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[PMID]:27170418
[Au] Autor:Singh PK; Subbarao SM
[Ad] Endereço:Department of Biochemistry, Indian Institute of Science, Bangalore, 560012, India.
[Ti] Título:The RNA triphosphatase domain of L protein of Rinderpest virus exhibits pyrophosphatase and tripolyphosphatase activities.
[So] Source:Virus Genes;52(5):743-7, 2016 Oct.
[Is] ISSN:1572-994X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:L protein of the Rinderpest virus, an archetypal paramyxovirus possesses RNA-dependent RNA polymerase activity which transcribes the genome into mRNAs as well as replicates the RNA genome. The protein also possesses RNA triphosphatase (RTPase), guanylyltransferase (GTase) and methyltransferase enzyme activities responsible for capping the mRNAs in a conventional pathway similar to that of the host pathway. Subsequent to the earlier characterization of the GTase activity of L protein and identification of the RTPase domain of the L protein, we report here, additional enzymatic activities associated with the RTPase domain. We have characterized the pyrophosphatase and tripolyphosphatase activities of the L-RTPase domain which are metal-dependent and proceed much faster than the RTPase activity. Interestingly, the mutant proteins E1645A and E1647A abrogated the pyrophosphatase and tripolyphosphatase significantly, indicating a strong overlap of the active sites of these activities with that of RTPase. We discuss the likely role of GTase-associated L protein pyrophosphatase in the polymerase function. We also discuss a possible biological role for the tripolyphosphatase activity hitherto considered insignificant for the viruses possessing such activity.
[Mh] Termos MeSH primário: Hidrolases Anidrido Ácido/metabolismo
Pirofosfatases/metabolismo
Vírus da Peste Bovina/metabolismo
Proteínas Virais/metabolismo
[Mh] Termos MeSH secundário: Escherichia coli/metabolismo
Nucleotidiltransferases/metabolismo
Capuzes de RNA/metabolismo
RNA Replicase/metabolismo
RNA Mensageiro/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA Caps); 0 (RNA, Messenger); 0 (Viral Proteins); EC 2.7.7.- (Nucleotidyltransferases); EC 2.7.7.- (guanylyltransferase); EC 2.7.7.48 (RNA Replicase); EC 3.6.- (Acid Anhydride Hydrolases); EC 3.6.1.- (Pyrophosphatases); EC 3.6.1.- (RNA triphosphatase); EC 3.6.1.- (tripolyphosphatase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160513
[St] Status:MEDLINE
[do] DOI:10.1007/s11262-016-1353-7


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[PMID]:26984722
[Au] Autor:Holzer B; Hodgson S; Logan N; Willett B; Baron MD
[Ad] Endereço:The Pirbright Institute, Pirbright, Surrey, United Kingdom.
[Ti] Título:Protection of Cattle against Rinderpest by Vaccination with Wild-Type but Not Attenuated Strains of Peste des Petits Ruminants Virus.
[So] Source:J Virol;90(10):5152-62, 2016 05 15.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:UNLABELLED: Although rinderpest virus (RPV) has been eradicated in the wild, efforts are still continuing to restrict the extent to which live virus is distributed in facilities around the world and to prepare for any reappearance of the disease, whether through deliberate or accidental release. In an effort to find an alternative vaccine which could be used in place of the traditional live attenuated RPV strains, we have determined whether cattle can be protected from rinderpest by inoculation with vaccine strains of the related morbillivirus, peste des petits ruminants virus (PPRV). Cattle were vaccinated with wild-type PPRV or either of two established PPRV vaccine strains, Nigeria/75/1 or Sungri/96. All animals developed antibody and T cell immune responses to the inoculated PPRV. However, only the animals given wild-type PPRV were protected from RPV challenge. Animals given PPRV/Sungri/96 were only partially protected, and animals given PPRV/Nigeria/75/1 showed no protection against RPV challenge. While sera from animals vaccinated with the vaccine strain of RPV showed cross-neutralizing ability against PPRV, none of the sera from animals vaccinated with any strain of PPRV was able to neutralize RPV although sera from animals inoculated with wild-type PPRV were able to neutralize RPV-pseudotyped vesicular stomatitis virus. IMPORTANCE: Rinderpest virus has been eradicated, and it is only the second virus for which this is so. Significant efforts are still required to ensure preparedness for a possible escape of RPV from a laboratory or its deliberate release. Since RPV vaccine protects sheep and goats from PPRV, it is important to determine if the reverse is true as this would provide a non-RPV vaccine for dealing with suspected RPV outbreaks. This is probably the last in vivo study with live RPV that will be approved.
[Mh] Termos MeSH primário: Doenças dos Bovinos/prevenção & controle
Vírus da Peste dos Pequenos Ruminantes/imunologia
Vírus da Peste Bovina/imunologia
Peste Bovina/prevenção & controle
Vacinas Virais/imunologia
[Mh] Termos MeSH secundário: Animais
Anticorpos Antivirais/imunologia
Bovinos
Doenças dos Bovinos/virologia
Reações Cruzadas
Ensaio de Imunoadsorção Enzimática
Peste dos Pequenos Ruminantes/imunologia
Vírus da Peste dos Pequenos Ruminantes/genética
Vírus da Peste dos Pequenos Ruminantes/patogenicidade
Peste Bovina/virologia
Vacinação/veterinária
Vacinas Atenuadas/administração & dosagem
Vacinas Atenuadas/imunologia
Vacinas Virais/administração & dosagem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibodies, Viral); 0 (Vaccines, Attenuated); 0 (Viral Vaccines)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160318
[St] Status:MEDLINE
[do] DOI:10.1128/JVI.00040-16


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[PMID]:26506137
[Au] Autor:Berguido FJ; Bodjo SC; Loitsch A; Diallo A
[Ad] Endereço:Animal Production and Health Laboratory, FAO/IAEA Agriculture and & Biotechnology Laboratory, IAEA Laboratories Seibersdorf, International Atomic Energy Agency (IAEA), Wagramer Strasse 5, P.O. Box 100, A1400, Vienna, Austria. Electronic address: f.berguido@iaea.org.
[Ti] Título:Specific detection of peste des petits ruminants virus antibodies in sheep and goat sera by the luciferase immunoprecipitation system.
[So] Source:J Virol Methods;227:40-6, 2016 Jan.
[Is] ISSN:1879-0984
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Peste des petits ruminants (PPR) is a contagious and often fatal transboundary animal disease affecting mostly sheep, goats and wild small ruminants. This disease is endemic in most of Africa, the Middle, Near East, and large parts of Asia. The causal agent is peste des petits ruminants virus (PPRV), which belongs to the genus Morbillivirus in the family Paramyxoviridae. This genus also includes measles virus (MV), canine distemper virus (CDV) and rinderpest virus (RPV). All are closely related viruses with serological cross reactivity. In this study, we have developed a Luciferase Immunoprecipitation System (LIPS) for the rapid detection of antibodies against PPRV in serum samples and for specific differentiation from antibodies against RPV. PPR and rinderpest (RP) serum samples were assayed by PPR-LIPS and two commercially available PPR cELISA tests. The PPR-LIPS showed high sensitivity and specificity for the samples tested and showed no cross reactivity with RPV unlike the commercial PPR cELISA tests which did cross react with RPV. Based on the results shown in this study, PPR-LIPS is presented as a good candidate for the specific serosurveillance of PPR.
[Mh] Termos MeSH primário: Anticorpos Antivirais/sangue
Ensaio de Imunoadsorção Enzimática/métodos
Cabras/imunologia
Vírus da Peste dos Pequenos Ruminantes/imunologia
Vírus da Peste Bovina/imunologia
Ovinos/imunologia
[Mh] Termos MeSH secundário: Animais
Anticorpos Antivirais/imunologia
Cabras/sangue
Cabras/virologia
Imunoprecipitação
Luciferases
Peste dos Pequenos Ruminantes/diagnóstico
Peste dos Pequenos Ruminantes/imunologia
Peste dos Pequenos Ruminantes/virologia
Sensibilidade e Especificidade
Ovinos/sangue
Ovinos/virologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Antibodies, Viral); EC 1.13.12.- (Luciferases)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:151209
[Lr] Data última revisão:
151209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151028
[St] Status:MEDLINE


  4 / 473 MEDLINE  
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[PMID]:26584400
[Au] Autor:Hamilton K; Visser D; Evans B; Vallat B
[Ti] Título:Identifying and Reducing Remaining Stocks of Rinderpest Virus.
[So] Source:Emerg Infect Dis;21(12):2117-21, 2015 Dec.
[Is] ISSN:1080-6059
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In 2011, the world was declared free from rinderpest, one of the most feared and devastating infectious diseases of animals. Rinderpest is the second infectious disease, after smallpox, to have been eradicated. However, potentially infectious rinderpest virus material remains widely disseminated among research and diagnostic facilities across the world and poses a risk for disease recurrence should it be released. Member Countries of the World Organisation for Animal Health and the Food and Agricultural Organization of the United Nations are committed to destroying remaining stocks of infectious material or ensuring that it is stored under international supervision in a limited number of approved facilities. To facilitate this commitment and maintain global freedom from rinderpest, World Organisation for Animal Health Member Countries must report annually on rinderpest material held in their countries. The first official surveys, conducted during 2013-2015, revealed that rinderpest material was stored in an unacceptably high number of facilities and countries.
[Mh] Termos MeSH primário: Doenças Transmissíveis
Erradicação de Doenças
Vírus da Peste Bovina
[Mh] Termos MeSH secundário: Animais
Bovinos/virologia
Saúde Global
Inquéritos e Questionários
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1607
[Cu] Atualização por classe:151209
[Lr] Data última revisão:
151209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151120
[St] Status:MEDLINE
[do] DOI:10.3201/eid2112.150227


  5 / 473 MEDLINE  
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[PMID]:26446666
[Au] Autor:Gopinath M; Shaila MS
[Ad] Endereço:Department of Microbiology and Cell Biology, Indian Institute of Science, Bangalore, 560012, India.
[Ti] Título:Evidence for N7 guanine methyl transferase activity encoded within the modular domain of RNA-dependent RNA polymerase L of a Morbillivirus.
[So] Source:Virus Genes;51(3):356-60, 2015 Dec.
[Is] ISSN:1572-994X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Post-transcriptional modification of viral mRNA is essential for the translation of viral proteins by cellular translation machinery. Due to the cytoplasmic replication of Paramyxoviruses, the viral-encoded RNA-dependent RNA polymerase (RdRP) is thought to possess all activities required for mRNA capping and methylation. In the present work, using partially purified recombinant RNA polymerase complex of rinderpest virus expressed in insect cells, we demonstrate the in vitro methylation of capped mRNA. Further, we show that a recombinant C-terminal fragment (1717-2183 aa) of L protein is capable of methylating capped mRNA, suggesting that the various post-transcriptional activities of the L protein are located in independently folding domains.
[Mh] Termos MeSH primário: Metiltransferases/genética
Metiltransferases/metabolismo
RNA Replicase/genética
RNA Replicase/metabolismo
Vírus da Peste Bovina/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Seres Humanos
Insetos Vetores/genética
Dados de Sequência Molecular
Capuzes de RNA
RNA Mensageiro/genética
RNA Viral/genética
Vírus da Peste Bovina/genética
Homologia de Sequência de Aminoácidos
Transcrição Genética
Proteínas Virais/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (L protein, paramyxoviridae); 0 (RNA Caps); 0 (RNA, Messenger); 0 (RNA, Viral); 0 (Viral Proteins); EC 2.1.1.- (Methyltransferases); EC 2.1.1.56 (mRNA (guanine(N7))-methyltransferase); EC 2.7.7.48 (RNA Replicase)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151009
[St] Status:MEDLINE
[do] DOI:10.1007/s11262-015-1252-3


  6 / 473 MEDLINE  
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[PMID]:26168720
[Au] Autor:Singh PK; Ratnam N; Narayanarao KB; Bugatha H; Karande AA; Melkote Subbarao S
[Ad] Endereço:Department of Biochemistry, Indian Institute of Science, Bangalore 560012, India.
[Ti] Título:A carboxy terminal domain of the L protein of rinderpest virus possesses RNA triphosphatase activity - The first enzyme in the viral mRNA capping pathway.
[So] Source:Biochem Biophys Res Commun;464(2):629-34, 2015 Aug 21.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The large protein L of negative-sense RNA viruses is a multifunctional protein involved in transcription and replication of genomic RNA. It also possesses enzymatic activities involved in capping and methylation of viral mRNAs. The pathway for mRNA capping followed by the L protein of the viruses in the Morbillivirus genus has not been established, although it has been speculated that these viruses may follow the unconventional capping pathway as has been shown for some viruses of Rhabdoviridae family. We had earlier shown that the large protein L of Rinderpest virus expressed as recombinant L-P complex in insect cells as well as the ribonucleoprotein complex from purified virus possesses RNA triphosphatase (RTPase) and guanylyltransferase activities, in addition to RNA dependent RNA polymerase activity. In the present work, we demonstrate that RTPase as well as nucleoside triphosphatase (NTPase) activities are exhibited by a subdomain of the L protein in the C terminal region (a.a. 1640-1840). The RTPase activity depends absolutely on a divalent cation, either magnesium or manganese. Both the RTPase and NTPase activities of the protein show dual metal specificity. Two mutant proteins having alanine mutations in the glutamic acid residues in motif-A of the RTPase domain did not show RTPase activity, while exhibiting reduced NTPase activity suggesting overlapping active sites for the two enzymatic functions. The RTPase and NTPase activities of the L subdomain resemble those of the Vaccinia capping enzyme D1 and the baculovirus LEF4 proteins.
[Mh] Termos MeSH primário: Hidrolases Anidrido Ácido/metabolismo
Capuzes de RNA
RNA Viral/metabolismo
Vírus da Peste Bovina/química
Proteínas Virais/metabolismo
[Mh] Termos MeSH secundário: Hidrolases Anidrido Ácido/química
Sequência de Aminoácidos
Dados de Sequência Molecular
Homologia de Sequência de Aminoácidos
Proteínas Virais/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (RNA Caps); 0 (RNA, Viral); 0 (Viral Proteins); EC 3.6.- (Acid Anhydride Hydrolases); EC 3.6.1.- (RNA triphosphatase)
[Em] Mês de entrada:1511
[Cu] Atualização por classe:150803
[Lr] Data última revisão:
150803
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150715
[St] Status:MEDLINE


  7 / 473 MEDLINE  
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[PMID]:24703852
[Au] Autor:Buczkowski H; Muniraju M; Parida S; Banyard AC
[Ad] Endereço:Animal Health and Veterinary Laboratories Agency, Woodham Lane, Weybridge, Surrey, KT15 3NB, United Kingdom.
[Ti] Título:Morbillivirus vaccines: recent successes and future hopes.
[So] Source:Vaccine;32(26):3155-61, 2014 May 30.
[Is] ISSN:1873-2518
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The impact of morbilliviruses on both human and animal populations is well documented in the history of mankind. Indeed, prior to the development of vaccines for these diseases, morbilliviruses plagued both humans and their livestock that were heavily relied upon for food and motor power within communities. Measles virus (MeV) was responsible for the death of millions of people annually across the world and those fortunate enough to escape the disease often faced starvation where their livestock had died following infection with rinderpest virus (RPV) or peste des petits ruminants virus (PPRV). Canine distemper virus has affected dog populations for centuries and in the past few decades appears to have jumped species, now causing disease in a number of non-canid species, some of which are been pushed to the brink of extinction by the virus. During the age of vaccination, the introduction and successful application of vaccines against rinderpest and measles has led to the eradication of the former and the greater control of the latter. Vaccines against PPR and canine distemper have also been generated; however, the diseases still pose a threat to susceptible species. Here we review the currently available vaccines against these four morbilliviruses and discuss the prospects for the development of new generation vaccines.
[Mh] Termos MeSH primário: Infecções por Morbillivirus/prevenção & controle
Morbillivirus
Vacinas Virais/uso terapêutico
[Mh] Termos MeSH secundário: Animais
Vírus da Cinomose Canina
Cães
História do Século XX
História do Século XXI
Seres Humanos
Vírus do Sarampo
Vírus da Peste dos Pequenos Ruminantes
Vírus da Peste Bovina
Ruminantes
Vacinação/história
Vacinas Atenuadas/uso terapêutico
Vacinas de DNA/uso terapêutico
[Pt] Tipo de publicação:HISTORICAL ARTICLE; JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Vaccines, Attenuated); 0 (Vaccines, DNA); 0 (Viral Vaccines)
[Em] Mês de entrada:1411
[Cu] Atualização por classe:171110
[Lr] Data última revisão:
171110
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140408
[St] Status:MEDLINE


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[PMID]:24566884
[Au] Autor:Moutou F
[Ad] Endereço:42, rue de l'Est, 92100, Boulogne-Billancourt, France, francoismoutou@orange.fr.
[Ti] Título:The second eradication: rinderpest.
[So] Source:Bull Soc Pathol Exot;107(3):137-8, 135-6, 2014 Aug.
[Is] ISSN:0037-9085
[Cp] País de publicação:France
[La] Idioma:eng; fre
[Ab] Resumo:The eradication of rinderpest virus was less celebrated than the eradication of smallpox virus. However, this is only the second campaign to eradicate a virus worldwide which is successful. This gives the opportunity to recall how important rinderpest had been these past centuries for farmers and for public health.
[Mh] Termos MeSH primário: Erradicação de Doenças/métodos
Peste Bovina/prevenção & controle
[Mh] Termos MeSH secundário: Animais
Bovinos
Doenças dos Bovinos/prevenção & controle
Doenças dos Bovinos/virologia
Seres Humanos
Vacinação em Massa/veterinária
Vírus da Peste Bovina/patogenicidade
[Pt] Tipo de publicação:EDITORIAL
[Em] Mês de entrada:1504
[Cu] Atualização por classe:140806
[Lr] Data última revisão:
140806
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140226
[St] Status:MEDLINE
[do] DOI:10.1007/s13149-014-0336-y


  9 / 473 MEDLINE  
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[PMID]:24299903
[Au] Autor:Fournié G; Jones BA; Beauvais W; Lubroth J; Njeumi F; Cameron A; Pfeiffer DU
[Ad] Endereço:Veterinary Epidemiology, Economics and Public Health Group, Department of Production and Population Health, Royal Veterinary College, Hawkshead Lane, North Mymms, AL9 7TA Hatfield, United Kingdom. Electronic address: gfournie@rvc.ac.uk.
[Ti] Título:The risk of rinderpest re-introduction in post-eradication era.
[So] Source:Prev Vet Med;113(2):175-84, 2014 Feb 01.
[Is] ISSN:1873-1716
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:In 2011, ten years after the last reported outbreak, the eradication of rinderpest was declared. However, as rinderpest virus stocks still exist, there remains a risk of rinderpest re-introduction. A semi-quantitative risk assessment was conducted to assess this risk, which was defined as the probability of at least one host becoming infected and infectious outside a laboratory anywhere in the world within a one-year period. Pathways leading to rinderpest re-introduction were: deliberate or accidental use of virus in laboratories, deliberate or accidental use of vaccines, host exposure to an environmental source of virus, and use of virus for anti-animal biological warfare. The probability of each pathway step occurring was estimated through expert opinion elicitation. The risk estimate was associated with a high degree of uncertainty. It was estimated to range from negligible to high, with the median being very low. The accidental use of laboratory virus stocks was the highest risk pathway. Reducing the number of virus stocks and restricting their use, as well as upgrading the laboratories to a higher biosafety level, would effectively decrease the maximum and median risks. Likewise, ensuring that remaining vaccine stocks are not used and are instead destroyed or relocated to a limited number of regional repositories would also have a major effect on these estimates. However, these measures are unlikely to eliminate the risk of rinderpest re-introduction so that maintaining response preparedness is essential.
[Mh] Termos MeSH primário: Doenças dos Bovinos/virologia
Surtos de Doenças/veterinária
Vírus da Peste Bovina/crescimento & desenvolvimento
Peste Bovina/virologia
[Mh] Termos MeSH secundário: Animais
Bovinos
Doenças dos Bovinos/prevenção & controle
Surtos de Doenças/prevenção & controle
Modelos Teóricos
Peste Bovina/prevenção & controle
Medição de Risco/métodos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Em] Mês de entrada:1408
[Cu] Atualização por classe:131231
[Lr] Data última revisão:
131231
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131205
[St] Status:MEDLINE


  10 / 473 MEDLINE  
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[PMID]:24158397
[Au] Autor:Chinnakannan SK; Holzer B; Bernardo BS; Nanda SK; Baron MD
[Ad] Endereço:The Pirbright Institute, Ash Road, Pirbright, Surrey GU24 0NF, UK.
[Ti] Título:Different functions of the common P/V/W and V-specific domains of rinderpest virus V protein in blocking IFN signalling.
[So] Source:J Gen Virol;95(Pt 1):44-51, 2014 Jan.
[Is] ISSN:1465-2099
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The V proteins of paramyxoviruses are composed of two evolutionarily distinct domains, the N-terminal 75 % being common to the viral P, V and W proteins, and not highly conserved between viruses, whilst the remaining 25 % consists of a cysteine-rich V-specific domain, which is conserved across almost all paramyxoviruses. There is evidence supporting a number of different functions of the V proteins of morbilliviruses in blocking the signalling pathways of type I and II IFNs, but it is not clear which domains of V are responsible for which activities and whether all these activities are required for effective blockade of IFN signalling. We have shown here that the two domains of rinderpest virus V protein have distinct functions: the N-terminal domain acted to bind STAT1, whilst the C-terminal V-specific domain interacted with the IFN receptor-associated kinases Jak1 and Tyk2. Effective blockade of IFN signalling required the intact V protein.
[Mh] Termos MeSH primário: Interferons/metabolismo
Vírus da Peste Bovina/metabolismo
Peste Bovina/metabolismo
Transdução de Sinais
Proteínas Virais/química
Proteínas Virais/metabolismo
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Seres Humanos
Interferons/genética
Janus Quinase 1/genética
Janus Quinase 1/metabolismo
Fosforilação
Estrutura Terciária de Proteína
Peste Bovina/enzimologia
Peste Bovina/genética
Peste Bovina/virologia
Vírus da Peste Bovina/química
Vírus da Peste Bovina/genética
Fator de Transcrição STAT1/genética
Fator de Transcrição STAT1/metabolismo
Proteínas Virais/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (STAT1 Transcription Factor); 0 (STAT1 protein, human); 0 (V protein, Paramyxovirus); 0 (Viral Proteins); 9008-11-1 (Interferons); EC 2.7.10.2 (Janus Kinase 1)
[Em] Mês de entrada:1403
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131026
[St] Status:MEDLINE
[do] DOI:10.1099/vir.0.056739-0



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