Base de dados : MEDLINE
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[PMID]:29382836
[Au] Autor:Füzik T; Formanová P; Ruzek D; Yoshii K; Niedrig M; Plevka P
[Ad] Endereço:Structural Virology, Central European Institute of Technology, Masaryk University, Kamenice 753/5, 62500, Brno, Czech Republic.
[Ti] Título:Structure of tick-borne encephalitis virus and its neutralization by a monoclonal antibody.
[So] Source:Nat Commun;9(1):436, 2018 01 30.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Tick-borne encephalitis virus (TBEV) causes 13,000 cases of human meningitis and encephalitis annually. However, the structure of the TBEV virion and its interactions with antibodies are unknown. Here, we present cryo-EM structures of the native TBEV virion and its complex with Fab fragments of neutralizing antibody 19/1786. Flavivirus genome delivery depends on membrane fusion that is triggered at low pH. The virion structure indicates that the repulsive interactions of histidine side chains, which become protonated at low pH, may contribute to the disruption of heterotetramers of the TBEV envelope and membrane proteins and induce detachment of the envelope protein ectodomains from the virus membrane. The Fab fragments bind to 120 out of the 180 envelope glycoproteins of the TBEV virion. Unlike most of the previously studied flavivirus-neutralizing antibodies, the Fab fragments do not lock the E-proteins in the native-like arrangement, but interfere with the process of virus-induced membrane fusion.
[Mh] Termos MeSH primário: Anticorpos Neutralizantes/química
Anticorpos Antivirais/química
Vírus da Encefalite Transmitidos por Carrapatos/ultraestrutura
Fragmentos Fab das Imunoglobulinas/química
Proteínas Virais/química
Vírion/ultraestrutura
[Mh] Termos MeSH secundário: Anticorpos Neutralizantes/biossíntese
Anticorpos Antivirais/biossíntese
Linhagem Celular Tumoral
Microscopia Crioeletrônica
Vírus da Encefalite Transmitidos por Carrapatos/genética
Vírus da Encefalite Transmitidos por Carrapatos/metabolismo
Expressão Gênica
Seres Humanos
Concentração de Íons de Hidrogênio
Fragmentos Fab das Imunoglobulinas/biossíntese
Fusão de Membrana/genética
Neurônios/patologia
Neurônios/virologia
Domínios Proteicos
Multimerização Proteica
Proteínas Virais/genética
Proteínas Virais/metabolismo
Vírion/genética
Vírion/metabolismo
Internalização do Vírus
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibodies, Neutralizing); 0 (Antibodies, Viral); 0 (Immunoglobulin Fab Fragments); 0 (Viral Proteins)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180307
[Lr] Data última revisão:
180307
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180201
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-018-02882-0


  2 / 11417 MEDLINE  
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[PMID]:28461070
[Au] Autor:Albulescu IC; Kovacikova K; Tas A; Snijder EJ; van Hemert MJ
[Ad] Endereço:Molecular Virology Laboratory, Department of Medical Microbiology, Leiden University Medical Center, Leiden, The Netherlands.
[Ti] Título:Suramin inhibits Zika virus replication by interfering with virus attachment and release of infectious particles.
[So] Source:Antiviral Res;143:230-236, 2017 07.
[Is] ISSN:1872-9096
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Zika virus (ZIKV) is a mosquito-borne flavivirus that mostly causes asymptomatic infections or mild disease characterized by low-grade fever, rash, conjunctivitis, and malaise. However, the recent massive ZIKV epidemics in the Americas have also linked ZIKV infection to fetal malformations like microcephaly and Guillain-Barré syndrome in adults, and have uncovered previously unrecognized routes of vertical and sexual transmission. Here we describe inhibition of ZIKV replication by suramin, originally an anti-parasitic drug, which was more recently shown to inhibit multiple viruses. In cell culture-based assays, using reduction of cytopathic effect as read-out, suramin had an EC of ∼40 µM and a selectivity index of 48. In single replication cycle experiments, suramin treatment also caused a strong dose-dependent decrease in intracellular ZIKV RNA levels and a >3-log reduction in infectious progeny titers. Time-of-addition experiments revealed that suramin inhibits a very early step of the replication cycle as well as the release of infectious progeny. Only during the first 2 h of infection suramin treatment strongly reduced the fraction of cells that became infected with ZIKV, suggesting the drug affects virus binding/entry. Binding experiments at 4 °C using S-labeled ZIKV demonstrated that suramin interferes with attachment to host cells. When suramin treatment was initiated post-entry, viral RNA synthesis was unaffected, while both the release of genomes and the infectivity of ZIKV were reduced. This suggests the compound also affects virion biogenesis, possibly by interfering with glycosylation and the maturation of ZIKV during its traffic through the secretory pathway. The inhibitory effect of suramin on ZIKV attachment and virion biogenesis and its broad-spectrum activity warrant further evaluation of this compound as a potential therapeutic.
[Mh] Termos MeSH primário: Suramina/antagonistas & inibidores
Vírion/efeitos dos fármacos
Ligação Viral/efeitos dos fármacos
Liberação de Vírus/efeitos dos fármacos
Replicação Viral/efeitos dos fármacos
Zika virus/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Cercopithecus aethiops
Efeito Citopatogênico Viral/efeitos dos fármacos
Replicação do DNA/efeitos dos fármacos
Flavivirus/efeitos dos fármacos
Glicosilação/efeitos dos fármacos
Ácido Micofenólico/administração & dosagem
Ácido Micofenólico/antagonistas & inibidores
RNA Viral/análise
RNA Viral/biossíntese
RNA Viral/efeitos dos fármacos
Suramina/administração & dosagem
Fatores de Tempo
Células Vero
Internalização do Vírus/efeitos dos fármacos
Zika virus/crescimento & desenvolvimento
Zika virus/fisiologia
Infecção pelo Zika virus/tratamento farmacológico
Infecção pelo Zika virus/virologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (RNA, Viral); 6032D45BEM (Suramin); HU9DX48N0T (Mycophenolic Acid)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180213
[Lr] Data última revisão:
180213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE


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[PMID]:29235442
[Au] Autor:Li S; Erdemci-Tandogan G; van der Schoot P; Zandi R
[Ad] Endereço:Department of Physics and Astronomy, University of California, Riverside, CA 92521, United States of America.
[Ti] Título:The effect of RNA stiffness on the self-assembly of virus particles.
[So] Source:J Phys Condens Matter;30(4):044002, 2018 Jan 31.
[Is] ISSN:1361-648X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Under many in vitro conditions, some small viruses spontaneously encapsidate a single stranded (ss) RNA into a protein shell called the capsid. While viral RNAs are found to be compact and highly branched because of long distance base-pairing between nucleotides, recent experiments reveal that in a head-to-head competition between an ssRNA with no secondary or higher order structure and a viral RNA, the capsid proteins preferentially encapsulate the linear polymer! In this paper, we study the impact of genome stiffness on the encapsidation free energy of the complex of RNA and capsid proteins. We show that an increase in effective chain stiffness because of base-pairing could be the reason why under certain conditions linear chains have an advantage over branched chains when it comes to encapsidation efficiency. While branching makes the genome more compact, RNA base-pairing increases the effective Kuhn length of the RNA molecule, which could result in an increase of the free energy of RNA confinement, that is, the work required to encapsidate RNA, and thus less efficient packaging.
[Mh] Termos MeSH primário: Pareamento de Bases
Proteínas do Capsídeo/metabolismo
RNA Viral/química
Vírion/química
[Mh] Termos MeSH secundário: Capsídeo
Conformação de Ácido Nucleico
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Capsid Proteins); 0 (RNA, Viral)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180209
[Lr] Data última revisão:
180209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171214
[St] Status:MEDLINE
[do] DOI:10.1088/1361-648X/aaa159


  4 / 11417 MEDLINE  
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[PMID]:29074234
[Au] Autor:Sasaki M; Anindita PD; Phongphaew W; Carr M; Kobayashi S; Orba Y; Sawa H
[Ad] Endereço:Division of Molecular Pathobiology, Research Center for Zoonosis Control, Hokkaido University, Sapporo 001-0020, Japan.
[Ti] Título:Development of a rapid and quantitative method for the analysis of viral entry and release using a NanoLuc luciferase complementation assay.
[So] Source:Virus Res;243:69-74, 2018 01 02.
[Is] ISSN:1872-7492
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Subviral particles (SVPs) self-assemble and are released from cells transfected with expression plasmids encoding flavivirus structural proteins. Flavivirus-like particles (VLPs), consisting of flavivirus structural proteins and a subgenomic replicon, can enter cells and cause single-round infections. Neither SVPs or VLPs possess complete viral RNA genomes, therefore are replication-incompetent systems; however, they retain the capacity to fuse and bud from target cells and follow the same maturation process as whole virions. SVPs and VLPs have been previously employed in studies analyzing entry and release steps of viral life cycles. In this study, we have developed quantitative methods for the detection of cellular entry and release of SVPs and VLPs by applying a luciferase complementation assay based on the high affinity interaction between the split NanoLuc luciferase protein, LgBiT and the small peptide, HiBiT. We introduced HiBiT into the structural protein of West Nile virus and generated SVPs and VLPs harboring HiBiT (SVP-HiBiT and VLP-HiBiT, respectively). As SVP-HiBiT emitted strong luminescence upon exposure to LgBiT and its substrate, the nascently budded SVP-HiBiT in the supernatant was readily quantified by luminometry. Similarly, the cellular entry of VLP-HiBiT generated luminescence when VLP-HiBiT was infected into LgBiT-expressing cells. These methods utilizing SVP-HiBiT and VLP-HiBiT will facilitate research into life cycles of flaviviruses, including WNV.
[Mh] Termos MeSH primário: Luciferases/análise
Vírion/fisiologia
Virologia/métodos
Internalização do Vírus
Liberação de Vírus
Vírus do Nilo Ocidental/fisiologia
[Mh] Termos MeSH secundário: Linhagem Celular
Seres Humanos
Luciferases/genética
Luciferases/metabolismo
Vírion/genética
Febre do Nilo Ocidental/virologia
Vírus do Nilo Ocidental/genética
[Pt] Tipo de publicação:EVALUATION STUDIES; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 1.13.12.- (Luciferases)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180209
[Lr] Data última revisão:
180209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171028
[St] Status:MEDLINE


  5 / 11417 MEDLINE  
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[PMID]:28463988
[Au] Autor:Calton CM; Bronnimann MP; Manson AR; Li S; Chapman JA; Suarez-Berumen M; Williamson TR; Molugu SK; Bernal RA; Campos SK
[Ad] Endereço:BIO5 Institute, University of Arizona, Tucson, Arizona, United States of America.
[Ti] Título:Translocation of the papillomavirus L2/vDNA complex across the limiting membrane requires the onset of mitosis.
[So] Source:PLoS Pathog;13(5):e1006200, 2017 May.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The human papillomavirus type 16 (HPV16) L2 protein acts as a chaperone to ensure that the viral genome (vDNA) traffics from endosomes to the trans-Golgi network (TGN) and eventually the nucleus, where HPV replication occurs. En route to the nucleus, the L2/vDNA complex must translocate across limiting intracellular membranes. The details of this critical process remain poorly characterized. We have developed a system based on subcellular compartmentalization of the enzyme BirA and its cognate substrate to detect membrane translocation of L2-BirA from incoming virions. We find that L2 translocation requires transport to the TGN and is strictly dependent on entry into mitosis, coinciding with mitotic entry in synchronized cells. Cell cycle arrest causes retention of L2/vDNA at the TGN; only release and progression past G2/M enables translocation across the limiting membrane and subsequent infection. Microscopy of EdU-labeled vDNA reveals a rapid and dramatic shift in vDNA localization during early mitosis. At late G2/early prophase vDNA egresses from the TGN to a pericentriolar location, accumulating there through prometaphase where it begins to associate with condensed chromosomes. By metaphase and throughout anaphase the vDNA is seen bound to the mitotic chromosomes, ensuring distribution into both daughter nuclei. Mutations in a newly defined chromatin binding region of L2 potently blocked translocation, suggesting that translocation is dependent on chromatin binding during prometaphase. This represents the first time a virus has been shown to functionally couple the penetration of limiting membranes to cellular mitosis, explaining in part the tropism of HPV for mitotic basal keratinocytes.
[Mh] Termos MeSH primário: Proteínas do Capsídeo/metabolismo
Genoma Viral/genética
Papillomavirus Humano 16/fisiologia
Mitose
Proteínas Oncogênicas Virais/metabolismo
Infecções por Papillomavirus/virologia
[Mh] Termos MeSH secundário: Transporte Biológico
Proteínas do Capsídeo/genética
Pontos de Checagem do Ciclo Celular
Linhagem Celular
Núcleo Celular/metabolismo
Núcleo Celular/virologia
DNA Viral/genética
DNA Viral/metabolismo
Endossomos/metabolismo
Endossomos/virologia
Papillomavirus Humano 16/genética
Seres Humanos
Queratinócitos/virologia
Mutação
Proteínas Oncogênicas Virais/genética
Tropismo Viral
Vírion
Internalização do Vírus
Rede trans-Golgi/metabolismo
Rede trans-Golgi/virologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Capsid Proteins); 0 (DNA, Viral); 0 (L2 protein, Human papillomavirus type 16); 0 (Oncogene Proteins, Viral)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006200


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[PMID]:29220409
[Au] Autor:Mata CP; Luque D; Gómez-Blanco J; Rodríguez JM; González JM; Suzuki N; Ghabrial SA; Carrascosa JL; Trus BL; Castón JR
[Ad] Endereço:Department of Structure of Macromolecules, Centro Nacional de Biotecnología (CNB-CSIC), Campus Cantoblanco, Madrid, Spain.
[Ti] Título:Acquisition of functions on the outer capsid surface during evolution of double-stranded RNA fungal viruses.
[So] Source:PLoS Pathog;13(12):e1006755, 2017 Dec.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Unlike their counterparts in bacterial and higher eukaryotic hosts, most fungal viruses are transmitted intracellularly and lack an extracellular phase. Here we determined the cryo-EM structure at 3.7 Å resolution of Rosellinia necatrix quadrivirus 1 (RnQV1), a fungal double-stranded (ds)RNA virus. RnQV1, the type species of the family Quadriviridae, has a multipartite genome consisting of four monocistronic segments. Whereas most dsRNA virus capsids are based on dimers of a single protein, the ~450-Å-diameter, T = 1 RnQV1 capsid is built of P2 and P4 protein heterodimers, each with more than 1000 residues. Despite a lack of sequence similarity between the two proteins, they have a similar α-helical domain, the structural signature shared with the lineage of the dsRNA bluetongue virus-like viruses. Domain insertions in P2 and P4 preferential sites provide additional functions at the capsid outer surface, probably related to enzyme activity. The P2 insertion has a fold similar to that of gelsolin and profilin, two actin-binding proteins with a function in cytoskeleton metabolism, whereas the P4 insertion suggests protease activity involved in cleavage of the P2 383-residue C-terminal region, absent in the mature viral particle. Our results indicate that the intimate virus-fungus partnership has altered the capsid genome-protective and/or receptor-binding functions. Fungal virus evolution has tended to allocate enzyme activities to the virus capsid outer surface.
[Mh] Termos MeSH primário: Proteínas do Capsídeo/metabolismo
Capsídeo/metabolismo
Modelos Moleculares
Vírus de RNA/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Capsídeo/enzimologia
Capsídeo/ultraestrutura
Proteínas do Capsídeo/química
Proteínas do Capsídeo/genética
Sequência Conservada
Microscopia Crioeletrônica
Evolução Molecular
Imagem Tridimensional
Mutagênese Insercional
Conformação Proteica em alfa-Hélice
Conformação Proteica em Folha beta
Domínios e Motivos de Interação entre Proteínas
Multimerização Proteica
Estabilidade Proteica
Vírus de RNA/enzimologia
Vírus de RNA/genética
Vírus de RNA/ultraestrutura
Alinhamento de Sequência
Homologia Estrutural de Proteína
Propriedades de Superfície
Vírion/enzimologia
Vírion/genética
Vírion/metabolismo
Vírion/ultraestrutura
Xylariales/virologia
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Capsid Proteins)
[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:171209
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006755


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[PMID]:29211815
[Au] Autor:Berger AK; Yi H; Kearns DB; Mainou BA
[Ad] Endereço:Department of Pediatrics, Emory University School of Medicine, Atlanta, Georgia, United States of America.
[Ti] Título:Bacteria and bacterial envelope components enhance mammalian reovirus thermostability.
[So] Source:PLoS Pathog;13(12):e1006768, 2017 Dec.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Enteric viruses encounter diverse environments as they migrate through the gastrointestinal tract to infect their hosts. The interaction of eukaryotic viruses with members of the host microbiota can greatly impact various aspects of virus biology, including the efficiency with which viruses can infect their hosts. Mammalian orthoreovirus, a human enteric virus that infects most humans during childhood, is negatively affected by antibiotic treatment prior to infection. However, it is not known how components of the host microbiota affect reovirus infectivity. In this study, we show that reovirus virions directly interact with Gram positive and Gram negative bacteria. Reovirus interaction with bacterial cells conveys enhanced virion thermostability that translates into enhanced attachment and infection of cells following an environmental insult. Enhanced virion thermostability was also conveyed by bacterial envelope components lipopolysaccharide (LPS) and peptidoglycan (PG). Lipoteichoic acid and N-acetylglucosamine-containing polysaccharides enhanced virion stability in a serotype-dependent manner. LPS and PG also enhanced the thermostability of an intermediate reovirus particle (ISVP) that is associated with primary infection in the gut. Although LPS and PG alter reovirus thermostability, these bacterial envelope components did not affect reovirus utilization of its proteinaceous cellular receptor junctional adhesion molecule-A or cell entry kinetics. LPS and PG also did not affect the overall number of reovirus capsid proteins σ1 and σ3, suggesting their effect on virion thermostability is not mediated through altering the overall number of major capsid proteins on the virus. Incubation of reovirus with LPS and PG did not significantly affect the neutralizing efficiency of reovirus-specific antibodies. These data suggest that bacteria enhance reovirus infection of the intestinal tract by enhancing the thermal stability of the reovirus particle at a variety of temperatures through interactions between the viral particle and bacterial envelope components.
[Mh] Termos MeSH primário: Bacillus subtilis/fisiologia
Enterócitos/virologia
Escherichia coli K12/fisiologia
Infecções por Reoviridae/virologia
Reoviridae/fisiologia
[Mh] Termos MeSH secundário: Acetilglucosamina/análogos & derivados
Acetilglucosamina/metabolismo
Acetilglucosamina/toxicidade
Bacillus subtilis/metabolismo
Bacillus subtilis/ultraestrutura
Bacillus subtilis/virologia
Células CACO-2
Endotoxinas/metabolismo
Endotoxinas/toxicidade
Enterócitos/efeitos dos fármacos
Enterócitos/microbiologia
Enterócitos/patologia
Escherichia coli K12/metabolismo
Escherichia coli K12/ultraestrutura
Escherichia coli K12/virologia
Microbioma Gastrointestinal
Células HeLa
Temperatura Alta
Seres Humanos
Lipopolissacarídeos/metabolismo
Lipopolissacarídeos/toxicidade
Proteínas Luminescentes/genética
Proteínas Luminescentes/metabolismo
Microscopia Eletrônica de Transmissão
Peptidoglicano/metabolismo
Peptidoglicano/toxicidade
RNA/metabolismo
Estabilidade de RNA/efeitos dos fármacos
Proteínas Recombinantes/metabolismo
Reoviridae/química
Reoviridae/efeitos dos fármacos
Reoviridae/patogenicidade
Infecções por Reoviridae/metabolismo
Infecções por Reoviridae/microbiologia
Infecções por Reoviridae/patologia
Ácidos Teicoicos/metabolismo
Ácidos Teicoicos/toxicidade
Vírion/química
Vírion/patogenicidade
Vírion/fisiologia
Ligação Viral/efeitos dos fármacos
Internalização do Vírus/efeitos dos fármacos
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Endotoxins); 0 (Lipopolysaccharides); 0 (Luminescent Proteins); 0 (Peptidoglycan); 0 (RNA, recombinant); 0 (Recombinant Proteins); 0 (Teichoic Acids); 0 (red fluorescent protein); 56411-57-5 (lipoteichoic acid); 63231-63-0 (RNA); 67924-63-4 (endotoxin, Escherichia coli); V956696549 (Acetylglucosamine)
[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:171207
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006768


  8 / 11417 MEDLINE  
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[PMID]:29244872
[Au] Autor:Barrado-Gil L; Galindo I; Martínez-Alonso D; Viedma S; Alonso C
[Ad] Endereço:Department of Biotechnology, Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria, INIA, Madrid, Spain.
[Ti] Título:The ubiquitin-proteasome system is required for African swine fever replication.
[So] Source:PLoS One;12(12):e0189741, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Several viruses manipulate the ubiquitin-proteasome system (UPS) to initiate a productive infection. Determined viral proteins are able to change the host's ubiquitin machinery and some viruses even encode their own ubiquitinating or deubiquitinating enzymes. African swine fever virus (ASFV) encodes a gene homologous to the E2 ubiquitin conjugating (UBC) enzyme. The viral ubiquitin-conjugating enzyme (UBCv1) is expressed throughout ASFV infection and accumulates at late times post infection. UBCv is also present in the viral particle suggesting that the ubiquitin-proteasome pathway could play an important role at early ASFV infection. We determined that inhibition of the final stage of the ubiquitin-proteasome pathway blocked a post-internalization step in ASFV replication in Vero cells. Under proteasome inhibition, ASF viral genome replication, late gene expression and viral production were severely reduced. Also, ASFV enhanced proteasome activity at late times and the accumulation of polyubiquitinated proteins surrounding viral factories. Core-associated and/or viral proteins involved in DNA replication may be targets for the ubiquitin-proteasome pathway that could possibly assist virus uncoating at final core breakdown and viral DNA release. At later steps, polyubiquitinated proteins at viral factories could exert regulatory roles in cell signaling.
[Mh] Termos MeSH primário: Vírus da Febre Suína Africana/genética
Febre Suína Africana/genética
Enzimas de Conjugação de Ubiquitina/genética
Proteínas Virais/genética
Replicação Viral/genética
[Mh] Termos MeSH secundário: Febre Suína Africana/virologia
Vírus da Febre Suína Africana/patogenicidade
Animais
Cercopithecus aethiops
Replicação do DNA/genética
DNA Viral/genética
Genoma Viral
Complexo de Endopeptidases do Proteassoma/genética
Suínos/virologia
Ubiquitina/genética
Células Vero
Vírion/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Viral); 0 (Ubiquitin); 0 (Viral Proteins); EC 2.3.2.23 (Ubiquitin-Conjugating Enzymes); EC 2.3.2.23 (ubiquitin-conjugating enzyme UBCv1, African swine fever virus); EC 3.4.25.1 (Proteasome Endopeptidase Complex)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180102
[Lr] Data última revisão:
180102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171216
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189741


  9 / 11417 MEDLINE  
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[PMID]:29251589
[Au] Autor:Ghabrial SA; Castón JR; Coutts RHA; Hillman BI; Jiang D; Kim DH; Moriyama H; Ictv Report Consortium
[Ad] Endereço:1​Department of Plant Pathology, University of Kentucky, Lexington, KY 40546, USA.
[Ti] Título:ICTV Virus Taxonomy Profile: Chrysoviridae.
[So] Source:J Gen Virol;99(1):19-20, 2018 Jan.
[Is] ISSN:1465-2099
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The Chrysoviridae is a family of small, isometric, non-enveloped viruses (40 nm in diameter) with segmented dsRNA genomes (typically four segments). The genome segments are individually encapsidated and together comprise 11.5-12.8 kbp. The single genus Chrysovirus includes nine species. Chrysoviruses lack an extracellular phase to their life cycle; they are transmitted via intracellular routes within an individual during hyphal growth, in asexual or sexual spores, or between individuals via hyphal anastomosis. There are no known natural vectors for chrysoviruses. This is a summary of the International Committee on Taxonomy of Viruses (ICTV) Report on the taxonomy of the Chrysoviridae, which is available at www.ictv.global/report/chrysoviridae.
[Mh] Termos MeSH primário: Genoma Viral
Filogenia
Vírus de RNA/genética
RNA de Cadeia Dupla/genética
RNA Viral/genética
Vírion/genética
[Mh] Termos MeSH secundário: Ascomicetos/virologia
Basidiomycota/virologia
Hifas/virologia
Vírus de RNA/classificação
Vírus de RNA/ultraestrutura
Esporos Fúngicos/virologia
Terminologia como Assunto
Vírion/ultraestrutura
Replicação Viral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Double-Stranded); 0 (RNA, Viral)
[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:171219
[St] Status:MEDLINE
[do] DOI:10.1099/jgv.0.000994


  10 / 11417 MEDLINE  
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[PMID]:29235978
[Au] Autor:Hakobyan A; Galindo I; Nañez A; Arabyan E; Karalyan Z; Chistov AA; Streshnev PP; Korshun VA; Alonso C; Zakaryan H
[Ad] Endereço:1​Group of Antiviral Defense Mechanisms, Institute of Molecular Biology of NAS RA, 0014, Yerevan, Armenia.
[Ti] Título:Rigid amphipathic fusion inhibitors demonstrate antiviral activity against African swine fever virus.
[So] Source:J Gen Virol;99(1):148-156, 2018 Jan.
[Is] ISSN:1465-2099
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Rigid amphipathic fusion inhibitors (RAFIs) are a family of nucleoside derivatives that inhibit the infectivity of several enveloped viruses by interacting with virion envelope lipids and inhibiting fusion between viral and cellular membranes. Here we tested the antiviral activity of two RAFIs, 5-(Perylen-3-ylethynyl)-arabino-uridine (aUY11) and 5-(Perylen-3-ylethynyl)uracil-1-acetic acid (cm1UY11) against African swine fever virus (ASFV), for which no effective vaccine is available. Both compounds displayed a potent, dose-dependent inhibitory effect on ASFV infection in Vero cells. The major antiviral effect was observed when aUY11 and cm1UY11 were added at early stages of infection and maintained during the complete viral cycle. Furthermore, virucidal assay revealed a significant extracellular anti-ASFV activity for both compounds. We also found decrease in the synthesis of early and late viral proteins in Vero cells treated with cm1UY11. Finally, the inhibitory effect of aUY11 and cm1UY11 on ASFV infection in porcine alveolar macrophages was confirmed. Overall, our study has identified novel anti-ASFV compounds with potential for future therapeutic developments.
[Mh] Termos MeSH primário: Vírus da Febre Suína Africana/efeitos dos fármacos
Antivirais/farmacologia
Perileno/análogos & derivados
Uracila/análogos & derivados
Uridina/análogos & derivados
Proteínas Virais/antagonistas & inibidores
Vírion/efeitos dos fármacos
Internalização do Vírus/efeitos dos fármacos
[Mh] Termos MeSH secundário: Vírus da Febre Suína Africana/crescimento & desenvolvimento
Vírus da Febre Suína Africana/metabolismo
Animais
Antivirais/síntese química
Membrana Celular/efeitos dos fármacos
Membrana Celular/virologia
Cercopithecus aethiops
Relação Dose-Resposta a Droga
Macrófagos Alveolares/efeitos dos fármacos
Macrófagos Alveolares/virologia
Testes de Sensibilidade Microbiana
Perileno/síntese química
Perileno/farmacologia
Cultura Primária de Células
Suínos
Uracila/síntese química
Uracila/farmacologia
Uridina/síntese química
Uridina/farmacologia
Células Vero
Proteínas Virais/biossíntese
Vírion/crescimento & desenvolvimento
Vírion/metabolismo
Replicação Viral/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (5-(perylen-3-yl)ethynylarabinouridine); 0 (5-(perylen-3-ylethynyl)uracil-1-acetic acid); 0 (Antiviral Agents); 0 (Viral Proteins); 56HH86ZVCT (Uracil); 5QD5427UN7 (Perylene); WHI7HQ7H85 (Uridine)
[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:171214
[St] Status:MEDLINE
[do] DOI:10.1099/jgv.0.000991



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