannot effectively control the overall HFMD epidemic. In this study, a chimeric EV71, whose VP1/210-225 epitope was replaced by that of CA16, was constructed using a reverse genetics technique to produce a candidate EV71/CA16 bivalent vaccine strain. The chimeric EV71 was infectious and showed similar growth characteristics as its parental strain. The replacement of the VP1/210-225 epitope did not significantly affect the antigenicity and immunogenicity of EV71. More importantly, the chimeric EV71 could induce protective immunity against both EV71 and CA16, and protect neonatal mice against either EV71 or CA16 lethal infections, the chimeric EV71 constructed in this study was shown to be a feasible and promising candidate bivalent vaccine against both EV71 and CA16. The construction of a chimeric enterovirus also provides an alternative platform for broad-spectrum HFMD vaccines development.
[Mh] Termos MeSH primário: Infecções por Coxsackievirus/prevenção & controle
Proteção Cruzada
Infecções por Enterovirus/prevenção & controle
Enterovirus/imunologia
Vacinas Virais/imunologia
[Mh] Termos MeSH secundário: Animais
Anticorpos Neutralizantes/sangue
Anticorpos Antivirais/sangue
Infecções por Coxsackievirus/imunologia
Enterovirus Humano A/genética
Enterovirus Humano A/imunologia
Infecções por Enterovirus/imunologia
Epitopos/imunologia
Doença de Mão, Pé e Boca/prevenção & controle
Seres Humanos
Imunogenicidade da Vacina
Camundongos
Genética Reversa
Vacinas de Produtos Inativados/administração & dosagem
Vacinas de Produtos Inativados/imunologia
Vacinas Virais/administração & dosagem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibodies, Neutralizing); 0 (Antibodies, Viral); 0 (Epitopes); 0 (Vaccines, Inactivated); 0 (Viral Vaccines)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180206
[Lr] Data última revisão:
180206
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE


  4 / 1213 MEDLINE  
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[PMID]:28745308
[Au] Autor:Zhang X; Shi J; Ye X; Ku Z; Zhang C; Liu Q; Huang Z
[Ad] Endereço:Unit of Vaccinology &Antiviral Strategies, CAS Key Laboratory of Molecular Virology &Immunology, Institut Pasteur of Shanghai, Chinese Academy of Sciences, Shanghai 200031, China.
[Ti] Título:Coxsackievirus A16 utilizes cell surface heparan sulfate glycosaminoglycans as its attachment receptor.
[So] Source:Emerg Microbes Infect;6(7):e65, 2017 Jul 26.
[Is] ISSN:2222-1751
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Coxsackievirus A16 (CVA16) is one of the major pathogens responsible for hand, foot and mouth disease, which affects more than two million children in the Asian-Pacific region annually. Previous studies have shown that scavenger receptor B2 is a functional receptor for CVA16 that facilitates the uncoating process. However, it remains unclear whether other receptors are required for efficient CVA16 infection. In this study, by using a variety of assays we demonstrated that CVA16 utilizes surface heparan sulfate glycosaminoglycans as its attachment receptor. We further showed that five surface-exposed positively charged residues located in a cluster at the five-fold vertex of the virion are critical to heparan sulfate binding and cellular attachment of CVA16. Among the five residues, the arginine at position 166 (R166) of VP1 capsid protein appeared to be the most important for the interaction between CVA16 and heparan sulfate. Alanine substitution at this site (R166A) almost completely abolished heparan sulfate binding and cellular attachment of the virus. Our work achieves insight into the early events of CVA16 infection, thereby providing information that may facilitate the rational design of antiviral drugs and vaccines against CVA16 infection.
[Mh] Termos MeSH primário: Enterovirus Humano A/fisiologia
Heparitina Sulfato/metabolismo
Receptores Virais/metabolismo
Ligação Viral
[Mh] Termos MeSH secundário: Alanina
Substituição de Aminoácidos
Animais
Arginina
Proteínas do Capsídeo/química
Proteínas do Capsídeo/metabolismo
Cercopithecus aethiops
Enterovirus Humano A/química
Heparitina Sulfato/química
Seres Humanos
Receptores Virais/química
Células Vero
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Capsid Proteins); 0 (Receptors, Virus); 0 (VP1 protein, Foot-and-mouth disease virus); 9050-30-0 (Heparitin Sulfate); 94ZLA3W45F (Arginine); OF5P57N2ZX (Alanine)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180118
[Lr] Data última revisão:
180118
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE
[do] DOI:10.1038/emi.2017.55


  5 / 1213 MEDLINE  
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[PMID]:29216216
[Au] Autor:Chen M; Ju Y; Chen M; Xie Z; Zhou K; Tan Y; Mo J
[Ad] Endereço:Institute of Acute Infectious Diseases Control and Prevention, Guangxi Zhuang Autonomous Region Center for Disease Prevention and Control, Nanning, Guangxi, China.
[Ti] Título:Epidemiological and genetic characteristics of EV71 in hand, foot, and mouth disease in Guangxi, southern China, from 2010 to 2015.
[So] Source:PLoS One;12(12):e0188640, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hand, foot, and mouth disease (HFMD) is a significant public health challenge in China. Human enterovirus 71 (EV71) is regarded as the predominant causative pathogen of HFMD. Since 2015, two inactivated EV71 vaccines have been approved in mainland China, and because their use could change the HFMD pathogen spectrum, this should now be monitored. However, the epidemiological and genetic trends of EV71 with respect to HFMD in Guangxi, southern China, are still not clear. In this study, we describe the epidemiological and genetic characterization of this virus in clinically-diagnosed HFMD reported from 2010 to 2015 in Guangxi. Data showed that a two-year epidemic cycle, with a predominance of EV71 infections, contributed to HFMD outbreaks in Guangxi. Furthermore, this virus is a major causative agent of severe and fatal HFMD. Interestingly, in Guangxi, EV71-positive rates tended to decrease over time. In particular, EV71-positive rates were found in Fangchenggang city, which reported very few severe and fatal cases over the six-year period. Phylogenetic analysis of the VP1 gene revealed that the major circulating strains belonged exclusively to genotype C, subtype 4a (C4a), and most clustered with strains circulating in southern China. The most interesting finding was that a strain isolated in 2012 clustered with Vietnamese strains isolated from 2011-2012. The data highlight the importance of pathogen surveillance for HFMD in China, especially Guangxi, which is located on the border of China and the Association of Southeast Asian Nations.
[Mh] Termos MeSH primário: Enterovirus Humano A/patogenicidade
Doença de Mão, Pé e Boca/epidemiologia
[Mh] Termos MeSH secundário: China/epidemiologia
Surtos de Doenças
Enterovirus Humano A/genética
Enterovirus Humano A/isolamento & purificação
Feminino
Genes Virais
Seres Humanos
Masculino
Filogenia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171229
[Lr] Data última revisão:
171229
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171208
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0188640


  6 / 1213 MEDLINE  
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[PMID]:29182509
[Au] Autor:Xie L; Lu B; Zheng Z; Miao Y; Liu Y; Zhang Y; Zheng C; Ke X; Hu Q; Wang H
[Ad] Endereço:1​CAS Key Laboratory of Special Pathogens and Biosafety, Center for Emerging Infectious Diseases, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, PR China.
[Ti] Título:The 3C protease of enterovirus A71 counteracts the activity of host zinc-finger antiviral protein (ZAP).
[So] Source:J Gen Virol;99(1):73-85, 2018 Jan.
[Is] ISSN:1465-2099
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Enterovirus A71 (EV-A71) is a positive-strand RNA virus that causes hand-foot-mouth disease and neurological complications in children and infants. Although the underlying mechanisms remain to be further defined, impaired immunity is thought to play an important role. The host zinc-finger antiviral protein (ZAP), an IFN-stimulated gene product, has been reported to specifically inhibit the replication of certain viruses. However, whether ZAP restricts the infection of enteroviruses remains unknown. Here, we report that EV-A71 infection upregulates ZAP mRNA in RD and HeLa cells. Moreover, ZAP overexpression rendered 293 T cells resistant to EV-A71 infection, whereas siRNA-mediated depletion of endogenous ZAP enhanced EV-A71 infection. The EV-A71 infection stimulated site-specific proteolysis of two ZAP isoforms, leading to the accumulation of a 40 kDa N-terminal ZAP fragment in virus-infected cells. We further revealed that the 3C protease (3Cpro) of EV-A71 mediates ZAP cleavage, which requires protease activity. Furthermore, ZAP variants with single amino acid substitutions at Gln-369 were resistant to 3Cpro cleavage, implying that Gln-369 is the sole cleavage site in ZAP. Moreover, although ZAP overexpression inhibited EV-A71 replication, the cleaved fragments did not show this effect. Our results indicate that an equilibrium between ZAP and enterovirus 3Cpro controls viral infection. The findings in this study suggest that viral 3Cpro mediated ZAP cleavage may represent a mechanism to escape host antiviral responses.
[Mh] Termos MeSH primário: Cisteína Endopeptidases/metabolismo
Enterovirus Humano A/enzimologia
Interações Hospedeiro-Patógeno
Proteínas de Ligação a RNA/metabolismo
Proteínas Virais/metabolismo
Replicação Viral
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Substituição de Aminoácidos
Animais
Linhagem Celular Tumoral
Cisteína Endopeptidases/genética
Enterovirus Humano A/genética
Regulação da Expressão Gênica
Genes Reporter
Células HEK293
Células HeLa
Seres Humanos
Luciferases/genética
Luciferases/metabolismo
Células Musculares/metabolismo
Células Musculares/virologia
Proteólise
RNA Interferente Pequeno/genética
RNA Interferente Pequeno/metabolismo
Proteínas de Ligação a RNA/antagonistas & inibidores
Proteínas de Ligação a RNA/genética
Células Sf9/imunologia
Células Sf9/virologia
Transdução de Sinais
Spodoptera
Proteínas Virais/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Small Interfering); 0 (RNA-Binding Proteins); 0 (Viral Proteins); 0 (ZC3HAV1 protein, human); EC 1.13.12.- (Luciferases); EC 3.4.22.- (Cysteine Endopeptidases); EC 3.4.22.28 (3C proteases)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171229
[Lr] Data última revisão:
171229
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171129
[St] Status:MEDLINE
[do] DOI:10.1099/jgv.0.000982


  7 / 1213 MEDLINE  
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[PMID]:28455446
[Au] Autor:Wang C; Sun M; Yuan X; Ji L; Jin Y; Cardona CJ; Xing Z
[Ad] Endereço:From the Medical School and Jiangsu Provincial Key Laboratory of Medicine, Nanjing University, Nanjing 210008, China.
[Ti] Título:Enterovirus 71 suppresses interferon responses by blocking Janus kinase (JAK)/signal transducer and activator of transcription (STAT) signaling through inducing karyopherin-α1 degradation.
[So] Source:J Biol Chem;292(24):10262-10274, 2017 06 16.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Enterovirus 71 (EV71) has emerged as one of the most important enteroviruses since the eradication of poliovirus, and it causes severe neurological symptoms for which no effective antiviral drugs are available. Type I interferons (IFN) α/ß have been used clinically as antiviral therapy as the first line of defense against virus infections successfully for decades. However, treatment with type I interferons has not been effective in patients with EV71 infection. In this study, we found that in cells pretreated with IFN-ß, EV71 infection could still lead to a cytopathic effect, and the viral replication was not affected. The mechanism by which EV71 antagonizes interferon signaling, however, has been controversial. Our study indicated that EV71 infection did not inhibit phosphorylation of STAT1/2 induced by IFN-ß stimulation, but p-STAT1/2 transport into the nucleus was significantly blocked. We showed that EV71 infection reduced the formation of STAT/karyopherin-α1 (KPNA1) complex upon interferon stimulation and that the virus down-regulated the expression of KPNA1, a nuclear localization signal receptor for p-STAT1. Using specific caspase inhibitors and siRNA for caspase-3, we demonstrated that EV71 infection induced degradation of cellular KPNA1 in a caspase-3-dependent manner, which led to decreased induction of interferon-inducible genes and IFN response. Viral 2A and 3C proteases did not degrade KPNA1, inhibit the activity of ISRE or suppress the transcription of interferon-inducible genes induced by IFN-ß. Our study demonstrates a novel mechanism by which antiviral signaling is suppressed through degradation of KPNA1 by activated caspase-3 induced in an enteroviral infection.
[Mh] Termos MeSH primário: Caspase 3/metabolismo
Enterócitos/virologia
Enterovirus Humano A/fisiologia
Interferon beta/metabolismo
Janus Quinase 1/metabolismo
Transdução de Sinais
alfa Carioferinas/antagonistas & inibidores
[Mh] Termos MeSH secundário: Transporte Ativo do Núcleo Celular
Animais
Caspase 3/química
Caspase 3/genética
Cercopithecus aethiops
Enterócitos/imunologia
Enterócitos/metabolismo
Enterovirus Humano A/crescimento & desenvolvimento
Células HT29
Células HeLa
Seres Humanos
Interferon beta/genética
Janus Quinase 1/genética
Fosforilação
Processamento de Proteína Pós-Traducional
Proteólise
Interferência de RNA
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Fator de Transcrição STAT1/metabolismo
Fator de Transcrição STAT2/metabolismo
Células Vero
Replicação Viral
alfa Carioferinas/genética
alfa Carioferinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (KPNA1 protein, human); 0 (Recombinant Fusion Proteins); 0 (STAT1 Transcription Factor); 0 (STAT1 protein, human); 0 (STAT2 Transcription Factor); 0 (STAT2 protein, human); 0 (alpha Karyopherins); 77238-31-4 (Interferon-beta); EC 2.7.10.2 (JAK1 protein, human); EC 2.7.10.2 (Janus Kinase 1); EC 3.4.22.- (CASP3 protein, human); EC 3.4.22.- (Caspase 3)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171228
[Lr] Data última revisão:
171228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170430
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.745729


  8 / 1213 MEDLINE  
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[PMID]:27771495
[Au] Autor:Karrasch M; Fischer E; Scholten M; Sauerbrei A; Henke A; Renz DM; Mentzel HJ; Böer K; Böttcher S; Diedrich S; Krumbholz A; Zell R
[Ad] Endereço:Institute of Medical Microbiology, Jena University Hospital, Jena, Germany. Electronic address: matthias.karrasch@med.uni-jena.de.
[Ti] Título:A severe pediatric infection with a novel enterovirus A71 strain, Thuringia, Germany.
[So] Source:J Clin Virol;84:90-95, 2016 11.
[Is] ISSN:1873-5967
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Infection by Enterovirus A71 (EV-A71) is an important cause of hand, foot, and mouth disease (HFMD). Outbreaks including severe cases with neurological and cardiopulmonary complications have been reported particularly from Southeast Asia. In Europe, the epidemiology of EV-A71 is not well understood. In summer 2015, a two-year-old girl from Thuringia, Germany, presented with rhombencephalitis/brainstem encephalitis associated with severe neurological and cardiopulmonary complications. EV-A71 was detected in stool and almost the entire viral genome was amplified and sequenced. While the capsid protein VP1-encoding region belongs to the EV-A71 subgenogroup C1, the 3D polymerase encoding region represents a unique lineage. Thus, the data suggest that the Thuringian EV-A71 sequence likely represents a recombinant. The case underlines the importance of intensified EV-A71 surveillance in Germany and Europe including analysis of full-genome data.
[Mh] Termos MeSH primário: Encefalite Viral/virologia
Enterovirus Humano A/isolamento & purificação
Infecções por Enterovirus/virologia
[Mh] Termos MeSH secundário: Proteínas do Capsídeo/genética
Pré-Escolar
Surtos de Doenças
Encefalite Viral/diagnóstico
Encefalite Viral/epidemiologia
Enterovirus Humano A/classificação
Enterovirus Humano A/genética
Enterovirus Humano A/patogenicidade
Infecções por Enterovirus/diagnóstico
Infecções por Enterovirus/epidemiologia
Fezes/virologia
Feminino
Genoma Viral
Alemanha/epidemiologia
Sequenciamento de Nucleotídeos em Larga Escala
Seres Humanos
Recombinação Genética
Estações do Ano
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Capsid Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171124
[Lr] Data última revisão:
171124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE


  9 / 1213 MEDLINE  
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[PMID]:28993196
[Au] Autor:Meng J; Yao Z; He Y; Zhang R; Yang H; Yao X; Chen L; Zhang H; Cheng J
[Ad] Endereço:Shenzhen Center for Disease Control and Prevention, Shenzhen, Guangdong, China.
[Ti] Título:Long non-coding RNA expression profiles in different severity EV71-infected hand foot and mouth disease patients.
[So] Source:Biochem Biophys Res Commun;493(4):1594-1600, 2017 Dec 02.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Enterovirus 71 (EV71) is associated with the severe hand foot and mouth disease (HFMD) outcomes, however the host-virus interaction mechanism and the pathogenesis remain poorly understood. Long non-coding RNAs (lncRNAs) are involved in variety physiological and pathological processes, but the functions of lncRNAs in EV71 infection remain elusive. Here we profiled the expression of lncRNAs in peripheral blood mononuclear cells (PBMCs) from EV71-infected mild patients, severe patients as well as the healthy controls, and identified 8541 lncRNAs were differentially expressed. Focused on the dynamic changed lncRNAs, we performed systematic bioinformatics analysis with Series Test of Cluster (STC) algorithm, Gene Ontology (GO) analysis, pathway analysis and lncRNA-mRNA co-expression network analysis, and revealed the potential functions and related pathways of these lncRNAs were associated with immunity and inflammation during the clinical process of EV71-infected HFMD. Among the significant dynamic changed lncRNAs, ten lncRNAs were screened whose expression were further validated in EV71-infected mild patients, severe patients and healthy control. These results shed light on the potential roles of lncRNAs in EV71-infected HFMD, especially in distinguishing the mild and severe cases for early diagnose and treatment, moreover, provide deeper insight into the mechanism of EV71-induced immune and inflammatory responses, as well as the pathogenesis of the imbalanced inflammation in severe EV71 infection.
[Mh] Termos MeSH primário: Enterovirus Humano A/patogenicidade
Doença de Mão, Pé e Boca/genética
Doença de Mão, Pé e Boca/virologia
RNA Longo não Codificante/genética
[Mh] Termos MeSH secundário: Animais
Estudos de Casos e Controles
Pré-Escolar
Biologia Computacional
Feminino
Ontologia Genética
Doença de Mão, Pé e Boca/sangue
Interações Hospedeiro-Patógeno/genética
Interações Hospedeiro-Patógeno/imunologia
Seres Humanos
Imunidade Inata/genética
Lactente
Leucócitos Mononucleares/imunologia
Leucócitos Mononucleares/metabolismo
Masculino
RNA Longo não Codificante/sangue
RNA Longo não Codificante/imunologia
Índice de Gravidade de Doença
Transcriptoma
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Long Noncoding)
[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:171011
[St] Status:MEDLINE


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[PMID]:28985237
[Au] Autor:Wang T; Wang B; Huang H; Zhang C; Zhu Y; Pei B; Cheng C; Sun L; Wang J; Jin Q; Zhao Z
[Ad] Endereço:MOH Key Laboratory of Systems Biology of Pathogens, Institute of Pathogen Biology, Chinese Academy of Medical Sciences & Peking Union Medical College, Beijing, PR China.
[Ti] Título:Enterovirus 71 protease 2Apro and 3Cpro differentially inhibit the cellular endoplasmic reticulum-associated degradation (ERAD) pathway via distinct mechanisms, and enterovirus 71 hijacks ERAD component p97 to promote its replication.
[So] Source:PLoS Pathog;13(10):e1006674, 2017 Oct.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Endoplasmic reticulum-associated degradation (ERAD) is an important function for cellular homeostasis. The mechanism of how picornavirus infection interferes with ERAD remains unclear. In this study, we demonstrated that enterovirus 71 (EV71) infection significantly inhibits cellular ERAD by targeting multiple key ERAD molecules with its proteases 2Apro and 3Cpro using different mechanisms. Ubc6e was identified as the key E2 ubiquitin-conjugating enzyme in EV71 disturbed ERAD. EV71 3Cpro cleaves Ubc6e at Q219G, Q260S, and Q273G. EV71 2Apro mainly inhibits the de novo synthesis of key ERAD molecules Herp and VIMP at the protein translational level. Herp differentially participates in the degradation of different glycosylated ERAD substrates α-1 antitrypsin Null Hong Kong (NHK) and the C-terminus of sonic hedgehog (SHH-C) via unknown mechanisms. p97 was identified as a host factor in EV71 replication; it redistributed and co-exists with the viral protein and other known replication-related molecules in EV71-induced replication organelles. Electron microscopy and multiple-color confocal assays also showed that EV71-induced membranous vesicles were closely associated with the endoplasmic reticulum (ER), and the ER membrane molecule RTN3 was redistributed to the viral replication complex during EV71 infection. Therefore, we propose that EV71 rearranges ER membranes and hijacks p97 from cellular ERAD to benefit its replication. These findings add to our understanding of how viruses disturb ERAD and provide potential anti-viral targets for EV71 infection.
[Mh] Termos MeSH primário: Endopeptidases/metabolismo
Degradação Associada com o Retículo Endoplasmático/fisiologia
Retículo Endoplasmático/enzimologia
Enterovirus Humano A/fisiologia
Ubiquitina-Proteína Ligases/metabolismo
Proteínas Virais/metabolismo
Replicação Viral
[Mh] Termos MeSH secundário: Seres Humanos
Proteínas de Membrana/metabolismo
Transporte Proteico/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Membrane Proteins); 0 (Viral Proteins); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 3.4.- (Endopeptidases)
[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:171007
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006674



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