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[PMID]:27735965
[Au] Autor:Marschang RE; Kolesnik E
[Ad] Endereço:Rachel E. Marschang, Laboklin GmbH & Co. KG, Steubenstraße 4, 97688 Bad Kissingen, E-Mail: rachel.marschang@googlemail.com.
[Ti] Título:Detection of nidoviruses in live pythons and boas.
[Ti] Título:Nachweis von Nidoviren bei lebenden Pythons und Boas..
[So] Source:Tierarztl Prax Ausg K Kleintiere Heimtiere;45(1):22-26, 2017 Feb 09.
[Is] ISSN:1434-1239
[Cp] País de publicação:Germany
[La] Idioma:eng; ger
[Ab] Resumo:OBJECTIVES: Nidoviruses have recently been described as a putative cause of severe respiratory disease in pythons in the USA and Europe. The objective of this study was to establish the use of a conventional PCR for the detection of nidoviruses in samples from live animals and to extend the list of susceptible species. MATERIALS AND METHODS: A PCR targeting a portion of ORF1a of python nidoviruses was used to detect nidoviruses in diagnostic samples from live boas and pythons. A total of 95 pythons, 84 boas and 22 snakes of unknown species were included in the study. Samples tested included oral swabs and whole blood. RESULTS: Nidoviruses were detected in 27.4% of the pythons and 2.4% of the boas tested. They were most commonly detected in ball pythons (Python [P.] regius) and Indian rock pythons (P. molurus), but were also detected for the first time in other python species, including Morelia spp. and Boa constrictor. Oral swabs were most commonly tested positive. CONCLUSION: The PCR described here can be used for the detection of nidoviruses in oral swabs from live snakes. These viruses appear to be relatively common among snakes in captivity in Europe and screening for these viruses should be considered in the clinical work-up. CLINICAL RELEVANCE: Nidoviruses are believed to be an important cause of respiratory disease in pythons, but can also infect boas. Detection of these viruses in live animals is now possible and can be of interest both in diseased animals as well as in quarantine situations.
[Mh] Termos MeSH primário: Boidae/virologia
Infecções por Nidovirales/veterinária
Nidovirales/isolamento & purificação
Infecções Respiratórias/veterinária
[Mh] Termos MeSH secundário: Animais
Boca/virologia
Nidovirales/genética
Infecções por Nidovirales/diagnóstico
Infecções por Nidovirales/virologia
Filogenia
Reação em Cadeia da Polimerase/veterinária
RNA Viral/isolamento & purificação
Infecções Respiratórias/diagnóstico
Infecções Respiratórias/virologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Viral)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170809
[Lr] Data última revisão:
170809
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161014
[St] Status:MEDLINE
[do] DOI:10.15654/TPK-151067


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[PMID]:27828982
[Au] Autor:O'Dea MA; Jackson B; Jackson C; Xavier P; Warren K
[Ad] Endereço:School of Veterinary and Life Sciences, Murdoch University, Murdoch, WA, Australia.
[Ti] Título:Discovery and Partial Genomic Characterisation of a Novel Nidovirus Associated with Respiratory Disease in Wild Shingleback Lizards (Tiliqua rugosa).
[So] Source:PLoS One;11(11):e0165209, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A respiratory disease syndrome has been observed in large numbers of wild shingleback lizards (Tiliqua rugosa) admitted to wildlife care facilities in the Perth metropolitan region of Western Australia. Mortality rates are reportedly high without supportive treatment and care. Here we used next generation sequencing techniques to screen affected and unaffected individuals admitted to Kanyana Wildlife Rehabilitation Centre in Perth between April and December 2015, with the resultant discovery of a novel nidovirus significantly associated with cases of respiratory disease according to a case definition based on clinical signs. Interestingly this virus was also found in 12% of apparently healthy individuals, which may reflect testing during the incubation period or a carrier status, or it may be that this agent is not causative in the disease process. This is the first report of a nidovirus in lizards globally. In addition to detection of this virus, characterisation of a 23,832 nt segment of the viral genome revealed the presence of characteristic nidoviral genomic elements providing phylogenetic support for the inclusion of this virus in a novel genus alongside Ball Python nidovirus, within the Torovirinae sub-family of the Coronaviridae. This study highlights the importance of next generation sequencing technologies to detect and describe emerging infectious diseases in wildlife species, as well as the importance of rehabilitation centres to enhance early detection mechanisms through passive and targeted health surveillance. Further development of diagnostic tools from these findings will aid in detection and control of this agent across Australia, and potentially in wild lizard populations globally.
[Mh] Termos MeSH primário: Lagartos/virologia
Infecções por Nidovirales/virologia
Nidovirales/fisiologia
Doenças Respiratórias/virologia
[Mh] Termos MeSH secundário: Animais
Animais Selvagens/virologia
Genoma Viral/genética
Genômica/métodos
Sequenciamento de Nucleotídeos em Larga Escala/métodos
Interações Hospedeiro-Patógeno
Nidovirales/classificação
Nidovirales/genética
Infecções por Nidovirales/diagnóstico
Filogenia
RNA Viral/genética
Doenças Respiratórias/diagnóstico
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Austrália Ocidental
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Viral)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170707
[Lr] Data última revisão:
170707
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161110
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0165209


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[PMID]:27230033
[Au] Autor:Faisal M; Baird A; Winters AD; Millard EV; Marcquenski S; Hsu HM; Hennings A; Bochsler P; Standish I; Loch TP; Gunn MR; Warg J
[Ad] Endereço:a Department of Fisheries and Wildlife, College of Agriculture and Natural Resources , Michigan State University , 1129 Farm Lane, Room 174, East Lansing, Michigan 48824 , USA.
[Ti] Título:Isolation of the Fathead Minnow Nidovirus from Muskellunge Experiencing Lingering Mortality.
[So] Source:J Aquat Anim Health;28(2):131-41, 2016 06.
[Is] ISSN:1548-8667
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In 2011, the Fathead Minnow nidovirus (FHMNV; Genus Bafinivirus, Family Coronaviridae, Order Nidovirales) was isolated from pond-raised juvenile Muskellunge Esox masquinongy suffering from lingering mortality at the Wild Rose Hatchery in Wild Rose, Wisconsin. Moribund Muskellunge exhibited tubular necrosis in the kidneys as well as multifocal coalescing necrotizing hepatitis. The FHMNV was also isolated from apparently healthy juvenile Muskellunge at the Wolf Lake State Fish Hatchery in Mattawan, Michigan. The identity of the two syncytia-forming viruses (designated MUS-WR and MUS-WL from Wild Rose Hatchery and Wolf Lake State Fish Hatchery, respectively) as strains of FHMNV was determined based on multiple-gene sequencing and phylogenetic analyses. The pathogenicity of the MUS-WL FHMNV strain was determined by experimentally infecting naive juvenile Muskellunge through intraperitoneal injection with two viral concentrations (63 and 6.3 × 10(3) TCID50/fish). Both doses resulted in 100% mortality in experimentally infected fish, which exhibited severely pale gills and petechial hemorrhaging in eyes, fins, and skin. Histopathological alterations in experimentally infected fish were observed mainly in the hematopoietic tissues in the form of focal areas of necrosis. Phylogenetic analysis of concatenated partial spike glycoprotein and helicase gene sequences revealed differences between the MUS-WL FHMNV, MUS-WR FHMNV, and two other FHMNV originally isolated from moribund Fathead Minnows Pimephales promelas including the index FHMNV strain (GU002364). Based on a partial helicase gene sequence, a reverse transcriptase PCR assay was developed that is specific to FHMNV. These results give evidence that the risks posed to Muskellunge by FHMNV should be taken seriously. Received May 1, 2015; accepted February 8, 2016.
[Mh] Termos MeSH primário: Aquicultura
Esocidae
Doenças dos Peixes/virologia
Infecções por Nidovirales/veterinária
Nidovirales/isolamento & purificação
[Mh] Termos MeSH secundário: Animais
Doenças dos Peixes/mortalidade
Nidovirales/classificação
Nidovirales/genética
Infecções por Nidovirales/virologia
Filogenia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170210
[Lr] Data última revisão:
170210
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160528
[St] Status:MEDLINE
[do] DOI:10.1080/08997659.2016.1159620


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[PMID]:27170751
[Au] Autor:Zeng C; Wu A; Wang Y; Xu S; Tang Y; Jin X; Wang S; Qin L; Sun Y; Fan C; Snijder EJ; Neuman BW; Chen Y; Ahola T; Guo D
[Ad] Endereço:State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, People's Republic of China.
[Ti] Título:Identification and Characterization of a Ribose 2'-O-Methyltransferase Encoded by the Ronivirus Branch of Nidovirales.
[So] Source:J Virol;90(15):6675-85, 2016 Aug 01.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:UNLABELLED: The order Nidovirales currently comprises four virus families: Arteriviridae, Coronaviridae (divided into the subfamilies Coronavirinae and Torovirinae), Roniviridae, and the recently recognized Mesoniviridae RNA cap formation and methylation have been best studied for coronaviruses, with emphasis on the identification and characterization of two virus-encoded methyltransferases (MTases) involved in RNA capping, a guanine-N7-MTase and a ribose-2'-O-MTase. Although bioinformatics analyses suggest that these MTases may also be encoded by other nidoviruses with large genomes, such as toroviruses and roniviruses, no experimental evidence has been reported thus far. In this study, we show that a ronivirus, gill-associated virus (GAV), encodes the 2'-O-MTase activity, although we could not detect 2'-O-MTase activity for the homologous protein of a torovirus, equine torovirus, which is more closely related to coronaviruses. Like the coronavirus 2'-O-MTase, the roniviral 2'-O-MTase harbors a catalytic K-D-K-E tetrad that is conserved among 2'-O-MTases and can target only the N7-methylated cap structure of adenylate-primed RNA substrates. However, in contrast with the coronavirus protein, roniviral 2'-O-MTase does not require a protein cofactor for stimulation of its activity and differs in its preference for several biochemical parameters, such as reaction temperature and pH. Furthermore, the ronivirus 2'-O-MTase can be targeted by MTase inhibitors. These results extend our current understanding of nidovirus RNA cap formation and methylation beyond the coronavirus family. IMPORTANCE: Methylation of the 5'-cap structure of viral RNAs plays important roles in genome replication and evasion of innate recognition of viral RNAs by cellular sensors. It is known that coronavirus nsp14 acts as an N7-(guanine)-methyltransferase (MTase) and nsp16 as a 2'-O-MTase, which are involved in the modification of RNA cap structure. However, these enzymatic activities have not been shown for any other nidoviruses beyond coronaviruses in the order Nidovirales In this study, we identified a 2'-O-methyltransferase encoded by ronivirus that shows common and unique features in comparison with that of coronaviruses. Ronivirus 2'-O-MTase does not need a protein cofactor for MTase activity, whereas coronavirus nsp16 needs the stimulating factor nsp10 for its full activity. The conserved K-D-K-E catalytic tetrad is identified in ronivirus 2'-O-MTase. These results extend our understanding of nidovirus RNA capping and methylation beyond coronaviruses and also strengthen the evolutionary and functional links between roniviruses and coronaviruses.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Metiltransferases/metabolismo
Nidovirales/enzimologia
Ribose/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Bactérias/genética
Metilação
Metiltransferases/genética
Nidovirales/genética
Infecções por Nidovirales/genética
Infecções por Nidovirales/metabolismo
Infecções por Nidovirales/virologia
Estrutura Terciária de Proteína
Capuzes de RNA/genética
RNA Viral/genética
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (RNA Caps); 0 (RNA, Viral); 681HV46001 (Ribose); EC 2.1.1.- (Methyltransferases); EC 2.1.1.- (RNA 2'-O-methyltransferase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170602
[Lr] Data última revisão:
170602
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160513
[St] Status:MEDLINE
[do] DOI:10.1128/JVI.00658-16


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[PMID]:27068501
[Au] Autor:Baird A; Faisal M
[Ad] Endereço:Department of Fisheries and Wildlife, College of Agriculture and Natural Resources, Michigan State University, East Lansing, MI 48824, USA.
[Ti] Título:Fathead minnow nidovirus infects spotfin shiner Cyprinella spiloptera and golden shiner Notemigonus crysoleucas.
[So] Source:Dis Aquat Organ;119(1):37-44, 2016 Apr 12.
[Is] ISSN:0177-5103
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Since the initial isolation of the fathead minnow nidovirus (FHMNV), concerns have been raised regarding the risks it may pose to other fish species. In this study, 7 fish species resident to the Laurentian Great Lakes were challenged intraperitoneally with 2 doses of FHMNV: 102.8 and 104.8 median tissue culture infective dose (TCID(50)) ml(-1). Infected spotfin shiner Cyprinella spiloptera and golden shiner Notemigonus crysoleucas suffered morbidity and mortality during the 40 d observation period, while other species, including creek chub Semotilus atromaculatus, rainbow trout Oncorhynchus mykiss, largemouth bass Micropterus salmoides and walleye Sander vitreus, showed no clinical signs or mortality. FHMNV was re-isolated on the epithelioma papulosum cyprini cell line from the tissues of infected spotfin shiner and golden shiner, which harbored high numbers of viral RNA copies as measured by quantitative loop-mediated isothermal amplification. Infected spotfin shiner and golden shiner exhibited external petechiae, exophthalmia, oedematous kidneys, and liver pallor. Histopathological analysis revealed multifocal areas of necrosis in the kidney, spleen and liver of infected fish. Spotfin shiner and golden shiner were then infected with 2 doses of FHMNV (10(3.5) and 10(3.9) TCID(50) ml(-1)) by immersion to mimic more natural modes of infection. Spotfin shiner experienced 60% mortality at both doses, while golden shiner did not experience mortality nor develop any clinical signs following a 40 d observation period. Overall, piscivorous fish tested in this study do not seem to be at risk for infection, while cyprinids appear to vary in their susceptibility to the strain of FHMNV used in this study.
[Mh] Termos MeSH primário: Doenças dos Peixes/virologia
Infecções por Nidovirales/veterinária
Nidovirales/classificação
[Mh] Termos MeSH secundário: Animais
Doenças dos Peixes/patologia
Peixes
Infecções por Nidovirales/patologia
Infecções por Nidovirales/virologia
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Em] Mês de entrada:1608
[Cu] Atualização por classe:160412
[Lr] Data última revisão:
160412
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160413
[St] Status:MEDLINE
[do] DOI:10.3354/dao02970


  6 / 78 MEDLINE  
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[PMID]:26977900
[Au] Autor:Blanck S; Ziebuhr J
[Ad] Endereço:Institute of Medical Virology, Justus Liebig University, Giessen, Germany.
[Ti] Título:Proteolytic processing of mesonivirus replicase polyproteins by the viral 3C-like protease.
[So] Source:J Gen Virol;97(6):1439-45, 2016 Jun.
[Is] ISSN:1465-2099
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Mesoniviridae are a family of insect RNA viruses that diverged profoundly from other families of the Nidovirales. Mesonivirus replicative proteins are produced from large polyprotein (pp) precursors (pp1a and pp1ab) through proteolytic cleavage by the viral 3C-like protease (3CLpro) and, possibly, other proteases. Using recombinant forms of the Cavally virus 3CLpro and pp1a/pp1ab-derived substrates, we characterized 3CLpro cleavage sites in mesonivirus polyproteins. Our data lead us to suggest that 3CLpro cleaves the central and C-proximal regions of mesonivirus pp1a/pp1ab at 12 conserved sites. Compared to other nidovirus homologues, the mesonivirus 3CLpro features a distinct substrate specificity, with asparagine at P2 being a major specificity determinant. Furthermore, we provide evidence that expression of the ORF1b-encoded part of pp1ab involves a -1 ribosomal frameshift at a conserved GGAUUUU heptanucleotide sequence in the ORF1a/1b overlap region. Taken together, the study identifies critical steps in the expression and maturation of mesonivirus replicative proteins.
[Mh] Termos MeSH primário: Cisteína Endopeptidases/metabolismo
Nidovirales/enzimologia
Nidovirales/fisiologia
Poliproteínas/metabolismo
Processamento de Proteína Pós-Traducional
Proteínas Virais/metabolismo
[Mh] Termos MeSH secundário: Animais
Insetos
Proteólise
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Polyproteins); 0 (Viral Proteins); EC 3.4.22.- (Cysteine Endopeptidases); EC 3.4.22.28 (3C proteases)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160316
[St] Status:MEDLINE
[do] DOI:10.1099/jgv.0.000458


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[PMID]:26874014
[Au] Autor:Giles J; Perrott M; Roe W; Dunowska M
[Ad] Endereço:Institute of Veterinary, Animal and Biomedical Sciences, Massey University, Tennent drive, Palmerston North, New Zealand. Electronic address: J.C.Giles@Massey.ac.nz.
[Ti] Título:The aetiology of wobbly possum disease: Reproduction of the disease with purified nidovirus.
[So] Source:Virology;491:20-6, 2016 Apr.
[Is] ISSN:1096-0341
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The objective of this study was to investigate a role of a recently discovered marsupial nidovirus in the development of a neurological disease, termed wobbly possum disease (WPD), in the Australian brushtail possum (Trichosurus vulpecula). Four possums received 1 mL of a standard inoculum that had been prepared from tissues of WPD-affected possums, 4 possums received 1.8 mL (1 × 10(6) TCID50) of a cell lysate from inoculated cultures, and 4 possums received 1 mL (× 10(7) TCID50) of a purified WPD isolate. All but one possum that received infectious inocula developed neurological disease and histopathological lesions characteristic for WPD. High levels of viral RNA were detected in livers from all possums that received infectious inocula, but not from control possums. Altogether, our data provide strong experimental evidence for the causative involvement of WPD virus in development of a neurological disease in infected animals.
[Mh] Termos MeSH primário: Infecções por Nidovirales/veterinária
Nidovirales/fisiologia
Trichosurus/virologia
[Mh] Termos MeSH secundário: Animais
Austrália
Feminino
Fígado/patologia
Fígado/virologia
Masculino
Nidovirales/classificação
Nidovirales/genética
Nidovirales/isolamento & purificação
Infecções por Nidovirales/patologia
Infecções por Nidovirales/virologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Em] Mês de entrada:1608
[Cu] Atualização por classe:160309
[Lr] Data última revisão:
160309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160214
[St] Status:MEDLINE


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[PMID]:26304538
[Au] Autor:Lehmann KC; Gulyaeva A; Zevenhoven-Dobbe JC; Janssen GM; Ruben M; Overkleeft HS; van Veelen PA; Samborskiy DV; Kravchenko AA; Leontovich AM; Sidorov IA; Snijder EJ; Posthuma CC; Gorbalenya AE
[Ad] Endereço:Department of Medical Microbiology, Leiden University Medical Center, Leiden, 2300 RC, Leiden, The Netherlands.
[Ti] Título:Discovery of an essential nucleotidylating activity associated with a newly delineated conserved domain in the RNA polymerase-containing protein of all nidoviruses.
[So] Source:Nucleic Acids Res;43(17):8416-34, 2015 Sep 30.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:RNA viruses encode an RNA-dependent RNA polymerase (RdRp) that catalyzes the synthesis of their RNA(s). In the case of positive-stranded RNA viruses belonging to the order Nidovirales, the RdRp resides in a replicase subunit that is unusually large. Bioinformatics analysis of this non-structural protein has now revealed a nidoviral signature domain (genetic marker) that is N-terminally adjacent to the RdRp and has no apparent homologs elsewhere. Based on its conservation profile, this domain is proposed to have nucleotidylation activity. We used recombinant non-structural protein 9 of the arterivirus equine arteritis virus (EAV) and different biochemical assays, including irreversible labeling with a GTP analog followed by a proteomics analysis, to demonstrate the manganese-dependent covalent binding of guanosine and uridine phosphates to a lysine/histidine residue. Most likely this was the invariant lysine of the newly identified domain, named nidovirus RdRp-associated nucleotidyltransferase (NiRAN), whose substitution with alanine severely diminished the described binding. Furthermore, this mutation crippled EAV and prevented the replication of severe acute respiratory syndrome coronavirus (SARS-CoV) in cell culture, indicating that NiRAN is essential for nidoviruses. Potential functions supported by NiRAN may include nucleic acid ligation, mRNA capping and protein-primed RNA synthesis, possibilities that remain to be explored in future studies.
[Mh] Termos MeSH primário: Nidovirales/enzimologia
Nucleotidiltransferases/química
RNA Replicase/química
Proteínas Virais/química
[Mh] Termos MeSH secundário: Vírus da Arterite Equina/enzimologia
Vírus da Arterite Equina/fisiologia
Sítios de Ligação
Sequência Conservada
Guanosina/química
Guanosina Trifosfato/metabolismo
Manganês/química
Nidovirales/genética
Nucleotídeos/metabolismo
Nucleotidiltransferases/metabolismo
Fosfatos/química
Poliproteínas/química
Poliproteínas/metabolismo
Estrutura Terciária de Proteína
RNA Replicase/genética
RNA Replicase/metabolismo
Vírus da SARS/enzimologia
Vírus da SARS/fisiologia
Uridina/química
Uridina Trifosfato/metabolismo
Proteínas Virais/genética
Proteínas Virais/metabolismo
Replicação Viral
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Nucleotides); 0 (Phosphates); 0 (Polyproteins); 0 (Viral Proteins); 12133JR80S (Guanosine); 42Z2K6ZL8P (Manganese); 86-01-1 (Guanosine Triphosphate); EC 2.7.7.- (Nucleotidyltransferases); EC 2.7.7.48 (RNA Replicase); UT0S826Z60 (Uridine Triphosphate); WHI7HQ7H85 (Uridine)
[Em] Mês de entrada:1601
[Cu] Atualização por classe:160316
[Lr] Data última revisão:
160316
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150826
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkv838


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[PMID]:26095364
[Au] Autor:Langereis MA; Bakkers MJ; Deng L; Padler-Karavani V; Vervoort SJ; Hulswit RJ; van Vliet AL; Gerwig GJ; de Poot SA; Boot W; van Ederen AM; Heesters BA; van der Loos CM; van Kuppeveld FJ; Yu H; Huizinga EG; Chen X; Varki A; Kamerling JP; de Groot RJ
[Ad] Endereço:Virology Division, Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, 3584 CL Utrecht, the Netherlands.
[Ti] Título:Complexity and Diversity of the Mammalian Sialome Revealed by Nidovirus Virolectins.
[So] Source:Cell Rep;11(12):1966-78, 2015 Jun 30.
[Is] ISSN:2211-1247
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sialic acids (Sias), 9-carbon-backbone sugars, are among the most complex and versatile molecules of life. As terminal residues of glycans on proteins and lipids, Sias are key elements of glycotopes of both cellular and microbial lectins and thus act as important molecular tags in cell recognition and signaling events. Their functions in such interactions can be regulated by post-synthetic modifications, the most common of which is differential Sia-O-acetylation (O-Ac-Sias). The biology of O-Ac-Sias remains mostly unexplored, largely because of limitations associated with their specific in situ detection. Here, we show that dual-function hemagglutinin-esterase envelope proteins of nidoviruses distinguish between a variety of closely related O-Ac-Sias. By using soluble forms of hemagglutinin-esterases as lectins and sialate-O-acetylesterases, we demonstrate differential expression of distinct O-Ac-sialoglycan populations in an organ-, tissue- and cell-specific fashion. Our findings indicate that programmed Sia-O-acetylation/de-O-acetylation may be critical to key aspects of cell development, homeostasis, and/or function.
[Mh] Termos MeSH primário: Acetilesterase/biossíntese
Hemaglutininas Virais/genética
Ácido N-Acetilneuramínico/genética
Ácidos Siálicos/genética
Proteínas Virais de Fusão/genética
[Mh] Termos MeSH secundário: Acetilação
Acetilesterase/genética
Animais
Regulação da Expressão Gênica
Genoma
Hemaglutininas Virais/química
Hemaglutininas Virais/metabolismo
Seres Humanos
Lipídeos/química
Lipídeos/genética
Mamíferos
Ácido N-Acetilneuramínico/química
Ácido N-Acetilneuramínico/metabolismo
Nidovirales/química
Proteínas/química
Proteínas/genética
Ácidos Siálicos/química
Especificidade da Espécie
Proteínas Virais de Fusão/química
Proteínas Virais de Fusão/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Hemagglutinins, Viral); 0 (Lipids); 0 (Proteins); 0 (Sialic Acids); 0 (Viral Fusion Proteins); 0 (hemagglutinin esterase); EC 3.1.1.6 (Acetylesterase); EC 3.1.1.6 (sialate O-acetylesterase); GZP2782OP0 (N-Acetylneuraminic Acid)
[Em] Mês de entrada:1603
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150623
[St] Status:MEDLINE


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[PMID]:26028426
[Au] Autor:Giles JC; Perrott MR; Dunowska M
[Ad] Endereço:Institute of Veterinary, Animal and Biomedical Sciences, Massey University, Palmerston North, New Zealand. Electronic address: J.C.Giles@Massey.ac.nz.
[Ti] Título:Primary possum macrophage cultures support the growth of a nidovirus associated with wobbly possum disease.
[So] Source:J Virol Methods;222:66-71, 2015 Sep 15.
[Is] ISSN:1879-0984
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The objective of the study was to establish a system for isolation of a recently described, thus far uncultured, marsupial nidovirus associated with a neurological disease of possums, termed wobbly possum disease (WPD). Primary cultures of possum macrophages were established from livers of adult Australian brushtail possums (Trichosurus vulpecula). High viral copy numbers (up to 6.9×10(8)/mL of cell lysate) were detected in infected cell culture lysates from up to the 5th passage of the virus, indicating that the putative WPD virus (WPDV) was replicating in cultured cells. A purified virus stock with a density of 1.09 g/mL was prepared using iodixanol density gradient ultracentrifugation. Virus-like particles approximately 60 nm in diameter were observed using electron microscopy in negatively stained preparations of the purified virus. The one-step growth curve of WPDV in macrophage cultures showed the highest increase in intracellular viral RNA between 6 and 12h post-infection. Maximum levels of cell-associated viral RNA were detected at 24h post-infection, followed by a decline. Levels of extracellular RNA increased starting at 9h post-infection, with maximum levels detected at 48 h post-infection. The establishment of the in vitro system to culture WPDV will facilitate further characterisation of this novel nidovirus.
[Mh] Termos MeSH primário: Macrófagos/virologia
Infecções por Nidovirales/veterinária
Nidovirales/crescimento & desenvolvimento
Nidovirales/isolamento & purificação
Trichosurus/virologia
Cultura de Vírus/métodos
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Centrifugação com Gradiente de Concentração
Microscopia Eletrônica de Transmissão
Nidovirales/ultraestrutura
Infecções por Nidovirales/virologia
Vírion/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Em] Mês de entrada:1604
[Cu] Atualização por classe:150807
[Lr] Data última revisão:
150807
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150602
[St] Status:MEDLINE



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