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Pesquisa : D12.776.964.970.600 [Categoria DeCS]
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  1 / 2009 MEDLINE  
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[PMID]:28457899
[Au] Autor:Yu J; Liu Y; Zhang Y; Zhu X; Ren S; Guo L; Liu X; Sun W; Chen Z; Cong X; Chen L; Shi J; Du Y; Li J; Wu J; Wang J
[Ad] Endereço:Shandong Academy of Agricultural Sciences, Jinan 250100, China; Shandong Key Lab of Animal Disease Control and Breeding, Jinan 250022, China.
[Ti] Título:The integrity of PRRSV nucleocapsid protein is necessary for up-regulation of optimal interleukin-10 through NF-κB and p38 MAPK pathways in porcine alveolar macrophages.
[So] Source:Microb Pathog;109:319-324, 2017 Aug.
[Is] ISSN:1096-1208
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Porcine reproductive and respiratory syndrome (PRRS), a highly contagious disease, has been constantly causing huge economic losses all over the world. PRRS virus (PRRSV) infection results in immunosuppression and IL-10 up-regulation. The relationship between them is still in dispute. Previous studies demonstrated the protein of PRRSV nucleocapsid (N) protein is able to up-regulate IL-10, yet the underlying molecular mechanisms remain unknown. In this study, the expression kinetics of IL-10 up-regulation induced by PRRSV N protein were analyzed in immortalized porcine alveolar macrophages (PAMs). N protein induced IL-10 expression in a time- and dose-dependent manner. Inhibition experiments of signaling pathways suggested NF-κB and p38 MAPK pathways are both involved in N protein-induced IL-10 up-regulation. Besides, the integrity of N protein is essential for significant IL-10 up-regulation. This research is beneficial for further understanding of the interplay between PRRSV and host immune system.
[Mh] Termos MeSH primário: Interleucina-10/metabolismo
Macrófagos Alveolares/imunologia
NF-kappa B/metabolismo
Proteínas do Nucleocapsídeo/metabolismo
Vírus da Síndrome Respiratória e Reprodutiva Suína/metabolismo
Suínos/imunologia
Regulação para Cima
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Regulação da Expressão Gênica
Imunossupressão
Macrófagos Alveolares/virologia
Proteínas do Nucleocapsídeo/genética
Síndrome Respiratória e Reprodutiva Suína/imunologia
Síndrome Respiratória e Reprodutiva Suína/virologia
Vírus da Síndrome Respiratória e Reprodutiva Suína/genética
Vírus da Síndrome Respiratória e Reprodutiva Suína/imunologia
Transdução de Sinais
Suínos/virologia
Proteínas Virais/genética
Proteínas Virais/metabolismo
Proteínas Quinases p38 Ativadas por Mitógeno/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (NF-kappa B); 0 (Nucleocapsid Proteins); 0 (Viral Proteins); 130068-27-8 (Interleukin-10); EC 2.7.11.24 (p38 Mitogen-Activated Protein Kinases)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180302
[Lr] Data última revisão:
180302
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170502
[St] Status:MEDLINE


  2 / 2009 MEDLINE  
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[PMID]:29324338
[Au] Autor:Gamba E; Mori M; Kovalenko L; Giannini A; Sosic A; Saladini F; Fabris D; Mély Y; Gatto B; Botta M
[Ad] Endereço:Dipartimento di Scienze del Farmaco, Università di Padova, via Marzolo 5, 35131 Padova, Italy.
[Ti] Título:Identification of novel 2-benzoxazolinone derivatives with specific inhibitory activity against the HIV-1 nucleocapsid protein.
[So] Source:Eur J Med Chem;145:154-164, 2018 Feb 10.
[Is] ISSN:1768-3254
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:In this report, we present a new benzoxazole derivative endowed with inhibitory activity against the HIV-1 nucleocapsid protein (NC). NC is a 55-residue basic protein with nucleic acid chaperone properties, which has emerged as a novel and potential pharmacological target against HIV-1. In the pursuit of novel NC-inhibitor chemotypes, we performed virtual screening and in vitro biological evaluation of a large library of chemical entities. We found that compounds sharing a benzoxazolinone moiety displayed putative inhibitory properties, which we further investigated by considering a series of chemical analogues. This approach provided valuable information on the structure-activity relationships of these compounds and, in the process, demonstrated that their anti-NC activity could be finely tuned by the addition of specific substituents to the initial benzoxazolinone scaffold. This study represents the starting point for the possible development of a new class of antiretroviral agents targeting the HIV-1 NC protein.
[Mh] Termos MeSH primário: Fármacos Anti-HIV/farmacologia
Benzoxazóis/farmacologia
HIV/efeitos dos fármacos
Proteínas do Nucleocapsídeo/antagonistas & inibidores
[Mh] Termos MeSH secundário: Fármacos Anti-HIV/síntese química
Fármacos Anti-HIV/química
Benzoxazóis/síntese química
Benzoxazóis/química
Relação Dose-Resposta a Droga
Testes de Sensibilidade Microbiana
Estrutura Molecular
Proteínas do Nucleocapsídeo/metabolismo
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-HIV Agents); 0 (Benzoxazoles); 0 (Nucleocapsid Proteins); 3X996Q809V (benzoxazolone)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180227
[Lr] Data última revisão:
180227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180112
[St] Status:MEDLINE


  3 / 2009 MEDLINE  
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[PMID]:29267287
[Au] Autor:Mottram TJ; Li P; Dietrich I; Shi X; Brennan B; Varjak M; Kohl A
[Ad] Endereço:MRC-University of Glasgow Centre for Virus Research, Glasgow, Scotland, United Kingdom.
[Ti] Título:Mutational analysis of Rift Valley fever phlebovirus nucleocapsid protein indicates novel conserved, functional amino acids.
[So] Source:PLoS Negl Trop Dis;11(12):e0006155, 2017 12.
[Is] ISSN:1935-2735
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Rift Valley fever phlebovirus (RVFV; Phenuiviridae, Phlebovirus) is an important mosquito-borne pathogen of both humans and ruminants. The RVFV genome is composed of tripartite, single stranded, negative or ambisense RNAs. The small (S) segment encodes both the nucleocapsid protein (N) and the non-structural protein (NSs). The N protein is responsible for the formation of the viral ribonucleoprotein (RNP) complexes, which are essential in the virus life cycle and for the transcription and replication of the viral genome. There is currently limited knowledge surrounding the roles of the RVFV nucleocapsid protein in viral infection other than its key functions: N protein multimerisation, encapsidation of the RNA genome and interactions with the RNA-dependent RNA polymerase, L. By bioinformatic comparison of the N sequences of fourteen phleboviruses, mutational analysis, minigenome assays and packaging assays, we have further characterised the RVFV N protein. Amino acids P11 and F149 in RVFV N play an essential role in the function of RNPs and are neither associated with N protein multimerisation nor known nucleocapsid protein functions and may have additional roles in the virus life cycle. Amino acid Y30 exhibited increased minigenome activity despite reduced RNA binding capacity. Additionally, we have determined that the N-terminal arm of N protein is not involved in N-L interactions. Elucidating the fundamental processes that involve the nucleocapsid protein will add to our understanding of this important viral protein and may influence future studies in the development of novel antiviral strategies.
[Mh] Termos MeSH primário: Análise Mutacional de DNA
Genoma Viral/genética
Proteínas do Nucleocapsídeo/genética
RNA Viral/genética
Vírus da Febre do Vale do Rift/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Linhagem Celular
Cricetinae
Multimerização Proteica/genética
Multimerização Proteica/fisiologia
Proteínas de Ligação a RNA/genética
Febre do Vale de Rift/virologia
Alinhamento de Sequência
Replicação Viral
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Nucleocapsid Proteins); 0 (RNA, Viral); 0 (RNA-Binding Proteins)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180130
[Lr] Data última revisão:
180130
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171222
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pntd.0006155


  4 / 2009 MEDLINE  
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[PMID]:29236778
[Au] Autor:Wang C; Zeng N; Liu S; Miao Q; Zhou L; Ge X; Han J; Guo X; Yang H
[Ad] Endereço:Key Laboratory of Animal Epidemiology of the Ministry of Agriculture, College of Veterinary Medicine and State Key Laboratory of Agrobiotechnology, China Agricultural University, Beijing, People's Republic of China.
[Ti] Título:Interaction of porcine reproductive and respiratory syndrome virus proteins with SUMO-conjugating enzyme reveals the SUMOylation of nucleocapsid protein.
[So] Source:PLoS One;12(12):e0189191, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:SUMOylation is a reversible post-translational modification that regulates the function of target protein. In this study, we first predicted by software that the multiple proteins of porcine reproductive and respiratory syndrome virus (PRRSV) could be sumoylated. Next, we confirmed that Nsp1ß, Nsp4, Nsp9, Nsp10 and nucleocapsid (N) protein of PRRSV could interact with the sole SUMO E2 conjugating enzyme Ubc9, and Ubc9 could be co-localized with Nsp1ß, Nsp4, Nsp9 and Nsp10 in the cytoplasm, while with N protein in both the cytoplasm and nucleus. Finally, we demonstrated that N protein could be sumoylated by either SUMO1 or SUMO2/3. In addition, the overexpression of Ubc9 could inhibit viral genomic replication at early period of PRRSV infection and the knockdown of Ubc9 by siRNA could promote the virus replication. These findings reveal the SUMOylation property of PRRSV N protein and the involvement of Ubc9 in PRRSV replication through interaction with multiple proteins of PRRSV. To our knowledge, this is the first study indicating the interplay between SUMO modification system and PRRSV.
[Mh] Termos MeSH primário: Proteínas do Nucleocapsídeo/metabolismo
Vírus da Síndrome Respiratória e Reprodutiva Suína/metabolismo
Sumoilação
[Mh] Termos MeSH secundário: Animais
Vírus da Síndrome Respiratória e Reprodutiva Suína/fisiologia
Suínos
Técnicas do Sistema de Duplo-Híbrido
Replicação Viral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nucleocapsid Proteins)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171214
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189191


  5 / 2009 MEDLINE  
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[PMID]:28922369
[Au] Autor:Jeeva S; Pador S; Voss B; Ganaie SS; Mir MA
[Ad] Endereço:Western University of Health Sciences, Pomona, California, United States of America.
[Ti] Título:Crimean-Congo hemorrhagic fever virus nucleocapsid protein has dual RNA binding modes.
[So] Source:PLoS One;12(9):e0184935, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Crimean Congo hemorrhagic fever, a zoonotic viral disease, has high mortality rate in humans. There is currently no vaccine for Crimean Congo hemorrhagic fever virus (CCHFV) and chemical interventions are limited. The three negative sense genomic RNA segments of CCHFV are specifically encapsidated by the nucleocapsid protein into three ribonucleocapsids, which serve as templates for the viral RNA dependent RNA polymerase. Here we demonstrate that CCHFV nucleocapsid protein has two distinct binding modes for double and single strand RNA. In the double strand RNA binding mode, the nucleocapsid protein preferentially binds to the vRNA panhandle formed by the base pairing of complementary nucleotides at the 5' and 3' termini of viral genome. The CCHFV nucleocapsid protein does not have RNA helix unwinding activity and hence does not melt the duplex vRNA panhandle after binding. In the single strand RNA binding mode, the nucleocapsid protein does not discriminate between viral and non-viral RNA molecules. Binding of both vRNA panhandle and single strand RNA induce a conformational change in the nucleocapsid protein. Nucleocapsid protein remains in a unique conformational state due to simultaneously binding of structurally distinct vRNA panhandle and single strand RNA substrates. Although the role of dual RNA binding modes in the virus replication cycle is unknown, their involvement in the packaging of viral genome and regulation of CCHFV replication in conjunction with RdRp and host derived RNA regulators is highly likely.
[Mh] Termos MeSH primário: Vírus da Febre Hemorrágica da Crimeia-Congo
Conformação de Ácido Nucleico
Proteínas do Nucleocapsídeo
RNA Viral
Proteínas de Ligação a RNA
[Mh] Termos MeSH secundário: Vírus da Febre Hemorrágica da Crimeia-Congo/química
Vírus da Febre Hemorrágica da Crimeia-Congo/genética
Vírus da Febre Hemorrágica da Crimeia-Congo/metabolismo
Proteínas do Nucleocapsídeo/química
Proteínas do Nucleocapsídeo/genética
Proteínas do Nucleocapsídeo/metabolismo
Ligação Proteica
RNA Viral/química
RNA Viral/genética
RNA Viral/metabolismo
Proteínas de Ligação a RNA/química
Proteínas de Ligação a RNA/genética
Proteínas de Ligação a RNA/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nucleocapsid Proteins); 0 (RNA, Viral); 0 (RNA-Binding Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171013
[Lr] Data última revisão:
171013
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170919
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184935


  6 / 2009 MEDLINE  
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[PMID]:28911104
[Au] Autor:Nußbaumer F; Juen MA; Gasser C; Kremser J; Müller T; Tollinger M; Kreutz C
[Ad] Endereço:Institute of Organic Chemistry, Leopold-Franzens-University of Innsbruck, and Center for Molecular Biosciences Innsbruck, Innrain 80/82, 6020 Innsbruck, Austria.
[Ti] Título:Synthesis and incorporation of 13C-labeled DNA building blocks to probe structural dynamics of DNA by NMR.
[So] Source:Nucleic Acids Res;45(15):9178-9192, 2017 Sep 06.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:We report the synthesis of atom-specifically 13C-modified building blocks that can be incorporated into DNA via solid phase synthesis to facilitate investigations on structural and dynamic features via NMR spectroscopy. In detail, 6-13C-modified pyrimidine and 8-13C purine DNA phosphoramidites were synthesized and incorporated into a polypurine tract DNA/RNA hybrid duplex to showcase the facile resonance assignment using site-specific labeling. We also addressed micro- to millisecond dynamics in the mini-cTAR DNA. This DNA is involved in the HIV replication cycle and our data points toward an exchange process in the lower stem of the hairpin that is up-regulated in the presence of the HIV-1 nucleocapsid protein 7. As another example, we picked a G-quadruplex that was earlier shown to exist in two folds. Using site-specific 8-13C-2'deoxyguanosine labeling we were able to verify the slow exchange between the two forms on the chemical shift time scale. In a real-time NMR experiment the re-equilibration of the fold distribution after a T-jump could be monitored yielding a rate of 0.012 min-1. Finally, we used 13C-ZZ-exchange spectroscopy to characterize the kinetics between two stacked X-conformers of a Holliday junction mimic. At 25°C, the refolding process was found to occur at a forward rate constant of 3.1 s-1 and with a backward rate constant of 10.6 s-1.
[Mh] Termos MeSH primário: DNA Cruciforme/química
DNA/química
Repetição Terminal Longa de HIV
Proteínas do Nucleocapsídeo/química
Compostos Organofosforados/química
RNA/química
[Mh] Termos MeSH secundário: Pareamento de Bases
Isótopos de Carbono
Quadruplex G
HIV-1/química
Marcação por Isótopo
Espectroscopia de Ressonância Magnética
Modelos Moleculares
Mimetismo Molecular
Conformação de Ácido Nucleico
Compostos Organofosforados/síntese química
Técnicas de Síntese em Fase Sólida
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carbon Isotopes); 0 (DNA, Cruciform); 0 (Nucleocapsid Proteins); 0 (Organophosphorus Compounds); 0 (phosphoramidite); 63231-63-0 (RNA); 9007-49-2 (DNA)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171012
[Lr] Data última revisão:
171012
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170916
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx592


  7 / 2009 MEDLINE  
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[PMID]:28777080
[Au] Autor:Baklouti A; Goulet A; Lichière J; Canard B; Charrel RN; Ferron F; Coutard B; Papageorgiou N
[Ad] Endereço:Architecture et Fonction des Macromolécules Biologiques, CNRS, Aix-Marseille Université, 13288 Marseille, France.
[Ti] Título:Toscana virus nucleoprotein oligomer organization observed in solution.
[So] Source:Acta Crystallogr D Struct Biol;73(Pt 8):650-659, 2017 Aug 01.
[Is] ISSN:2059-7983
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Toscana virus (TOSV) is an arthropod-borne virus belonging to the Phlebovirus genus within the Bunyaviridae family. As in other bunyaviruses, the genome of TOSV is made up of three RNA segments. They are encapsidated by the nucleoprotein (N), which also plays an essential role in virus replication. To date, crystallographic structures of phlebovirus N have systematically revealed closed-ring organizations which do not fully match the filamentous organization of the ribonucleoprotein (RNP) complex observed by electron microscopy. In order to further bridge the gap between crystallographic data on N and observations of the RNP by electron microscopy, the structural organization of recombinant TOSV N was investigated by an integrative approach combining X-ray diffraction crystallography, transmission electron microscopy, small-angle X-ray scattering, size-exclusion chromatography and multi-angle laser light scattering. It was found that in solution TOSV N forms open oligomers consistent with the encapsidation mechanism of phlebovirus RNA.
[Mh] Termos MeSH primário: Proteínas do Nucleocapsídeo/química
Nucleoproteínas/química
Vírus da Febre do Flebótomo Napolitano/química
[Mh] Termos MeSH secundário: Infecções por Bunyaviridae/virologia
Cristalografia por Raios X
Modelos Moleculares
Proteínas do Nucleocapsídeo/metabolismo
Proteínas do Nucleocapsídeo/ultraestrutura
Nucleoproteínas/metabolismo
Nucleoproteínas/ultraestrutura
Conformação Proteica
Multimerização Proteica
RNA Viral/metabolismo
Vírus da Febre do Flebótomo Napolitano/metabolismo
Espalhamento a Baixo Ângulo
Soluções
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nucleocapsid Proteins); 0 (Nucleoproteins); 0 (RNA, Viral); 0 (Solutions)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170805
[St] Status:MEDLINE
[do] DOI:10.1107/S2059798317008774


  8 / 2009 MEDLINE  
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[PMID]:28777079
[Au] Autor:Yekwa E; Khourieh J; Canard B; Papageorgiou N; Ferron F
[Ad] Endereço:CNRS, AFMB UMR 7257, 13288 Marseille, France.
[Ti] Título:Activity inhibition and crystal polymorphism induced by active-site metal swapping.
[So] Source:Acta Crystallogr D Struct Biol;73(Pt 8):641-649, 2017 Aug 01.
[Is] ISSN:2059-7983
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Arenaviridae family is one of the two RNA viral families that encode a 3'-5' exonuclease in their genome. An exonuclease domain is found in the Arenaviridae nucleoprotein and targets dsRNA specifically. This domain is directly involved in suppression of innate immunity in the host cell. Like most phosphate-processing enzymes, it requires a divalent metal ion such as Mg (or Mn ) as a cofactor to catalyse nucleotide-cleavage and nucleotide-transfer reactions. On the other hand, calcium (Ca ) inhibits this enzymatic activity, in spite of the fact that Mg and Ca present comparable binding affinities and biological availabilities. Here, the molecular and structural effects of the replacement of magnesium by calcium and its inhibition mechanism for phosphodiester cleavage, an essential reaction in the viral process of innate immunity suppression, are studied. Biochemical data and high-resolution structures of the Mopeia virus exonuclease domain complexed with each ion are reported for the first time. The consequences of the ion swap for the stability of the protein, the catalytic site and the functional role of a specific metal ion in enabling the catalytic cleavage of a dsRNA substrate are outlined.
[Mh] Termos MeSH primário: Arenavirus/química
Arenavirus/enzimologia
Exonucleases/química
Proteínas do Nucleocapsídeo/química
Nucleoproteínas/química
[Mh] Termos MeSH secundário: Infecções por Arenaviridae/virologia
Arenavirus/metabolismo
Sítios de Ligação
Cálcio/metabolismo
Domínio Catalítico
Cátions Bivalentes/metabolismo
Cristalização
Cristalografia por Raios X
Exonucleases/metabolismo
Magnésio/metabolismo
Manganês/metabolismo
Simulação de Acoplamento Molecular
Proteínas do Nucleocapsídeo/metabolismo
Nucleoproteínas/metabolismo
Domínios Proteicos
RNA Viral/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cations, Divalent); 0 (Nucleocapsid Proteins); 0 (Nucleoproteins); 0 (RNA, Viral); 42Z2K6ZL8P (Manganese); EC 3.1.- (Exonucleases); I38ZP9992A (Magnesium); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170805
[St] Status:MEDLINE
[do] DOI:10.1107/S205979831700866X


  9 / 2009 MEDLINE  
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[PMID]:28768868
[Au] Autor:Komoda K; Narita M; Yamashita K; Tanaka I; Yao M
[Ad] Endereço:Graduate School of Life Sciences, Hokkaido University, Sapporo, Hokkaido, Japan komoda.k@gmail.com yao@castor.sci.hokudai.ac.jp.
[Ti] Título:Asymmetric Trimeric Ring Structure of the Nucleocapsid Protein of Tospovirus.
[So] Source:J Virol;91(20), 2017 Oct 15.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:(TSWV), belonging to the genus of the family , causes significant economic damage to several vegetables and ornamental plants worldwide. Similar to those of all other negative-strand RNA viruses, the nucleocapsid (N) protein plays very important roles in its viral life cycle. N proteins protect genomic RNAs by encapsidation and form a viral ribonucleoprotein complex (vRNP) with some RNA-dependent RNA polymerases. Here we show the crystal structure of the N protein from TSWV. Protomers of TSWV N proteins consist of three parts: the N arm, C arm, and core domain. Unlike N proteins of other negative-strand RNA viruses, the TSWV N protein forms an asymmetric trimeric ring. To form the trimeric ring, the N and C arms of the N protein interact with the core domains of two adjacent N proteins. By solving the crystal structures of the TSWV N protein with nucleic acids, we showed that an inner cleft of the asymmetric trimeric ring is an RNA-binding site. These characteristics are similar to those of N proteins of other viruses of the family Based on these observations, we discuss possibilities of a TSWV encapsidation model. Tospoviruses cause significant crop losses throughout the world. Particularly, TSWV has an extremely wide host range (>1,000 plant species, including dicots and monocots), and worldwide losses are estimated to be in excess of $1 billion annually. Despite such importance, no proteins of tospoviruses have been elucidated so far. Among TSWV-encoded proteins, the N protein is required for assembling the viral genomic RNA into the viral ribonucleoprotein (vRNP), which is involved in various steps of the life cycle of these viruses, such as RNA replication, virus particle formation, and cell-to-cell movement. This study revealed the structure of the N protein, with or without nucleic acids, of TSWV as the first virus of the genus , so it completed our view of the N proteins of the family .
[Mh] Termos MeSH primário: Proteínas do Nucleocapsídeo/química
Tospovirus/química
[Mh] Termos MeSH secundário: Sítios de Ligação
Cristalografia por Raios X
Lycopersicon esculentum/virologia
Modelos Moleculares
Conformação Proteica
Multimerização Proteica
RNA Viral/química
Vírion
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nucleocapsid Proteins); 0 (RNA, Viral)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170804
[St] Status:MEDLINE


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[PMID]:28737119
[Au] Autor:Wise EL; Marston DA; Banyard AC; Goharriz H; Selden D; Maclaren N; Goddard T; Johnson N; McElhinney LM; Brouwer A; Aegerter JN; Smith GC; Horton DL; Breed AC; Fooks AR
[Ad] Endereço:Animal and Plant Health Agency (APHA, Weybridge),Surrey KT15 3NB,UK.
[Ti] Título:Passive surveillance of United Kingdom bats for lyssaviruses (2005-2015).
[So] Source:Epidemiol Infect;145(12):2445-2457, 2017 09.
[Is] ISSN:1469-4409
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Passive surveillance for lyssaviruses in UK bats has been ongoing since 1987 and has identified 13 cases of EBLV-2 from a single species; Myotis daubentonii. No other lyssavirus species has been detected. Between 2005 and 2015, 10 656 bats were submitted, representing 18 species, creating a spatially and temporally uneven sample of British bat fauna. Uniquely, three UK cases originate from a roost at Stokesay Castle in Shropshire, England, where daily checks for grounded and dead bats are undertaken and bat carcasses have been submitted for testing since 2007. Twenty per cent of Daubenton's bats submitted from Stokesay Castle since surveillance began, have tested positive for EBLV-2. Phylogenetic analysis reveals geographical clustering of UK viruses. Isolates from Stokesay Castle are more closely related to one another than to viruses from other regions. Daubenton's bats from Stokesay Castle represent a unique opportunity to study a natural population that appears to maintain EBLV-2 infection and may represent endemic infection at this site. Although the risk to public health from EBLV-2 is low, consequences of infection are severe and effective communication on the need for prompt post-exposure prophylaxis for anyone that has been bitten by a bat is essential.
[Mh] Termos MeSH primário: Quirópteros
Lyssavirus/isolamento & purificação
Infecções por Rhabdoviridae/veterinária
[Mh] Termos MeSH secundário: Animais
Monitoramento Epidemiológico/veterinária
Proteínas do Nucleocapsídeo/genética
Filogenia
Infecções por Rhabdoviridae/epidemiologia
Infecções por Rhabdoviridae/virologia
Análise de Sequência de DNA/veterinária
Reino Unido/epidemiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Nucleocapsid Proteins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171125
[Lr] Data última revisão:
171125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170725
[St] Status:MEDLINE
[do] DOI:10.1017/S0950268817001455



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