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[PMID]:28275191
[Au] Autor:El Bilali N; Duron J; Gingras D; Lippé R
[Ad] Endereço:Department of Pathology and Cell Biology, University of Montreal, Montreal, Quebec, Canada.
[Ti] Título:Quantitative Evaluation of Protein Heterogeneity within Herpes Simplex Virus 1 Particles.
[So] Source:J Virol;91(10), 2017 May 15.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Several virulence genes have been identified thus far in the herpes simplex virus 1 genome. It is also generally accepted that protein heterogeneity among virions further impacts viral fitness. However, linking this variability directly with infectivity has been challenging at the individual viral particle level. To address this issue, we resorted to flow cytometry (flow virometry), a powerful approach we recently employed to analyze individual viral particles, to identify which tegument proteins vary and directly address if such variability is biologically relevant. We found that the stoichiometry of the U 37, ICP0, and VP11/12 tegument proteins in virions is more stable than the VP16 and VP22 tegument proteins, which varied significantly among viral particles. Most interestingly, viruses sorted for their high VP16 or VP22 content yielded modest but reproducible increases in infectivity compared to their corresponding counterparts containing low VP16 or VP22 content. These findings were corroborated for VP16 in short interfering RNA experiments but proved intriguingly more complex for VP22. An analysis by quantitative Western blotting revealed substantial alterations of virion composition upon manipulation of individual tegument proteins and suggests that VP22 protein levels acted indirectly on viral fitness. These findings reaffirm the interdependence of the virion components and corroborate that viral fitness is influenced not only by the genome of viruses but also by the stoichiometry of proteins within each virion. The ability of viruses to spread in animals has been mapped to several viral genes, but other factors are clearly involved, including virion heterogeneity. To directly probe whether the latter influences viral fitness, we analyzed the protein content of individual herpes simplex virus 1 particles using an innovative flow cytometry approach. The data confirm that some viral proteins are incorporated in more controlled amounts, while others vary substantially. Interestingly, this correlates with the VP16 -activating viral protein and indirectly with VP22, a second virion component whose modulation profoundly alters virion composition. This reaffirms that not only the presence but also the amount of specific tegument proteins is an important determinant of viral fitness.
[Mh] Termos MeSH primário: Proteína Vmw65 do Vírus do Herpes Simples/metabolismo
Herpesvirus Humano 1/genética
Herpesvirus Humano 1/fisiologia
Proteínas Estruturais Virais/metabolismo
[Mh] Termos MeSH secundário: Animais
Western Blotting
Cercopithecus aethiops
Citometria de Fluxo
Genes Virais
Proteína Vmw65 do Vírus do Herpes Simples/análise
Proteína Vmw65 do Vírus do Herpes Simples/química
Herpesvirus Humano 1/patogenicidade
RNA Interferente Pequeno
Células Vero
Proteínas Estruturais Virais/análise
Proteínas Estruturais Virais/química
Vírion/genética
Vírion/fisiologia
Montagem de Vírus
[Pt] Tipo de publicação:EVALUATION STUDIES; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Herpes Simplex Virus Protein Vmw65); 0 (RNA, Small Interfering); 0 (Viral Structural Proteins); 0 (herpes simplex virus type 1 protein VP22)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171028
[Lr] Data última revisão:
171028
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170310
[St] Status:MEDLINE


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[PMID]:28222744
[Au] Autor:Zheng C; Su C
[Ad] Endereço:Institutes of Biology and Medical Sciences, Soochow University, Suzhou, 215123, China. zheng.alan@hotmail.com.
[Ti] Título:Herpes simplex virus 1 infection dampens the immediate early antiviral innate immunity signaling from peroxisomes by tegument protein VP16.
[So] Source:Virol J;14(1):35, 2017 Feb 21.
[Is] ISSN:1743-422X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Herpes simplex virus 1 (HSV-1) is an archetypal member of the alphaherpesvirus subfamily with a large genome encoding over 80 proteins, many of which play a critical role in virus-host interactions and immune modulation. Upon viral infections, the host cells activate innate immune responses to restrict their replications. Peroxisomes, which have long been defined to regulate metabolic activities, are reported to be important signaling platforms for antiviral innate immunity. It has been verified that signaling from peroxisomal MAVS (MAVS-Pex) triggers a rapid interferon (IFN) independent IFN-stimulated genes (ISGs) production against invading pathogens. However, little is known about the interaction between DNA viruses such as HSV-1 and the MAVS-Pex mediated signaling. RESULTS: HSV-1 could activate the MAVS-Pex signaling pathway at a low multiplicity of infection (MOI), while infection at a high MOI dampens MAVS-Pex induced immediately early ISGs production. A high-throughput screen assay reveals that HSV-1 tegument protein VP16 inhibits the immediate early ISGs expression downstream of MAVS-Pex signaling. Moreover, the expression of ISGs was recovered when VP16 was knockdown with its specific short hairpin RNA. CONCLUSION: HSV-1 blocks MAVS-Pex mediated early ISGs production through VP16 to dampen the immediate early antiviral innate immunity signaling from peroxisomes.
[Mh] Termos MeSH primário: Proteína Vmw65 do Vírus do Herpes Simples/metabolismo
Herpesvirus Humano 1/patogenicidade
Interações Hospedeiro-Patógeno
Evasão da Resposta Imune
Imunidade Inata
Peroxissomos/metabolismo
Transdução de Sinais
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Linhagem Celular
Seres Humanos
Endopeptidase Neutra Reguladora de Fosfato PHEX/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Herpes Simplex Virus Protein Vmw65); 0 (VISA protein, human); EC 3.4.24.- (PHEX Phosphate Regulating Neutral Endopeptidase); EC 3.4.24.- (PHEX protein, human)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170823
[Lr] Data última revisão:
170823
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170223
[St] Status:MEDLINE
[do] DOI:10.1186/s12985-017-0709-5


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[PMID]:28178699
[Au] Autor:Li F; Zhang Y; Chen S; Wang M; Jia R; Zhu D; Liu M; Sun K; Yang Q; Wu Y; Chen X; Cheng A
[Ad] Endereço:Institute of Preventive Veterinary Medicine, Sichuan Agricultural University, Chengdu, PR China.
[Ti] Título:Identification of the Nuclear Localization Signal Region of Duck Enteritis Virus UL14 and Its Interaction with VP16.
[So] Source:Intervirology;59(4):187-196, 2016.
[Is] ISSN:1423-0100
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:OBJECT: Duck enteritis virus (DEV) is a member of the Alphaherpesvirinae viruses. VP16 and pUL14 are both predicted to be tegument proteins of DEV. METHODS: An indirect immunofluorescence assay (IFA) was performed for preliminary analysis of the colocalization of pUL14 and VP16, which detected their subcellular localization in duck embryo fibroblasts (DEFs) during virus replication. The coexpression of pUL14 and VP16 was detected in transfected DEFs. A bimolecular fluorescence complementation (BiFC) assay was used to confirm a direct interaction between pUL14 and VP16. To better characterize the nuclear localization domain of pUL14, we designed a series of deletion mutants and transfected them with VP16. RESULTS: Our IFA findings indicated that pUL14 binds to VP16 in the cytoplasm and that pUL14 leads VP16 import into the nucleus during DEV replication. The BiFC assay revealed the presence of pUL14 and VP16 complexes. Furthermore, 1-98 amino acid (aa) at the N-terminus of pUL14 played a role in the nuclear localization signal (NLS) region and promoted translocation of VP16 into the nucleus to complete the virus life cycle. CONCLUSIONS: Our findings indicated that pUL14 could transport VP16 into the nucleus and that the N-terminal 1-98 aa may contain the NLS domain of pUL14.
[Mh] Termos MeSH primário: Proteína Vmw65 do Vírus do Herpes Simples/genética
Proteína Vmw65 do Vírus do Herpes Simples/metabolismo
Mardivirus/genética
Sinais de Localização Nuclear/genética
Sinais de Localização Nuclear/metabolismo
Proteínas Virais/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Linhagem Celular
Núcleo Celular/genética
Patos/virologia
Fibroblastos/ultraestrutura
Fibroblastos/virologia
Microscopia de Fluorescência
Mutação
Transfecção
Proteínas Virais/metabolismo
Replicação Viral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Herpes Simplex Virus Protein Vmw65); 0 (Nuclear Localization Signals); 0 (Viral Proteins)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170417
[Lr] Data última revisão:
170417
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170209
[St] Status:MEDLINE
[do] DOI:10.1159/000452711


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[PMID]:27645993
[Au] Autor:Huang G; Zhang Y; Shan Y; Yang S; Chelliah Y; Wang H; Takahashi JS
[Ad] Endereço:From the Department of Neuroscience and guocun.huang@utsouthwestern.edu.
[Ti] Título:Circadian Oscillations of NADH Redox State Using a Heterologous Metabolic Sensor in Mammalian Cells.
[So] Source:J Biol Chem;291(46):23906-23914, 2016 Nov 11.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:It is known that there are mechanistic links between circadian clocks and metabolic cycles. Reduced nicotinamide adenine dinucleotide (NADH) is a key metabolic cofactor in all living cells; however, it is not known whether levels of NADH oscillate or not. Here we employed REX, a bacterial NADH-binding protein, fused to the VP16 activator to convert intracellular endogenous redox balance into transcriptional readouts by a reporter gene in mammalian cells. EMSA results show that the DNA binding activity of both T- and S-REX::VP16 fusions is decreased with a reduced-to-oxidized cofactor ratio increase. Transient and stabilized cell lines bearing the REX::VP16 and the REX binding operator (ROP) exhibit two circadian luminescence cycles. Consistent with these results, NADH oscillations are observed in host cells, indicating REX can act as a NADH sensor to report intracellular dynamic redox homeostasis in mammalian cells in real time. NADH oscillations provide another metabolic signal for coupling the circadian clock and cellular metabolic states.
[Mh] Termos MeSH primário: Proteínas de Bactérias
Técnicas Biossensoriais
Relógios Circadianos
Proteína Vmw65 do Vírus do Herpes Simples
NAD/metabolismo
Proteínas Recombinantes de Fusão/biossíntese
[Mh] Termos MeSH secundário: Proteínas de Bactérias/biossíntese
Proteínas de Bactérias/genética
Células HEK293
Proteína Vmw65 do Vírus do Herpes Simples/biossíntese
Proteína Vmw65 do Vírus do Herpes Simples/genética
Seres Humanos
Oxirredução
Proteínas Recombinantes de Fusão/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Herpes Simplex Virus Protein Vmw65); 0 (Recombinant Fusion Proteins); 0U46U6E8UK (NAD)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171111
[Lr] Data última revisão:
171111
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160921
[St] Status:MEDLINE


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[PMID]:27607440
[Au] Autor:Sawtell NM; Thompson RL
[Ad] Endereço:Department of Pediatrics, Division of Infectious Diseases, Cincinnati Children's Hospital Medical Center, Cincinnati, Ohio, United States of America.
[Ti] Título:De Novo Herpes Simplex Virus VP16 Expression Gates a Dynamic Programmatic Transition and Sets the Latent/Lytic Balance during Acute Infection in Trigeminal Ganglia.
[So] Source:PLoS Pathog;12(9):e1005877, 2016 Sep.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The life long relationship between herpes simplex virus and its host hinges on the ability of the virus to aggressively replicate in epithelial cells at the site of infection and transport into the nervous system through axons innervating the infection site. Interaction between the virus and the sensory neuron represents a pivot point where largely unknown mechanisms lead to a latent or a lytic infection in the neuron. Regulation at this pivot point is critical for balancing two objectives, efficient widespread seeding of the nervous system and host survival. By combining genetic and in vivo in approaches, our studies reveal that the balance between latent and lytic programs is a process occurring early in the trigeminal ganglion. Unexpectedly, activation of the latent program precedes entry into the lytic program by 12 -14hrs. Importantly, at the individual neuronal level, the lytic program begins as a transition out of this acute stage latent program and this escape from the default latent program is regulated by de novo VP16 expression. Our findings support a model in which regulated de novo VP16 expression in the neuron mediates entry into the lytic cycle during the earliest stages of virus infection in vivo. These findings support the hypothesis that the loose association of VP16 with the viral tegument combined with sensory axon length and transport mechanisms serve to limit arrival of virion associated VP16 into neuronal nuclei favoring latency. Further, our findings point to specialized features of the VP16 promoter that control the de novo expression of VP16 in neurons and this regulation is a key component in setting the balance between lytic and latent infections in the nervous system.
[Mh] Termos MeSH primário: Regulação Viral da Expressão Gênica
Proteína Vmw65 do Vírus do Herpes Simples/biossíntese
Herpes Simples/metabolismo
Herpesvirus Humano 1/fisiologia
Gânglio Trigeminal/metabolismo
Latência Viral
[Mh] Termos MeSH secundário: Doença Aguda
Animais
Axônios/metabolismo
Axônios/virologia
Núcleo Celular/genética
Núcleo Celular/metabolismo
Núcleo Celular/virologia
Herpes Simples/genética
Proteína Vmw65 do Vírus do Herpes Simples/genética
Seres Humanos
Camundongos
Células Receptoras Sensoriais/metabolismo
Células Receptoras Sensoriais/virologia
Gânglio Trigeminal/virologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Herpes Simplex Virus Protein Vmw65)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170623
[Lr] Data última revisão:
170623
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160909
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1005877


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[PMID]:27213278
[Au] Autor:Dugan A; Pricer R; Katz M; Mapp AK
[Ad] Endereço:Life Sciences Institute, University of Michigan, Ann Arbor, Michigan.
[Ti] Título:TRIC: Capturing the direct cellular targets of promoter-bound transcriptional activators.
[So] Source:Protein Sci;25(8):1371-7, 2016 08.
[Is] ISSN:1469-896X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Transcriptional activators coordinate the dynamic assembly of multiprotein coactivator complexes required for gene expression to occur. Here we combine the power of in vivo covalent chemical capture with p-benzoyl-L-phenylalanine (Bpa), a genetically incorporated photo-crosslinking amino acid, and chromatin immunoprecipitation (ChIP) to capture the direct protein interactions of the transcriptional activator VP16 with the general transcription factor TBP at the GAL1 promoter in live yeast.
[Mh] Termos MeSH primário: Proteína Vmw65 do Vírus do Herpes Simples/genética
Saccharomyces cerevisiae/genética
Proteína de Ligação a TATA-Box/genética
Transativadores/genética
Ativação Transcricional
[Mh] Termos MeSH secundário: Benzofenonas/química
Benzofenonas/metabolismo
Imunoprecipitação da Cromatina
Reagentes para Ligações Cruzadas/química
Reagentes para Ligações Cruzadas/metabolismo
Galactoquinase/genética
Galactoquinase/metabolismo
Proteína Vmw65 do Vírus do Herpes Simples/metabolismo
Fenilalanina/análogos & derivados
Fenilalanina/química
Fenilalanina/metabolismo
Processos Fotoquímicos
Regiões Promotoras Genéticas
Ligação Proteica
Multimerização Proteica
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
Transdução de Sinais
Proteína de Ligação a TATA-Box/metabolismo
Transativadores/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (4-benzoylphenylalanine); 0 (Benzophenones); 0 (Cross-Linking Reagents); 0 (Herpes Simplex Virus Protein Vmw65); 0 (Saccharomyces cerevisiae Proteins); 0 (TATA-Box Binding Protein); 0 (Trans-Activators); 47E5O17Y3R (Phenylalanine); EC 2.7.1.6 (GAL1 protein, S cerevisiae); EC 2.7.1.6 (Galactokinase)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170801
[Lr] Data última revisão:
170801
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160524
[St] Status:MEDLINE
[do] DOI:10.1002/pro.2951


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[PMID]:27060489
[Au] Autor:Mehta ST; Luo X; Park KK; Bixby JL; Lemmon VP
[Ad] Endereço:Miami Project to Cure Paralysis, University of Miami Miller School of Medicine, Miami, FL 33136, USA. Electronic address: s.mehta8@med.miami.edu.
[Ti] Título:Hyperactivated Stat3 boosts axon regeneration in the CNS.
[So] Source:Exp Neurol;280:115-20, 2016 Jun.
[Is] ISSN:1090-2430
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Axonal regeneration after spinal cord injury (SCI) is intrinsically and extrinsically inhibited by multiple factors. One major factor contributing to intrinsic regeneration failure is the inability of mature neurons in the central nervous system (CNS) to activate regeneration-associated transcription factors (TFs) post-injury. A prior study identified TFs overexpressed in neurons of the peripheral nervous system (PNS) compared to the CNS; some of these could be involved in the ability of PNS neurons to regenerate. Of these, signal transducer and activator of transcription 3 (STAT3), as well its downstream regeneration-associated targets, showed a significant upregulation in PNS neurons relative to CNS neurons, and a constitutively active variant of Stat3 (Stat3CA) promoted neurite growth when expressed in cerebellar neurons (Lerch et al., 2012; Smith et al., 2011). To further enhance STAT3's neurite outgrowth enhancing activity, Stat3CA was fused with a viral activation domain (VP16). VP16 hyperactivates TFs by recruiting transcriptional co-factors to the DNA binding domain (Hirai et al., 2010). Overexpression of this VP16-Stat3CA chimera in primary cortical neurons led to a significant increase of neurite outgrowth as well as Stat3 transcriptional activity in vitro. Furthermore, in vivo transduction of retinal ganglion cells (RGCs) with AAV constructs expressing VP16-Stat3CA resulted in regeneration of optic nerve axons after injury, to a greater degree than for those expressing Stat3CA alone. These findings confirm and extend the concept that overexpression of hyperactivated transcription factors identified as functioning in PNS regeneration can promote axon regeneration in the CNS.
[Mh] Termos MeSH primário: Sistema Nervoso Central/patologia
Proteína Vmw65 do Vírus do Herpes Simples/metabolismo
Regeneração Nervosa/fisiologia
Traumatismos do Nervo Óptico/patologia
Fator de Transcrição STAT3/metabolismo
[Mh] Termos MeSH secundário: Análise de Variância
Animais
Animais Recém-Nascidos
Axônios/fisiologia
Células Cultivadas
Córtex Cerebral/citologia
Toxina da Cólera/toxicidade
Feminino
Proteína Vmw65 do Vírus do Herpes Simples/genética
Camundongos
Camundongos Endogâmicos C57BL
Mutação/genética
Neuritos
Ratos
Fator de Transcrição STAT3/genética
Transdução Genética
Regulação para Cima/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Herpes Simplex Virus Protein Vmw65); 0 (STAT3 Transcription Factor); 9012-63-9 (Cholera Toxin)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170601
[Lr] Data última revisão:
170601
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160410
[St] Status:MEDLINE


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[PMID]:27009950
[Au] Autor:Ivanova L; Buch A; Döhner K; Pohlmann A; Binz A; Prank U; Sandbaumhüter M; Bauerfeind R; Sodeik B
[Ad] Endereço:Institute of Virology, Hannover Medical School, Hannover, Germany German Center for Infection Research (DZIF), Hannover, Germany.
[Ti] Título:Conserved Tryptophan Motifs in the Large Tegument Protein pUL36 Are Required for Efficient Secondary Envelopment of Herpes Simplex Virus Capsids.
[So] Source:J Virol;90(11):5368-83, 2016 Jun 01.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:UNLABELLED: Herpes simplex virus (HSV) replicates in the skin and mucous membranes, and initiates lytic or latent infections in sensory neurons. Assembly of progeny virions depends on the essential large tegument protein pUL36 of 3,164 amino acid residues that links the capsids to the tegument proteins pUL37 and VP16. Of the 32 tryptophans of HSV-1-pUL36, the tryptophan-acidic motifs (1766)WD(1767) and (1862)WE(1863) are conserved in all HSV-1 and HSV-2 isolates. Here, we characterized the role of these motifs in the HSV life cycle since the rare tryptophans often have unique roles in protein function due to their large hydrophobic surface. The infectivity of the mutants HSV-1(17(+))Lox-pUL36-WD/AA-WE/AA and HSV-1(17(+))Lox-CheVP26-pUL36-WD/AA-WE/AA, in which the capsid has been tagged with the fluorescent protein Cherry, was significantly reduced. Quantitative electron microscopy shows that there were a larger number of cytosolic capsids and fewer enveloped virions compared to their respective parental strains, indicating a severe impairment in secondary capsid envelopment. The capsids of the mutant viruses accumulated in the perinuclear region around the microtubule-organizing center and were not dispersed to the cell periphery but still acquired the inner tegument proteins pUL36 and pUL37. Furthermore, cytoplasmic capsids colocalized with tegument protein VP16 and, to some extent, with tegument protein VP22 but not with the envelope glycoprotein gD. These results indicate that the unique conserved tryptophan-acidic motifs in the central region of pUL36 are required for efficient targeting of progeny capsids to the membranes of secondary capsid envelopment and for efficient virion assembly. IMPORTANCE: Herpesvirus infections give rise to severe animal and human diseases, especially in young, immunocompromised, and elderly individuals. The structural hallmark of herpesvirus virions is the tegument, which contains evolutionarily conserved proteins that are essential for several stages of the herpesvirus life cycle. Here we characterized two conserved tryptophan-acidic motifs in the central region of the large tegument protein pUL36 of herpes simplex virus. When we mutated these motifs, secondary envelopment of cytosolic capsids and the production of infectious particles were severely impaired. Our data suggest that pUL36 and its homologs in other herpesviruses, and in particular such tryptophan-acidic motifs, could provide attractive targets for the development of novel drugs to prevent herpesvirus assembly and spread.
[Mh] Termos MeSH primário: Capsídeo/metabolismo
Herpesvirus Humano 1/fisiologia
Triptofano/química
Proteínas Estruturais Virais/química
Proteínas Estruturais Virais/metabolismo
Montagem de Vírus
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Capsídeo/ultraestrutura
Proteínas do Capsídeo/química
Proteínas do Capsídeo/metabolismo
Linhagem Celular
Citoplasma/virologia
Proteína Vmw65 do Vírus do Herpes Simples/metabolismo
Herpesvirus Humano 1/química
Herpesvirus Humano 1/genética
Seres Humanos
Estágios do Ciclo de Vida
Microscopia Eletrônica
Mutação
Ligação Proteica
Domínios Proteicos
Triptofano/metabolismo
Proteínas Estruturais Virais/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Capsid Proteins); 0 (Herpes Simplex Virus Protein Vmw65); 0 (Viral Structural Proteins); 8DUH1N11BX (Tryptophan)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170428
[Lr] Data última revisão:
170428
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160325
[St] Status:MEDLINE
[do] DOI:10.1128/JVI.03167-15


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[PMID]:26857504
[Au] Autor:Caggiu E; Paulus K; Arru G; Piredda R; Sechi GP; Sechi LA
[Ad] Endereço:Dipartimento di Scienze Biomediche, Sezione di Microbiologia e Virologia, Università di Sassari, Italy.
[Ti] Título:Humoral cross reactivity between α-synuclein and herpes simplex-1 epitope in Parkinson's disease, a triggering role in the disease?
[So] Source:J Neuroimmunol;291:110-4, 2016 Feb 15.
[Is] ISSN:1872-8421
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Environmental factors are implicated in the development of Parkinson's disease (PD). We have investigated on the role of molecular mimicry between HSV1 and α-synuclein that could foster the progression of PD. The antibody response against homologous peptides in PD patients and healthy controls was evaluated, showing that these antibodies are highly prevalent among PD patients to healthy controls. The competitive assay demonstrated cross-reactivity between HSV1 and human α-synuclein peptides. The results may suggest the hypothesis of the involvement of HSV1 in stimulating the immune cells against the neurons of the substantia nigra as a consequence of the cross reactivity.
[Mh] Termos MeSH primário: Proteína Vmw65 do Vírus do Herpes Simples/metabolismo
Doença de Parkinson/complicações
alfa-Sinucleína/metabolismo
[Mh] Termos MeSH secundário: Idoso
Estudos de Casos e Controles
Reações Cruzadas
Ensaio de Imunoadsorção Enzimática
Feminino
Seres Humanos
Masculino
Meia-Idade
Mimetismo Molecular
Peptídeos/metabolismo
Curva ROC
Substância Negra/metabolismo
Substância Negra/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Herpes Simplex Virus Protein Vmw65); 0 (Peptides); 0 (SNCA protein, human); 0 (alpha-Synuclein)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:160209
[Lr] Data última revisão:
160209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160210
[St] Status:MEDLINE


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[PMID]:26259267
[Ti] Título:[EFFECTIVENESS OF POLYCATIONIC NANOPARTICLES OF POLYETHYLENEIMINE-POLYHYDROZIDE-CHITOSAN (PEI-PG-OCHG) AS A VECTOR FOR SMALL INTER- FERING RNA, DIRECTED TO SUPPRESS HERPES SIMPLEX TYPE 2 VIRUS REPLICATION].
[So] Source:Zh Mikrobiol Epidemiol Immunobiol;(3):31-7, 2015 May-Jun.
[Is] ISSN:0372-9311
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Ab] Resumo:AIM: Evaluation of an antiviral effect of miRNA in the nanoparticles of a polycationic compound against mRNA of vp16 protein (UL48 gene) of herpes simplex virus type 2 (HSV-2) in vitro. MATERIALS AND METHODS. 50% aqueous solution of polyethyleneimine (BDH, Great Britain), chitosan, containing approximately 15% of N-acetylated glucosamine chains (Sonat, Russia), hydrazine-hydrate and other chemical reagents (Chimmed, Russia); Vero continuous cell line, MS HSV-2 virus were used. Vero cells were cultivated in DMEM medium supplemented by 10% fetal bovine serum at 37°C in the atmosphere of 5% CO2. Cell viability was evaluated by using Neutral Red vital stain and MTT-test. Primers and probes for RT-PCR were modeled in Vector NTI 8.0 computer program according to the mRNA sequences of the studied genes (the sequences were obtained from GenBank) and synthesized in Sintol (Russia). RT-PCR tests were set using a standard procedure. Synthesis of PEI-PG-chitosan was carried out by Krivtsov G.G. et al. (2010). RESULTS: A design and synthesis of nucleotide sequences, that have interfering activity against this virus, was carried out to study the effect of siRNA on HSV-2 virus replication. During simultaneous addition of HSV-2 and specific siRNA to Vero cells in cell culture, a significant (by 4 lg) reduction of virus yield was observed. A level of UL48 mRNA expression level was determined after the influence of various siRNA variants. A S2 siRNA variant was shown to cause the most pronounced virus-inhibiting effect, aiming for the center of RNA-target (the level of expression of the studied gene decreased by 0.5 lg). CONCLUSION: siRNA in the PEI-PG-chitosan complexes were established to possess in vitro pronounced suppressive HSV-2 replication activity. The results obtained could be used in creation of new therapeutic preparation against herpes viruses.
[Mh] Termos MeSH primário: Herpesvirus Humano 2/efeitos dos fármacos
MicroRNAs/genética
Nanopartículas/administração & dosagem
Replicação Viral/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Bovinos
Cercopithecus aethiops
Quitosana/administração & dosagem
Quitosana/química
Regulação Viral da Expressão Gênica/efeitos dos fármacos
Proteína Vmw65 do Vírus do Herpes Simples/antagonistas & inibidores
Proteína Vmw65 do Vírus do Herpes Simples/biossíntese
Herpesvirus Humano 2/genética
Herpesvirus Humano 2/patogenicidade
Seres Humanos
MicroRNAs/administração & dosagem
MicroRNAs/química
Nanopartículas/química
Polietilenoimina/administração & dosagem
Polietilenoimina/química
Células Vero
[Pt] Tipo de publicação:ENGLISH ABSTRACT; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Herpes Simplex Virus Protein Vmw65); 0 (MicroRNAs); 9002-98-6 (Polyethyleneimine); 9012-76-4 (Chitosan)
[Em] Mês de entrada:1508
[Cu] Atualização por classe:150811
[Lr] Data última revisão:
150811
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150812
[St] Status:MEDLINE



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