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  1 / 12 MEDLINE  
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[PMID]:28257484
[Au] Autor:Teferi WM; Desaulniers MA; Noyce RS; Shenouda M; Umer B; Evans DH
[Ad] Endereço:Department of Medical Microbiology & Immunology, Li Ka Shing Institute of Virology, University of Alberta, Edmonton, Alberta, Canada.
[Ti] Título:The vaccinia virus K7 protein promotes histone methylation associated with heterochromatin formation.
[So] Source:PLoS One;12(3):e0173056, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:It has been well established that many vaccinia virus proteins suppress host antiviral pathways by targeting the transcription of antiviral proteins, thus evading the host innate immune system. However, whether viral proteins have an effect on the host's overall cellular transcription is less understood. In this study we investigated the regulation of heterochromatin during vaccinia virus infection. Heterochromatin is a highly condensed form of chromatin that is less transcriptionally active and characterized by methylation of histone proteins. We examined the change in methylation of two histone proteins, H3 and H4, which are major markers of heterochromatin, during the course of viral infection. Using immunofluorescence microscopy and flow cytometry we were able to track the overall change in the methylated levels of H3K9 and H4K20. Our results suggest that there is significant increase in methylation of H3K9 and H4K20 during Orthopoxviruses infection compared to mock-infected cells. However, this effect was not seen when we infected cells with Leporipoxviruses. We further screened several vaccinia virus single and multi-gene deletion mutant and identified the vaccinia virus gene K7R as a contributor to the increase in cellular histone methylation during infection.
[Mh] Termos MeSH primário: Epigênese Genética
Fibroblastos/virologia
Histonas/metabolismo
Vírus Vaccinia/genética
Proteínas Virais/metabolismo
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Cercopithecus aethiops
Montagem e Desmontagem da Cromatina
Embrião de Mamíferos
Fibroblastos/metabolismo
Heterocromatina/metabolismo
Heterocromatina/ultraestrutura
Histonas/genética
Interações Hospedeiro-Patógeno
Seres Humanos
Leporipoxvirus/genética
Leporipoxvirus/metabolismo
Metilação
Microscopia de Fluorescência
Mutação
Cultura Primária de Células
Vírus Vaccinia/metabolismo
Proteínas Virais/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Heterochromatin); 0 (Histones); 0 (Viral Proteins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170828
[Lr] Data última revisão:
170828
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170304
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0173056


  2 / 12 MEDLINE  
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[PMID]:25075821
[Au] Autor:Rivas AE; Righton AL; Bugman AM; Kihn AE; Coleman DA; Singh K; Whittington JK
[Ad] Endereço:Department of Veterinary Clinical Medicine, College of Veterinary Medicine, University of Illinois, Urbana, IL 61802.
[Ti] Título:Pathology in practice. Cutaneous and disseminated infection with squirrel fibroma virus (SFV).
[So] Source:J Am Vet Med Assoc;245(4):389-91, 2014 Aug 15.
[Is] ISSN:1943-569X
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Leporipoxvirus/isolamento & purificação
Sciuridae
Dermatopatias Virais/veterinária
[Mh] Termos MeSH secundário: Animais
Feminino
Masculino
Dermatopatias Virais/patologia
Dermatopatias Virais/virologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1503
[Cu] Atualização por classe:140731
[Lr] Data última revisão:
140731
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140731
[St] Status:MEDLINE
[do] DOI:10.2460/javma.245.4.389


  3 / 12 MEDLINE  
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[PMID]:23864636
[Au] Autor:Varjak M; Saul S; Arike L; Lulla A; Peil L; Merits A
[Ad] Endereço:Institute of Technology, University of Tartu, Tartu, Estonia.
[Ti] Título:Magnetic fractionation and proteomic dissection of cellular organelles occupied by the late replication complexes of Semliki Forest virus.
[So] Source:J Virol;87(18):10295-312, 2013 Sep.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Alphavirus replicase complexes are initially formed at the plasma membrane and are subsequently internalized by endocytosis. During the late stages of infection, viral replication organelles are represented by large cytopathic vacuoles, where replicase complexes bind to membranes of endolysosomal origin. In addition to viral components, these organelles harbor an unknown number of host proteins. In this study, a fraction of modified lysosomes carrying functionally intact replicase complexes was obtained by feeding Semliki Forest virus (SFV)-infected HeLa cells with dextran-covered magnetic nanoparticles and later magnetically isolating the nanoparticle-containing lysosomes. Stable isotope labeling with amino acids in cell culture combined with quantitative proteomics was used to reveal 78 distinct cellular proteins that were at least 2.5-fold more abundant in replicase complex-carrying vesicles than in vesicles obtained from noninfected cells. These host components included the RNA-binding proteins PCBP1, hnRNP M, hnRNP C, and hnRNP K, which were shown to colocalize with the viral replicase. Silencing of hnRNP M and hnRNP C expression enhanced the replication of SFV, Chikungunya virus (CHIKV), and Sindbis virus (SINV). PCBP1 silencing decreased SFV-mediated protein synthesis, whereas hnRNP K silencing increased this synthesis. Notably, the effect of hnRNP K silencing on CHIKV- and SINV-mediated protein synthesis was opposite to that observed for SFV. This study provides a new approach for analyzing the proteome of the virus replication organelle of positive-strand RNA viruses and helps to elucidate how host RNA-binding proteins exert important but diverse functions during positive-strand RNA viral infection.
[Mh] Termos MeSH primário: Células Epiteliais/virologia
Interações Hospedeiro-Patógeno
Lisossomos/virologia
Proteoma/análise
Vírus da Floresta de Semliki/fisiologia
Replicação Viral
[Mh] Termos MeSH secundário: Alphavirus
Vírus Chikungunya
Células Epiteliais/química
Células HeLa
Seres Humanos
Marcação por Isótopo
Leporipoxvirus
Lisossomos/química
Magnetismo
Proteômica/métodos
Vírus da Floresta de Semliki/crescimento & desenvolvimento
Vírus Sindbis
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Proteome)
[Em] Mês de entrada:1311
[Cu] Atualização por classe:150423
[Lr] Data última revisão:
150423
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130719
[St] Status:MEDLINE
[do] DOI:10.1128/JVI.01105-13


  4 / 12 MEDLINE  
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[PMID]:19276066
[Au] Autor:Bangari DS; Miller MA; Stevenson GW; Thacker HL; Sharma A; Mittal SK
[Ad] Endereço:Department of Comparative Pathobiology, College of Veterinary Medicine, Purdue University, 406 S. University Street, West Lafayette, IN 47907, USA. dsingh@purdue.edu
[Ti] Título:Cutaneous and systemic poxviral disease in red (Tamiasciurus hudsonicus) and gray (Sciurus carolinensis) squirrels.
[So] Source:Vet Pathol;46(4):667-72, 2009 Jul.
[Is] ISSN:1544-2217
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:From September 2005 through October 2006, fibromatosis was diagnosed in 2 red squirrels (Tamiasciurus hudsonicus) and 1 gray squirrel (Sciurus carolinensis). All 3 squirrels had multifocal to coalescing, tan, firm alopecic cutaneous nodules. Two squirrels also had pulmonary nodules. Histologically, the cutaneous nodules had marked epidermal hyperplasia, with ballooning degeneration of keratinocytes, spongiosis, and eosinophilic cytoplasmic inclusions. The dermis was expanded by proliferation of atypical mesenchymal cells with cytoplasmic inclusions. Additional findings included pulmonary adenomatous hyperplasia with cytoplasmic inclusions, renal tubular epithelial hyperplasia with cytoplasmic inclusions, atypical mesenchymal proliferation in the liver, and atypical mesenchymal proliferation with cytoplasmic inclusions in the seminal vesicles. Ultrastructurally, poxviral particles were observed in skin scrapings and sections of cutaneous and pulmonary nodules. Polymerase chain reaction targeting the highly conserved Leporipoxvirus DNA polymerase gene was positive using DNA extracted from the cutaneous lesions of all 3 squirrels. Nucleotide sequence of the 390 base PCR amplicons was closely related to that of other members of the genus Leporipoxvirus. To the authors' knowledge, this is the first report of cutaneous and systemic poxviral disease in American red squirrels with molecular characterization of the squirrel fibroma virus.
[Mh] Termos MeSH primário: Fibroma/veterinária
Leporipoxvirus/genética
Infecções por Poxviridae/veterinária
Doenças dos Roedores/patologia
Doenças dos Roedores/virologia
Sciuridae
Infecções Tumorais por Vírus/veterinária
[Mh] Termos MeSH secundário: Animais
Sequência de Bases
Análise por Conglomerados
Fibroma/patologia
Fibroma/virologia
Queratinócitos/ultraestrutura
Microscopia Eletrônica de Transmissão
Dados de Sequência Molecular
Filogenia
Reação em Cadeia da Polimerase
Infecções por Poxviridae/patologia
Análise de Sequência de DNA
Especificidade da Espécie
Infecções Tumorais por Vírus/patologia
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Em] Mês de entrada:0910
[Cu] Atualização por classe:090629
[Lr] Data última revisão:
090629
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:090312
[St] Status:MEDLINE
[do] DOI:10.1354/vp.08-VP-0305-B-BC


  5 / 12 MEDLINE  
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[PMID]:15827194
[Au] Autor:Teoh ML; Turner PV; Evans DH
[Ad] Endereço:Dept. of Medical Microbiology and Immunology, University of Alberta, 141 Medical Sciences Building, Edmonton, AB T6G 2H7, Canada.
[Ti] Título:Tumorigenic poxviruses up-regulate intracellular superoxide to inhibit apoptosis and promote cell proliferation.
[So] Source:J Virol;79(9):5799-811, 2005 May.
[Is] ISSN:0022-538X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Tumorigenic leporipoxviruses encode catalytically inactive homologs of cellular Cu-Zn superoxide dismutase (SOD1). The function of the orthologous myxoma virus M131R and Shope fibroma virus S131R gene products is uncertain, but they inhibit SOD1 activity by a process linked to binding its copper chaperone. Using a superoxide-sensitive dye (hydroethidine), we observed that virus infection increased intracellular superoxide levels in an M/S131R-dependent manner. To see whether this effect promotes infection, we deleted the Shope fibroma virus S131R gene and compared the clinical manifestations of wild-type and mutant virus infections in rabbits. S131RDelta virus produced significantly smaller fibroxanthosarcoma-like growths in vivo and, at a point where these growths were already receding, wild-type infections still showed extensive leukocyte infiltration, necrosis, and fibromatous cell proliferation. Coincidentally, whereas Jurkat cells are protected from mitochondria- and Fas-mediated apoptosis by wild-type myxoma virus in vitro, M131RDelta virus could not block Fas-initiated apoptosis as judged by DNA laddering, terminal deoxynucleotidyltransferase-mediated dUTP-fluorescein nick end labeling, and caspase 3 cleavage assays. These data suggest that tumorigenic poxviruses can modulate intracellular redox status to their advantage to stimulate infected cell growth and inhibit programmed cell death.
[Mh] Termos MeSH primário: Apoptose
Divisão Celular
Leporipoxvirus/fisiologia
Infecções por Poxviridae/virologia
Superóxido Dismutase/fisiologia
Infecções Tumorais por Vírus/virologia
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Modelos Animais de Doenças
Feminino
Leporipoxvirus/metabolismo
Oxirredução
Coelhos
Superóxido Dismutase/metabolismo
Superóxido Dismutase-1
Regulação para Cima
Fatores de Virulência
Zinco/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Virulence Factors); EC 1.15.1.1 (Superoxide Dismutase); EC 1.15.1.1 (Superoxide Dismutase-1); J41CSQ7QDS (Zinc)
[Em] Mês de entrada:0506
[Cu] Atualização por classe:170219
[Lr] Data última revisão:
170219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:050414
[St] Status:MEDLINE


  6 / 12 MEDLINE  
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[PMID]:15114007
[Au] Autor:Yao XD; Evans DH
[Ad] Endereço:Department of Molecular Biology & Genetics, University of Guelph, Guelph, Ontario, Canada.
[Ti] Título:Construction of recombinant vaccinia viruses using leporipoxvirus-catalyzed recombination and reactivation of orthopoxvirus DNA.
[So] Source:Methods Mol Biol;269:51-64, 2004.
[Is] ISSN:1064-3745
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Poxvirus DNA is not infectious because the initiation of the infective process requires proteins encapsidated along with the virus genome. However, infectious virus can be produced if purified poxvirus DNA is transfected into cells previously infected with another poxvirus. This process is termed heterologous reactivation if the infecting virus is different from the transfected virus. We describe a method in which the high-frequency recombination and replication reactions catalyzed by the Leporipoxvirus, Shope fibroma virus (SFV), can be coupled with SFV-promoted reactivation reactions to rapidly construct recombinant vaccinia viruses in high yields (25-100% recombinant progeny). The reactivated vaccinia viruses are easily purified free of the SFV helper virus by plating mixed populations of virus on cells that support only the growth of vaccinia virus. These heterologous reactivation reactions can be used to manipulate the structure of virus genomes and produce viruses that express recombinant proteins at high levels. We illustrate the method by polymerase chain reaction (PCR) cloning the gene encoding green fluorescent protein (GFP), then using double-strand break repair reactions to produce a recombinant virus that expresses high levels of GFP.
[Mh] Termos MeSH primário: DNA Viral/genética
Leporipoxvirus/genética
Orthopoxvirus/genética
Vírus Vaccinia/genética
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Cricetinae
Leporipoxvirus/fisiologia
Orthopoxvirus/fisiologia
Recombinação Genética
Vírus Vaccinia/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (DNA, Viral)
[Em] Mês de entrada:0408
[Cu] Atualização por classe:051117
[Lr] Data última revisão:
051117
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:040429
[St] Status:MEDLINE


  7 / 12 MEDLINE  
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[PMID]:12805426
[Au] Autor:Yao XD; Evans DH
[Ad] Endereço:Department of Molecular Biology & Genetics, University of Guelph, Guelph, Ontario N1G 2W1, Canada.
[Ti] Título:High-frequency genetic recombination and reactivation of orthopoxviruses from DNA fragments transfected into leporipoxvirus-infected cells.
[So] Source:J Virol;77(13):7281-90, 2003 Jul.
[Is] ISSN:0022-538X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Poxvirus DNA is not infectious because establishing an infection requires the activities of enzymes packaged in the virion. This barrier can be overcome by transfecting virus DNA into cells previously infected with another poxvirus, since the resident virus can provide the trans-acting systems needed to reactivate transfected DNA. In this study we show that cells infected with a leporipoxvirus, Shope fibroma virus (SFV), can reactivate vaccinia virus DNA. Similar heterologous packaging systems which used fowlpox-infected cells to reactivate vaccinia virus have been described, but SFV-infected cells promoted a far more efficient reaction that can produce virus titers exceeding 10(6) PFU/ micro g of transfected DNA. SFV-promoted reactions also exploit the hyperrecombinogenic systems previously characterized in SFV-infected cells, and these coupled recombination and reactivation reactions could be used to delete nonessential regions of the vaccinia virus genome and to reconstruct vaccinia virus from overlapping DNA fragments. SFV-catalyzed recombination reactions need only two 18- to 20-bp homologies to target PCR amplicons to restriction enzyme-cut vaccinia virus vectors, and this reaction feature was used to rapidly clone and express a gene encoding fluorescent green protein without the need for plaque purification or selectable markers. The ability of SFV-infected cells to reactivate fragments of vaccinia virus was ultimately limited by the number of recombinational exchanges required and one cannot reconstruct vaccinia virus from multiple PCR fragments spanning essential portions of the genome. These observations suggest that recombination is an integral part of poxvirus reactivation reactions and provide a useful new technique for altering the structure of poxvirus genomes.
[Mh] Termos MeSH primário: DNA Viral/genética
Leporipoxvirus/genética
Orthopoxvirus/genética
Recombinação Genética
Ativação Viral
[Mh] Termos MeSH secundário: Animais
Sequência de Bases
Linhagem Celular
Cricetinae
Dano ao DNA
Reparo do DNA
Leporipoxvirus/fisiologia
Microscopia Confocal
Orthopoxvirus/fisiologia
Reação em Cadeia da Polimerase
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA, Viral)
[Em] Mês de entrada:0308
[Cu] Atualização por classe:140611
[Lr] Data última revisão:
140611
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:030614
[St] Status:MEDLINE


  8 / 12 MEDLINE  
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[PMID]:12773543
[Au] Autor:Teoh ML; Walasek PJ; Evans DH
[Ad] Endereço:Department of Molecular Biology & Genetics, University of Guelph, Guelph, Ontario N1G 2W1, Canada.
[Ti] Título:Leporipoxvirus Cu,Zn-superoxide dismutase (SOD) homologs are catalytically inert decoy proteins that bind copper chaperone for SOD.
[So] Source:J Biol Chem;278(35):33175-84, 2003 Aug 29.
[Is] ISSN:0021-9258
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Many Chordopoxviruses encode catalytically inactive homologs of cellular Cu-Zn superoxide dismutase (SOD). The biological function of these proteins is unknown, although the proteins encoded by Leporipoxviruses have been shown to promote a slow decline in the level of superoxide dismutase activity in virus-infected cells. To gain more insights into their function, we have further characterized the enzymatic and biochemical properties of a SOD homolog encoded by Shope fibroma virus. Shope fibroma virus SOD has retained the zinc binding properties of its cellular homolog, but cannot bind copper. Site-directed mutagenesis showed that it requires at least four amino acid substitutions to partially restore copper binding activity, but even these changes still did not restore catalytic activity. Reciprocal co-immunoprecipitation experiments showed that recombinant Shope fibroma virus SOD forms very stable complexes with cellular copper chaperones for SOD and these observations were confirmed using glutathione-S-transferase tagged proteins. Similar viral SOD/chaperone complexes were formed in cells infected with a closely related myxoma virus, where we also noted that some of the SOD antigen co-localizes with mitochondrial markers using confocal fluorescence microscopy. About 2% of the viral SOD was subsequently detected in gradient-purified mitochondria extracted from virus-infected cells. These poxviral SOD homologs do not form stable complexes with cellular Cu,Zn-SOD or affect its concentration. We suggest that Leporipoxvirus SOD homologs are catalytically inert decoy proteins that are designed to interfere in the proper metallation and activation of cellular Cu,Zn-SOD. This reaction might be advantageous for tumorigenic poxviruses, since higher levels of superoxide have been proposed to have anti-apoptotic and tumorigenic activity.
[Mh] Termos MeSH primário: Cobre/metabolismo
Leporipoxvirus/enzimologia
Superóxido Dismutase/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Western Blotting
Catálise
Eletroforese em Gel de Poliacrilamida
Vírus do Fibroma dos Coelhos/enzimologia
Glutationa Transferase/metabolismo
Seres Humanos
Metais/farmacologia
Microscopia Confocal
Mitocôndrias/metabolismo
Dados de Sequência Molecular
Mutagênese Sítio-Dirigida
Mutação
Mixoma/metabolismo
Myxoma virus/enzimologia
Filogenia
Plasmídeos/metabolismo
Testes de Precipitina
Ligação Proteica
Proteínas Recombinantes/metabolismo
Homologia de Sequência de Aminoácidos
Superóxido Dismutase/metabolismo
Zinco/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Metals); 0 (Recombinant Proteins); 789U1901C5 (Copper); EC 1.15.1.1 (Superoxide Dismutase); EC 2.5.1.18 (Glutathione Transferase); J41CSQ7QDS (Zinc)
[Em] Mês de entrada:0310
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:030530
[St] Status:MEDLINE


  9 / 12 MEDLINE  
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[PMID]:12036324
[Au] Autor:Cao JX; Teoh ML; Moon M; McFadden G; Evans DH
[Ad] Endereço:Robarts Research Institute, The University of Western Ontario, London, Ontario, Canada.
[Ti] Título:Leporipoxvirus Cu-Zn superoxide dismutase homologs inhibit cellular superoxide dismutase, but are not essential for virus replication or virulence.
[So] Source:Virology;296(1):125-35, 2002 Apr 25.
[Is] ISSN:0042-6822
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Vertebrate poxviruses encode homologs of cellular cupro-zinc superoxide dismutases (Cu-Zn SOD). In this study we have examined the molecular genetic properties of two Cu-Zn SOD homologs encoded by the Shope fibroma virus (SFV) and myxoma virus. These Leporipoxvirus proteins should be catalytically inactive as judged by the point mutations which alter a key catalytic arginine and restructure the predicted Cu-binding domain. This prediction was confirmed using in situ gel assays and recombinant proteins produced both in bacteria and in mammalian cells. Western blot analysis showed that these proteins are produced in abundance late in infection and can, upon exposure to oxidizing conditions, form disulfide cross-linked dimers. They are also virion components and not essential for growth in culture or virulence. Leporipoxvirus Cu-Zn SOD homologs affected two phenotypes. First, deletion of the myxoma M131R gene caused the mutant virus to grow better ( approximately 10-fold) in culture than does the wild-type parent. Second, expression of either native or recombinant Leporipoxvirus proteins is accompanied by a decline in cellular Cu-Zn SOD activity. We concluded that these gene products can somehow modulate the activity of host Cu-Zn SODs, but what advantage is thus gained by the virus remains to be established.
[Mh] Termos MeSH primário: Leporipoxvirus/patogenicidade
Superóxido Dismutase/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Catálise
Células Cultivadas
Modelos Animais de Doenças
Regulação para Baixo
Vírus do Fibroma dos Coelhos/genética
Vírus do Fibroma dos Coelhos/metabolismo
Deleção de Genes
Genoma Viral
Haplorrinos
Leporipoxvirus/enzimologia
Dados de Sequência Molecular
Myxoma virus/genética
Myxoma virus/metabolismo
Coelhos
Alinhamento de Sequência
Superóxido Dismutase/biossíntese
Superóxido Dismutase/genética
Virulência
Replicação Viral
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 1.15.1.1 (Superoxide Dismutase)
[Em] Mês de entrada:0207
[Cu] Atualização por classe:061115
[Lr] Data última revisão:
061115
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:020531
[St] Status:MEDLINE


  10 / 12 MEDLINE  
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[PMID]:10562495
[Au] Autor:Willer DO; McFadden G; Evans DH
[Ad] Endereço:Department of Molecular Biology, The University of Guelph, Guelph, Ontario, N1G 2W1, Canada.
[Ti] Título:The complete genome sequence of shope (rabbit) fibroma virus.
[So] Source:Virology;264(2):319-43, 1999 Nov 25.
[Is] ISSN:0042-6822
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We have determined the complete DNA sequence of the Leporipoxvirus Shope fibroma virus (SFV). The SFV genome spans 159.8 kb and encodes 165 putative genes of which 13 are duplicated in the 12.4-kb terminal inverted repeats. Although most SFV genes have homologs encoded by other Chordopoxvirinae, the SFV genome lacks a key gene required for the production of extracellular enveloped virus. SFV also encodes only the smaller ribonucleotide reductase subunit and has a limited nucleotide biosynthetic capacity. SFV preserves the Chordopoxvirinae gene order from S012L near the left end of the chromosome through to S142R (homologs of vaccinia F2L and B1R, respectively). The unique right end of SFV appears to be genetically unstable because when the sequence is compared with that of myxoma virus, five myxoma homologs have been deleted (C. Cameron, S. Hota-Mitchell, L. Chen, J. Barrett, J.-X. Cao, C. Macaulay, D. Willer, D. Evans, and G. McFadden, 1999, Virology 264, 298-318). Most other differences between these two Leporipoxviruses are located in the telomeres. Leporipoxviruses encode several genes not found in other poxviruses including four small hydrophobic proteins of unknown function (S023R, S119L, S125R, and S132L), an alpha 2, 3-sialyltransferase (S143R), a protein belonging to the Ig-like protein superfamily (S141R), and a protein resembling the DNA-binding domain of proteins belonging to the HIN-200 protein family S013L). SFV also encodes a type II DNA photolyase (S127L). Melanoplus sanguinipes entomopoxvirus encodes a similar protein, but SFV is the first mammalian virus potentially capable of photoreactivating ultraviolet DNA damage.
[Mh] Termos MeSH primário: DNA Viral/análise
Vírus do Fibroma dos Coelhos/genética
Genoma Viral
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Sequência de Bases
Linhagem Celular
Regulação Viral da Expressão Gênica
Genes Virais
Seres Humanos
Leporipoxvirus/genética
Dados de Sequência Molecular
Vírus do Molusco Contagioso/genética
Coelhos
Sequências Repetitivas de Ácido Nucleico
Homologia de Sequência de Aminoácidos
Superóxido Dismutase/genética
Transcrição Genética
Vírus Vaccinia/genética
Vírus da Varíola/genética
Proteínas Virais/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA, Viral); 0 (Viral Proteins); EC 1.15.1.1 (Superoxide Dismutase)
[Em] Mês de entrada:0001
[Cu] Atualização por classe:091231
[Lr] Data última revisão:
091231
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:991124
[St] Status:MEDLINE



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