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[PMID]:28467302
[Au] Autor:Rickgauer JP; Grigorieff N; Denk W
[Ad] Endereço:Howard Hughes Medical Institute, Ashburn, United States.
[Ti] Título:Single-protein detection in crowded molecular environments in cryo-EM images.
[So] Source:Elife;6, 2017 05 03.
[Is] ISSN:2050-084X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:We present an approach to study macromolecular assemblies by detecting component proteins' characteristic high-resolution projection patterns, calculated from their known 3D structures, in single electron cryo-micrographs. Our method detects single apoferritin molecules in vitreous ice with high specificity and determines their orientation and location precisely. Simulations show that high spatial-frequency information and-in the presence of protein background-a whitening filter are essential for optimal detection, in particular for images taken far from focus. Experimentally, we could detect small viral RNA polymerase molecules, distributed randomly among binding locations, inside rotavirus particles. Based on the currently attainable image quality, we estimate a threshold for detection that is 150 kDa in ice and 300 kDa in 100 nm thick samples of dense biological material.
[Mh] Termos MeSH primário: Microscopia Crioeletrônica/métodos
Processamento de Imagem Assistida por Computador/métodos
Imagem Individual de Molécula/métodos
[Mh] Termos MeSH secundário: RNA Replicase/ultraestrutura
Rotavirus/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 2.7.7.48 (RNA Replicase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE


  2 / 3508 MEDLINE  
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[PMID]:29338047
[Au] Autor:Hsia HP; Yang YH; Szeto WC; Nilsson BE; Lo CY; Ng AK; Fodor E; Shaw PC
[Ad] Endereço:Centre for Protein Science and Crystallography, School of Life Sciences, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong, China.
[Ti] Título:Amino acid substitutions affecting aspartic acid 605 and valine 606 decrease the interaction strength between the influenza virus RNA polymerase PB2 '627' domain and the viral nucleoprotein.
[So] Source:PLoS One;13(1):e0191226, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The influenza virus RNA genome is transcribed and replicated in the context of the viral ribonucleoprotein (vRNP) complex by the viral RNA polymerase. The nucleoprotein (NP) is the structural component of the vRNP providing a scaffold for the viral RNA. In the vRNP as well as during transcription and replication the viral polymerase interacts with NP but it is unclear which parts of the polymerase and NP mediate these interactions. Previously the C-terminal '627' domain (amino acids 538-693) of PB2 was shown to interact with NP. Here we report that a fragment encompassing amino acids 146-185 of NP is sufficient to mediate this interaction. Using NMR chemical shift perturbation assays we show that amino acid region 601 to 607 of the PB2 '627' domain interacts with this fragment of NP. Substitutions of these PB2 amino acids resulted in diminished RNP activity and surface plasmon resonance assays showed that amino acids D605 was essential for the interaction with NP and V606 may also play a partial role in the interaction. Collectively these results reveal a possible interaction surface between NP and the PB2 subunit of the RNA polymerase complex.
[Mh] Termos MeSH primário: Vírus da Influenza A Subtipo H5N1/química
Vírus da Influenza A Subtipo H5N1/genética
RNA Replicase/química
RNA Replicase/genética
Proteínas de Ligação a RNA/química
Proteínas de Ligação a RNA/genética
Proteínas do Core Viral/química
Proteínas do Core Viral/genética
Proteínas Virais/química
Proteínas Virais/genética
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Ácido Aspártico/química
Genoma Viral
Células HEK293
Seres Humanos
Vírus da Influenza A Subtipo H5N1/fisiologia
Influenza Humana/virologia
Modelos Moleculares
Ressonância Magnética Nuclear Biomolecular
Domínios e Motivos de Interação entre Proteínas
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Ressonância de Plasmônio de Superfície
Valina/química
Replicação Viral
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (NP protein, Influenza A virus); 0 (PB2 protein, Influenzavirus A); 0 (RNA-Binding Proteins); 0 (Recombinant Proteins); 0 (Viral Core Proteins); 0 (Viral Proteins); 30KYC7MIAI (Aspartic Acid); EC 2.7.7.48 (RNA Replicase); HG18B9YRS7 (Valine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180117
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191226


  3 / 3508 MEDLINE  
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[PMID]:29214362
[Au] Autor:Zhuo T; Zhu LJ; Lu CC; Jiang CY; Chen ZY; Zhang G; Wang ZH; Jovel J; Han YH
[Ad] Endereço:College of Plant Protection, Fujian Agriculture and Forestry University, Fuzhou, 350002, China.
[Ti] Título:Complete nucleotide sequence of jasmine virus H, a new member of the family Tombusviridae.
[So] Source:Arch Virol;163(3):731-735, 2018 Mar.
[Is] ISSN:1432-8798
[Cp] País de publicação:Austria
[La] Idioma:eng
[Ab] Resumo:Jasmine virus H (JaVH) is a novel virus associated with symptoms of yellow mosaic on jasmine. The JaVH genome is 3,867 nt in length with five open reading frames (ORFs) encoding a 27-kDa protein (ORF 1), an 87-kDa replicase protein (ORF 2), two centrally located movement proteins (ORF 3 and 4), and a 37-kDa capsid protein (ORF 5). Based on genomic and phylogenetic analysis, JaVH is predicted to be a member of the genus Pelarspovirus in the family Tombusviridae.
[Mh] Termos MeSH primário: Genoma Viral
Jasminum/virologia
Filogenia
RNA Viral/genética
Tombusviridae/genética
[Mh] Termos MeSH secundário: Sequência de Bases
Proteínas do Capsídeo/genética
Sequenciamento de Nucleotídeos em Larga Escala
Fases de Leitura Aberta
RNA Replicase/genética
Tombusviridae/classificação
Tombusviridae/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Capsid Proteins); 0 (RNA, Viral); EC 2.7.7.48 (RNA Replicase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171208
[St] Status:MEDLINE
[do] DOI:10.1007/s00705-017-3663-z


  4 / 3508 MEDLINE  
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[PMID]:29283993
[Au] Autor:Chinello P; Petrosillo N; Pittalis S; Biava G; Ippolito G; Nicastri E; INMI Ebola Team
[Ad] Endereço:Lazzaro Spallanzani National Institute for Infectious Diseases (INMI), IRCCS, Rome, Italy.
[Ti] Título:QTc interval prolongation during favipiravir therapy in an Ebolavirus-infected patient.
[So] Source:PLoS Negl Trop Dis;11(12):e0006034, 2017 12.
[Is] ISSN:1935-2735
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Amidas/efeitos adversos
Amidas/uso terapêutico
Antivirais/efeitos adversos
Antivirais/uso terapêutico
Arritmias Cardíacas/induzido quimicamente
Doença pelo Vírus Ebola/tratamento farmacológico
Pirazinas/efeitos adversos
Pirazinas/uso terapêutico
[Mh] Termos MeSH secundário: Adulto
Ebolavirus/efeitos dos fármacos
Ebolavirus/patogenicidade
Eletrocardiografia
Doença pelo Vírus Ebola/virologia
Seres Humanos
Itália
Levofloxacino/efeitos adversos
Levofloxacino/uso terapêutico
Masculino
RNA Replicase/antagonistas & inibidores
Replicação Viral/efeitos dos fármacos
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amides); 0 (Antiviral Agents); 0 (Pyrazines); 6GNT3Y5LMF (Levofloxacin); EC 2.7.7.48 (RNA Replicase); EW5GL2X7E0 (favipiravir)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180130
[Lr] Data última revisão:
180130
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171229
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pntd.0006034


  5 / 3508 MEDLINE  
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[PMID]:29261807
[Au] Autor:Khamina K; Lercher A; Caldera M; Schliehe C; Vilagos B; Sahin M; Kosack L; Bhattacharya A; Májek P; Stukalov A; Sacco R; James LC; Pinschewer DD; Bennett KL; Menche J; Bergthaler A
[Ad] Endereço:CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, Lazarettgasse, Vienna, Austria.
[Ti] Título:Characterization of host proteins interacting with the lymphocytic choriomeningitis virus L protein.
[So] Source:PLoS Pathog;13(12):e1006758, 2017 Dec.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:RNA-dependent RNA polymerases (RdRps) play a key role in the life cycle of RNA viruses and impact their immunobiology. The arenavirus lymphocytic choriomeningitis virus (LCMV) strain Clone 13 provides a benchmark model for studying chronic infection. A major genetic determinant for its ability to persist maps to a single amino acid exchange in the viral L protein, which exhibits RdRp activity, yet its functional consequences remain elusive. To unravel the L protein interactions with the host proteome, we engineered infectious L protein-tagged LCMV virions by reverse genetics. A subsequent mass-spectrometric analysis of L protein pulldowns from infected human cells revealed a comprehensive network of interacting host proteins. The obtained LCMV L protein interactome was bioinformatically integrated with known host protein interactors of RdRps from other RNA viruses, emphasizing interconnected modules of human proteins. Functional characterization of selected interactors highlighted proviral (DDX3X) as well as antiviral (NKRF, TRIM21) host factors. To corroborate these findings, we infected Trim21-/- mice with LCMV and found impaired virus control in chronic infection. These results provide insights into the complex interactions of the arenavirus LCMV and other viral RdRps with the host proteome and contribute to a better molecular understanding of how chronic viruses interact with their host.
[Mh] Termos MeSH primário: RNA Helicases DEAD-box/metabolismo
Vírus da Coriomeningite Linfocítica/enzimologia
Modelos Moleculares
RNA Replicase/metabolismo
Proteínas Repressoras/metabolismo
Ribonucleoproteínas/metabolismo
Proteínas Virais/metabolismo
[Mh] Termos MeSH secundário: Animais
Sistemas CRISPR-Cas
Biologia Computacional
Cruzamentos Genéticos
RNA Helicases DEAD-box/química
Feminino
Células HEK293
Seres Humanos
Imunoprecipitação
Coriomeningite Linfocítica/metabolismo
Coriomeningite Linfocítica/veterinária
Masculino
Camundongos Endogâmicos C57BL
Camundongos Knockout
Domínios e Motivos de Interação entre Proteínas
RNA Replicase/química
RNA Replicase/genética
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Proteínas Repressoras/química
Ribonucleoproteínas/química
Ribonucleoproteínas/genética
Organismos Livres de Patógenos Específicos
Proteínas Virais/química
Proteínas Virais/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; VALIDATION STUDIES
[Nm] Nome de substância:
0 (NKRF protein, human); 0 (Recombinant Fusion Proteins); 0 (Repressor Proteins); 0 (Ribonucleoproteins); 0 (SS-A antigen); 0 (Viral Proteins); EC 2.7.7.48 (RNA Replicase); EC 3.6.1.- (DDX3X protein, human); EC 3.6.4.13 (DEAD-box RNA Helicases)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180109
[Lr] Data última revisão:
180109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171221
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006758


  6 / 3508 MEDLINE  
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[PMID]:28460010
[Au] Autor:de la Higuera I; Ferrer-Orta C; de Ávila AI; Perales C; Sierra M; Singh K; Sarafianos SG; Dehouck Y; Bastolla U; Verdaguer N; Domingo E
[Ad] Endereço:Centro de Biología Molecular "Severo Ochoa" (CSIC-UAM), Consejo Superior de Investigaciones Científicas (CSIC), Campus de Cantoblanco, Madrid, Spain.
[Ti] Título:Molecular and Functional Bases of Selection against a Mutation Bias in an RNA Virus.
[So] Source:Genome Biol Evol;9(5):1212-1228, 2017 05 01.
[Is] ISSN:1759-6653
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The selective pressures acting on viruses that replicate under enhanced mutation rates are largely unknown. Here, we describe resistance of foot-and-mouth disease virus to the mutagen 5-fluorouracil (FU) through a single polymerase substitution that prevents an excess of A to G and U to C transitions evoked by FU on the wild-type foot-and-mouth disease virus, while maintaining the same level of mutant spectrum complexity. The polymerase substitution inflicts upon the virus a fitness loss during replication in absence of FU but confers a fitness gain in presence of FU. The compensation of mutational bias was documented by in vitro nucleotide incorporation assays, and it was associated with structural modifications at the N-terminal region and motif B of the viral polymerase. Predictions of the effect of mutations that increase the frequency of G and C in the viral genome and encoded polymerase suggest multiple points in the virus life cycle where the mutational bias in favor of G and C may be detrimental. Application of predictive algorithms suggests adverse effects of the FU-directed mutational bias on protein stability. The results reinforce modulation of nucleotide incorporation as a lethal mutagenesis-escape mechanism (that permits eluding virus extinction despite replication in the presence of a mutagenic agent) and suggest that mutational bias can be a target of selection during virus replication.
[Mh] Termos MeSH primário: Substituição de Aminoácidos
Vírus da Febre Aftosa/genética
Mutação
[Mh] Termos MeSH secundário: Linhagem Celular
Fluoruracila/metabolismo
Vírus da Febre Aftosa/enzimologia
Vírus da Febre Aftosa/fisiologia
Aptidão Genética
Cinética
Modelos Moleculares
Dobramento de Proteína
RNA Replicase/genética
RNA Replicase/metabolismo
Replicação Viral
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 2.7.7.48 (RNA Replicase); U3P01618RT (Fluorouracil)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171206
[Lr] Data última revisão:
171206
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170502
[St] Status:MEDLINE
[do] DOI:10.1093/gbe/evx075


  7 / 3508 MEDLINE  
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[PMID]:29059239
[Au] Autor:Prasanth KR; Chuang C; Nagy PD
[Ad] Endereço:Department of Plant Pathology, University of Kentucky, Plant Science Building, Lexington, KY, United States of America.
[Ti] Título:Co-opting ATP-generating glycolytic enzyme PGK1 phosphoglycerate kinase facilitates the assembly of viral replicase complexes.
[So] Source:PLoS Pathog;13(10):e1006689, 2017 Oct.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The intricate interactions between viruses and hosts include exploitation of host cells for viral replication by using many cellular resources, metabolites and energy. Tomato bushy stunt virus (TBSV), similar to other (+)RNA viruses, induces major changes in infected cells that lead to the formation of large replication compartments consisting of aggregated peroxisomal and ER membranes. Yet, it is not known how TBSV obtains the energy to fuel these energy-consuming processes. In the current work, the authors discovered that TBSV co-opts the glycolytic ATP-generating Pgk1 phosphoglycerate kinase to facilitate the assembly of new viral replicase complexes. The recruitment of Pgk1 into the viral replication compartment is through direct interaction with the viral replication proteins. Altogether, we provide evidence that the ATP generated locally within the replication compartment by the co-opted Pgk1 is used to fuel the ATP-requirement of the co-opted heat shock protein 70 (Hsp70) chaperone, which is essential for the assembly of new viral replicase complexes and the activation of functional viral RNA-dependent RNA polymerase. The advantage of direct recruitment of Pgk1 into the virus replication compartment could be that the virus replicase assembly does not need to intensively compete with cellular processes for access to ATP. In addition, local production of ATP within the replication compartment could greatly facilitate the efficiency of Hsp70-driven replicase assembly by providing high ATP concentration within the replication compartment.
[Mh] Termos MeSH primário: Interações Hospedeiro-Patógeno/fisiologia
Fosfoglicerato Quinase/metabolismo
Tombusvirus/crescimento & desenvolvimento
Montagem de Vírus/fisiologia
[Mh] Termos MeSH secundário: RNA Replicase/metabolismo
Saccharomyces cerevisiae
Tabaco/virologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.7.2.3 (Phosphoglycerate Kinase); EC 2.7.7.48 (RNA Replicase)
[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:171024
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006689


  8 / 3508 MEDLINE  
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[PMID]:28933688
[Au] Autor:Luna AP; Rodríguez-Negrete EA; Morilla G; Wang L; Lozano-Durán R; Castillo AG; Bejarano ER
[Ad] Endereço:1​Instituto de Hortofruticultura Subtropical y Mediterránea 'La Mayora' (IHSM-UMA-CSIC), Area de Genética, Facultad de Ciencias, Universidad de Málaga, Campus de Teatinos s/n, E-29071 Málaga, Spain.
[Ti] Título:V2 from a curtovirus is a suppressor of post-transcriptional gene silencing.
[So] Source:J Gen Virol;98(10):2607-2614, 2017 Oct.
[Is] ISSN:1465-2099
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The suppression of gene silencing is a key mechanism for the success of viral infection in plants. DNA viruses from the Geminiviridae family encode several proteins that suppress transcriptional and post-transcriptional gene silencing (TGS/PTGS). In Begomovirus, the most abundant genus of this family, three out of six genome-encoded proteins, namely C2, C4 and V2, have been shown to suppress PTGS, with V2 being the strongest PTGS suppressor in transient assays. Beet curly top virus (BCTV), the model species for the Curtovirus genus, is able to infect the widest range of plants among geminiviruses. In this genus, only one protein, C2/L2, has been described as inhibiting PTGS. We show here that, despite the lack of sequence homology with its begomoviral counterpart, BCTV V2 acts as a potent PTGS suppressor, possibly by impairing the RDR6 (RNA-dependent RNA polymerase 6)/suppressor of gene silencing 3 (SGS3) pathway.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/genética
Begomovirus/genética
Interferência de RNA/fisiologia
RNA Replicase/metabolismo
Proteínas Virais/genética
[Mh] Termos MeSH secundário: Arabidopsis/virologia
Proteínas de Arabidopsis/metabolismo
Doenças das Plantas/virologia
Plantas Geneticamente Modificadas/genética
Plantas Geneticamente Modificadas/virologia
RNA Replicase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (SGS3 protein, Arabidopsis); 0 (Viral Proteins); EC 2.7.7.48 (RDR6 protein, Arabidopsis); EC 2.7.7.48 (RNA Replicase)
[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:170922
[St] Status:MEDLINE
[do] DOI:10.1099/jgv.0.000933


  9 / 3508 MEDLINE  
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[PMID]:28866238
[Au] Autor:Chen W; Xu Q; Zhong Y; Yu H; Shu J; Ma T; Li Z
[Ad] Endereço:Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi'an 710069, PR China.
[Ti] Título:Genetic variation and co-evolutionary relationship of RNA polymerase complex segments in influenza A viruses.
[So] Source:Virology;511:193-206, 2017 Nov.
[Is] ISSN:1096-0341
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The RNA polymerase complex (RNApc) in influenza A viruses (IVs) is composed of the PB2, PB1 and PA subunits, which are encoded by the three longest genome segments (Seg1-3) and are responsible for the replication of vRNAs and transcription of viral mRNAs. However, the co-evolutionary relationships of the three segments from the known 126 subtypes IVs are unclear. In this study, we performed a detailed analysis based on a total number of 121,191 nucleotide sequences. Three segment sequences were aligned before the repeated, incomplete and mixed sequences were removed for homologous and phylogenetic analyses. Subsequently, the estimated substitution rates and TMRCAs (Times for Most Recent Common Ancestor) were calculated by 175 representative IVs. Tracing the cladistic distribution of three segments from these IVs, co-evolutionary patterns and trajectories could be inferred. The further correlation analysis of six internal protein coding segments reflect the RNApc segments have the closer correlation than others during continuous reassortments. This global approach facilitates the establishment of a fast antiviral strategy and monitoring of viral variation.
[Mh] Termos MeSH primário: Evolução Molecular
Variação Genética
Vírus da Influenza A/enzimologia
Vírus da Influenza A/genética
RNA Replicase/genética
Proteínas Virais/genética
[Mh] Termos MeSH secundário: Biologia Computacional
Filogenia
Análise de Sequência de DNA
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (PA protein, influenza viruses); 0 (PB2 protein, Influenzavirus A); 0 (Viral Proteins); 0 (influenza virus polymerase basic protein 1); EC 2.7.7.48 (RNA Replicase)
[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:170904
[St] Status:MEDLINE


  10 / 3508 MEDLINE  
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Alfieri, Alice Fernandes
Alfieri, Amauri Alcindo
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[PMID]:28849283
[Au] Autor:Ribeiro J; Lorenzetti E; Júnior JCR; da Silva Medeiros TN; Alfieri AF; Alfieri AA
[Ad] Endereço:Laboratory of Animal Virology, Molecular Biology Unit, Department of Veterinary Preventive Medicine, Universidade Estadual de Londrina, Rodovia Celso Garcia Cid, Campus Universitário, PO Box 10011, CEP 86057-970, Londrina, PR, Brazil.
[Ti] Título:Phylogenetic analysis of VP1 and RdRP genes of Brazilian aichivirus B strains involved in a diarrhea outbreak in dairy calves.
[So] Source:Arch Virol;162(12):3691-3696, 2017 Dec.
[Is] ISSN:1432-8798
[Cp] País de publicação:Austria
[La] Idioma:eng
[Ab] Resumo:Aichivirus B has been reported worldwide in calves and adult cattle with and without diarrhea. The aim of this study was to describe the molecular characteristics of the RdRP and VP1 genes of aichivirus B strains identified as the most frequent etiologic agent in a neonatal diarrhea outbreak in a high-production Brazilian dairy cattle herd. Preliminary laboratory analysis ruled out important enteropathogens (Cryptosporidium spp; Eimeria spp., E. coli F5, and bovine coronavirus). Fecal samples from diarrheic (n = 24) and asymptomatic (n = 5) calves up to 30 days old were collected for virological analysis. RT-PCR assays were performed for the detection of aichivirus B RdRP and VP1 genes and for rotavirus A VP7 and VP4 genes in fecal samples. Asymptomatic calves (control group) were negative for both viruses. Aichivirus B and rotavirus A G10P[11] genotypes were found in 54.2% (13/24) and 25% (6/24) of the diarrheic fecal samples, respectively. Aichivirus B was only identified (83.3%, 10/12) in calves up to two weeks old. Phylogenetic analysis based on the RdRP gene grouped the Brazilian strains in a new branch within the aichivirus B group. Comparative analysis of the nucleotide sequence of the VP1 gene of Brazilian and Chinese aichivirus B strains allowed the strains identified in this study to be classified in the putative lineage 1. This is the first description of a high rate of aichivirus B detection in a diarrhea outbreak in dairy calves, and the first phylogenetic study of the VP1 gene of aichivirus B wild-type strains performed in South America.
[Mh] Termos MeSH primário: Doenças dos Bovinos/virologia
Diarreia/veterinária
Surtos de Doenças
Kobuvirus/classificação
Kobuvirus/isolamento & purificação
Filogenia
Infecções por Picornaviridae/veterinária
[Mh] Termos MeSH secundário: Animais
Brasil/epidemiologia
Bovinos
Doenças dos Bovinos/epidemiologia
Diarreia/epidemiologia
Diarreia/virologia
Kobuvirus/genética
Infecções por Picornaviridae/epidemiologia
Infecções por Picornaviridae/virologia
RNA Replicase/genética
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Homologia de Sequência
Proteínas Estruturais Virais/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Viral Structural Proteins); EC 2.7.7.48 (RNA Replicase)
[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:170830
[St] Status:MEDLINE
[do] DOI:10.1007/s00705-017-3531-x



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