Base de dados : MEDLINE
Pesquisa : A21.249.500 [Categoria DeCS]
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[PMID]:29300742
[Au] Autor:Oliveira LM; Ye Z; Katz A; Alimova A; Wei H; Herman GT; Gottlieb P
[Ad] Endereço:Department of Computer Science, Graduate Center of the City University of New York, New York, NY, United States of America.
[Ti] Título:Component tree analysis of cystovirus φ6 nucleocapsid Cryo-EM single particle reconstructions.
[So] Source:PLoS One;13(1):e0188858, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The 3-dimensional structure of the nucleocapsid (NC) of bacteriophage φ6 is described utilizing component tree analysis, a topological and geometric image descriptor. The component trees are derived from density maps of cryo-electron microscopy single particle reconstructions. Analysis determines position and occupancy of structure elements responsible for RNA packaging and transcription. Occupancy of the hexameric nucleotide triphosphorylase (P4) and RNA polymerase (P2) are found to be essentially complete in the NC. The P8 protein lattice likely fixes P4 and P2 in place during maturation. We propose that the viral procapsid (PC) is a dynamic structural intermediate where the P4 and P2 can attach and detach until held in place in mature NCs. During packaging, the PC expands to accommodate the RNA, and P2 translates from its original site near the inner 3-fold axis (20 sites) to the inner 5-fold axis (12 sites) with excess P2 positioned inside the central region of the NC.
[Mh] Termos MeSH primário: Microscopia Crioeletrônica/métodos
Cystoviridae/ultraestrutura
Nucleocapsídeo/ultraestrutura
Proteínas Virais/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Viral Proteins)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180129
[Lr] Data última revisão:
180129
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180105
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0188858


  2 / 1040 MEDLINE  
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[PMID]:28968422
[Au] Autor:Guo YJ; Fu SH; Li LL
[Ad] Endereço:Hubei Key Laboratory of Genetic Regulation and Integrative Biology, College of Life Sciences, Central China Normal University, Wuhan, China.
[Ti] Título:Autographa californica multiple nucleopolyhedrovirus ac75 is required for egress of nucleocapsids from the nucleus and formation of de novo intranuclear membrane microvesicles.
[So] Source:PLoS One;12(10):e0185630, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In this study, Autographa californica multiple nucleopolyhedrovirus ac75 was functionally characterized. Ac75 has homologs in all sequenced genomes of alphabaculoviruses, betabaculoviruses, and gammabaculoviruses. It was determined to encode a protein that is associated with the nucleocapsid of budded virus and with both envelope and nucleocapsids of occlusion-derived virus. Sf9 cells transfected by an ac75-knockout bacmid resulted in the infection being restricted to single cells. No budded virus were detected although viral DNA replication and late gene expression were unaffected. Electron microscopy revealed that the virogenic stroma, nucleocapsids and occlusion bodies appeared normal in the cells transfected by an ac75-knockout bacmid. However, the nucleocapsids were unenveloped, the occlusion bodies did not contain any virions or nucleocapsids, and no nucleocapsids were found outside the nucleus or spanning the nuclear membrane. In addition, de novo intranuclear membrane microvesicles that are the precursor of occlusion-derived virus envelopes were absent in the nuclei of transfected cells. Confocal microscopy showed that AC75 protein appeared in the cytoplasm as early as 6 hours post infection. It localized to the ring zone at the periphery of the nucleus from 15 to 24 hours post infection and demonstrated light blocky cloud-like distribution in the center of the nucleus. AC75 was found to co-immunoprecipitate with BV and ODV associated envelope protein ODV-E25. The data from this study suggest that ac75 is essential for induction of the intranuclear membrane microvesicles, it appears to be required for the intranuclear envelopment of nucleocapsids, and is also essential for egress of nucleocapsids from the nuclei, in infected cells.
[Mh] Termos MeSH primário: Núcleo Celular/metabolismo
Genes Virais
Membrana Nuclear/metabolismo
Nucleocapsídeo/metabolismo
Nucleopolyhedrovirus/genética
[Mh] Termos MeSH secundário: Animais
Transporte Biológico
Western Blotting
DNA Viral/biossíntese
Técnicas de Silenciamento de Genes
Microscopia Confocal
Microscopia Eletrônica de Transmissão
Plasmídeos
Reação em Cadeia da Polimerase em Tempo Real
Células Sf9
Replicação Viral/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Viral)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171003
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185630


  3 / 1040 MEDLINE  
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[PMID]:28945802
[Au] Autor:Guo F; Zhao Q; Sheraz M; Cheng J; Qi Y; Su Q; Cuconati A; Wei L; Du Y; Li W; Chang J; Guo JT
[Ad] Endereço:Baruch S. Blumberg Institute, Doylestown, Pennsylvania, United States of America.
[Ti] Título:HBV core protein allosteric modulators differentially alter cccDNA biosynthesis from de novo infection and intracellular amplification pathways.
[So] Source:PLoS Pathog;13(9):e1006658, 2017 Sep.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hepatitis B virus (HBV) core protein assembles viral pre-genomic (pg) RNA and DNA polymerase into nucleocapsids for reverse transcriptional DNA replication to take place. Several chemotypes of small molecules, including heteroaryldihydropyrimidines (HAPs) and sulfamoylbenzamides (SBAs), have been discovered to allosterically modulate core protein structure and consequentially alter the kinetics and pathway of core protein assembly, resulting in formation of irregularly-shaped core protein aggregates or "empty" capsids devoid of pre-genomic RNA and viral DNA polymerase. Interestingly, in addition to inhibiting nucleocapsid assembly and subsequent viral genome replication, we have now demonstrated that HAPs and SBAs differentially modulate the biosynthesis of covalently closed circular (ccc) DNA from de novo infection and intracellular amplification pathways by inducing disassembly of nucleocapsids derived from virions as well as double-stranded DNA-containing progeny nucleocapsids in the cytoplasm. Specifically, the mistimed cuing of nucleocapsid uncoating prevents cccDNA formation during de novo infection of hepatocytes, while transiently accelerating cccDNA synthesis from cytoplasmic progeny nucleocapsids. Our studies indicate that elongation of positive-stranded DNA induces structural changes of nucleocapsids, which confers ability of mature nucleocapsids to bind CpAMs and triggers its disassembly. Understanding the molecular mechanism underlying the dual effects of the core protein allosteric modulators on nucleocapsid assembly and disassembly will facilitate the discovery of novel core protein-targeting antiviral agents that can more efficiently suppress cccDNA synthesis and cure chronic hepatitis B.
[Mh] Termos MeSH primário: DNA Circular/biossíntese
Vírus da Hepatite B/fisiologia
Hepatite B Crônica/virologia
Replicação Viral/efeitos dos fármacos
[Mh] Termos MeSH secundário: Antivirais/farmacologia
Linhagem Celular
DNA Circular/genética
DNA Viral
DNA Polimerase Dirigida por DNA/metabolismo
Hepatócitos/virologia
Seres Humanos
Nucleocapsídeo/efeitos dos fármacos
Nucleocapsídeo/genética
Reação em Cadeia da Polimerase em Tempo Real
Replicação Viral/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antiviral Agents); 0 (DNA, Circular); 0 (DNA, Viral); EC 2.7.7.7 (DNA-Directed DNA Polymerase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171022
[Lr] Data última revisão:
171022
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170926
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006658


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[PMID]:28768856
[Au] Autor:Mura M; Combredet C; Najburg V; Sanchez David RY; Tangy F; Komarova AV
[Ad] Endereço:Unité de Génomique Virale et Vaccination, Institut Pasteur, CNRS UMR-3569, Paris, France.
[Ti] Título:Nonencapsidated 5' Copy-Back Defective Interfering Genomes Produced by Recombinant Measles Viruses Are Recognized by RIG-I and LGP2 but Not MDA5.
[So] Source:J Virol;91(20), 2017 Oct 15.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Attenuated measles virus (MV) is one of the most effective and safe vaccines available, making it an attractive candidate vector for preventing other infectious diseases. Yet the great capacity of this vaccine still needs to be understood at the molecular level. MV vaccine strains have different type I interferon (IFN)-inducing abilities that partially depend on the presence of 5' copy-back defective interfering genomes (DI-RNAs). DI-RNAs are pathogen-associated molecular patterns recognized by RIG-I-like receptors (RLRs) (RIG-I, MDA5, and LGP2) that activate innate immune signaling and shape the adaptive immune response. In this study, we characterized the DI-RNAs produced by various modified recombinant MVs (rMVs), including vaccine candidates, as well as wild-type MV. All tested rMVs produced 5' copy-back DI-RNAs that were different in length and nucleotide sequence but still respected the so-called "rule of six." We correlated the presence of DI-RNAs with a larger stimulation of the IFN-ß pathway and compared their immunostimulatory potentials. Importantly, we revealed that encapsidation of DI-RNA molecules within the MV nucleocapsid abolished their immunoactive properties. Furthermore, we identified specific interactions of DI-RNAs with both RIG-I and LGP2 but not MDA5. Our results suggest that DI-RNAs produced by rMV vaccine candidates may indeed strengthen their efficiency by triggering RLR signaling. Having been administered to hundreds of millions of children, the live attenuated measles virus (MV) vaccine is the safest and most widely used human vaccine, providing high protection with long-term memory. Additionally, recombinant MVs carrying heterologous antigens are promising vectors for new vaccines. The great capacity of this vaccine still needs to be elucidated at the molecular level. Here we document that recombinant MVs produce defective interfering genomes that have high immunostimulatory properties via their binding to RIG-I and LGP2 proteins, both of which are cytosolic nonself RNA sensors of innate immunity. Defective interfering genome production during viral replication should be considered of great importance due to the immunostimulatory properties of these genomes as intrinsic adjuvants produced by the vector that increase recognition by the innate immune system.
[Mh] Termos MeSH primário: Genoma Viral
Helicase IFIH1 Induzida por Interferon/metabolismo
Vírus do Sarampo/genética
RNA Helicases/metabolismo
RNA Viral/genética
RNA Viral/metabolismo
Receptores do Ácido Retinoico/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular
Seres Humanos
Imunidade Inata
Interferon beta/metabolismo
Sarampo/virologia
Vacina contra Sarampo/genética
Vacina contra Sarampo/imunologia
Vírus do Sarampo/patogenicidade
Nucleocapsídeo/metabolismo
RNA Viral/imunologia
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Measles Vaccine); 0 (RARRES3 protein, human); 0 (RNA, Viral); 0 (Receptors, Retinoic Acid); 77238-31-4 (Interferon-beta); EC 2.7.7.- (DHX58 protein, human); EC 3.6.1.- (IFIH1 protein, human); EC 3.6.4.13 (Interferon-Induced Helicase, IFIH1); EC 3.6.4.13 (RNA Helicases)
[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


  5 / 1040 MEDLINE  
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[PMID]:28679756
[Au] Autor:Kobayashi R; Kato A; Sagara H; Watanabe M; Maruzuru Y; Koyanagi N; Arii J; Kawaguchi Y
[Ad] Endereço:Division of Molecular Virology, Department of Microbiology and Immunology, The Institute of Medical Science, The University of Tokyo, Tokyo, Japan.
[Ti] Título:Herpes Simplex Virus 1 Small Capsomere-Interacting Protein VP26 Regulates Nucleocapsid Maturation.
[So] Source:J Virol;91(18), 2017 Sep 15.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:VP26 is a herpes simplex virus 1 (HSV-1) small capsomere-interacting protein. In this study, we investigated the function of VP26 in HSV-1-infected cells with the following results. (i) The VP26 null mutation significantly impaired incorporation of minor capsid protein UL25 into nucleocapsids (type C capsids) in the nucleus. (ii) The VP26 mutation caused improper localization of UL25 in discrete punctate domains containing multiple capsid proteins (e.g., the VP5 major capsid protein) in the nucleus; these domains corresponded to capsid aggregates. (iii) The VP26 mutation significantly impaired packaging of replicated viral DNA genomes into capsids but had no effect on viral DNA concatemer cleavage. (iv) The VP26 mutation reduced the frequency of type C capsids, which contain viral DNA but not scaffolding proteins, and produced an accumulation of type A capsids, which lack both viral DNA and scaffold proteins, and had no effect on accumulation of type B capsids, which lack viral DNA but retain cleaved scaffold proteins. Collectively, these results indicated that VP26 was required for efficient viral DNA packaging and proper localization of nuclear capsids. The phenotype of the VP26 null mutation was similar to that reported previously of the UL25 null mutation and of UL25 mutations that preclude UL25 binding to capsids. Thus, VP26 appeared to regulate nucleocapsid maturation by promoting incorporation of UL25 into capsids, which is likely to be required for proper capsid nuclear localization. HSV-1 VP26 has been reported to be important for viral replication and virulence in cell cultures and/or mouse models. However, little is known about the function of VP26 during HSV-1 replication, in particular, in viral nucleocapsid maturation although HSV-1 nucleocapsids are estimated to contain 900 copies of VP26. In this study, we present data suggesting that VP26 promoted packaging of HSV-1 DNA genomes into capsids by regulating incorporation of capsid protein UL25 into capsids, which was reported to increase stability of the capsid structure. We also showed that VP26 was required for proper localization of capsids in the infected cell nucleus. This is the first report showing that HSV-1 VP26 is a regulator for nucleocapsid maturation.
[Mh] Termos MeSH primário: Proteínas do Capsídeo/metabolismo
Herpesvirus Humano 1/fisiologia
Nucleocapsídeo/metabolismo
Montagem de Vírus
[Mh] Termos MeSH secundário: Animais
Proteínas do Capsídeo/genética
Linhagem Celular
Técnicas de Inativação de Genes
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Capsid Proteins); 0 (capsid protein VP26, herpes simplex virus type 1)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170707
[St] Status:MEDLINE


  6 / 1040 MEDLINE  
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[PMID]:28575072
[Au] Autor:Mangala Prasad V; Klose T; Rossmann MG
[Ad] Endereço:Department of Biological Sciences, 240 S. Martin Jischke Drive, Purdue University, West Lafayette, IN, United States of America.
[Ti] Título:Assembly, maturation and three-dimensional helical structure of the teratogenic rubella virus.
[So] Source:PLoS Pathog;13(6):e1006377, 2017 Jun.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Viral infections during pregnancy are a significant cause of infant morbidity and mortality. Of these, rubella virus infection is a well-substantiated example that leads to miscarriages or severe fetal defects. However, structural information about the rubella virus has been lacking due to the pleomorphic nature of the virions. Here we report a helical structure of rubella virions using cryo-electron tomography. Sub-tomogram averaging of the surface spikes established the relative positions of the viral glycoproteins, which differed from the earlier icosahedral models of the virus. Tomographic analyses of in vitro assembled nucleocapsids and virions provide a template for viral assembly. Comparisons of immature and mature virions show large rearrangements in the glycoproteins that may be essential for forming the infectious virions. These results present the first known example of a helical membrane-enveloped virus, while also providing a structural basis for its assembly and maturation pathway.
[Mh] Termos MeSH primário: Vírus da Rubéola/fisiologia
Rubéola (Sarampo Alemão)/virologia
Montagem de Vírus
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Tomografia com Microscopia Eletrônica
Seres Humanos
Nucleocapsídeo/genética
Nucleocapsídeo/metabolismo
Rubéola (Sarampo Alemão)/embriologia
Rubéola (Sarampo Alemão)/patologia
Vírus da Rubéola/química
Vírus da Rubéola/genética
Vírus da Rubéola/ultraestrutura
Teratogênese
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170921
[Lr] Data última revisão:
170921
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170603
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006377


  7 / 1040 MEDLINE  
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[PMID]:28383274
[Au] Autor:Pei Y; Wang C; Yan SF; Liu G
[Ad] Endereço:School of Pharmaceutical Sciences, Tsinghua University , Beijing 100084, China.
[Ti] Título:Past, Current, and Future Developments of Therapeutic Agents for Treatment of Chronic Hepatitis B Virus Infection.
[So] Source:J Med Chem;60(15):6461-6479, 2017 Aug 10.
[Is] ISSN:1520-4804
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:For decades, treatment of hepatitis B virus (HBV) infection has been relying on interferon (IFN)-based therapies and nucleoside/nucleotide analogues (NAs) that selectively target the viral polymerase reverse transcriptase (RT) domain and thereby disrupt HBV viral DNA synthesis. We have summarized here the key steps in the HBV viral life cycle, which could potentially be targeted by novel anti-HBV therapeutics. A wide range of next-generation direct antiviral agents (DAAs) with distinct mechanisms of actions are discussed, including entry inhibitors, transcription inhibitors, nucleoside/nucleotide analogues, inhibitors of viral ribonuclease H (RNase H), modulators of viral capsid assembly, inhibitors of HBV surface antigen (HBsAg) secretion, RNA interference (RNAi) gene silencers, antisense oligonucleotides (ASOs), and natural products. Compounds that exert their antiviral activities mainly through host factors and immunomodulation, such as host targeting agents (HTAs), programmed cell death protein 1 (PD-1)/programmed death ligand 1 (PD-L1) inhibitors, and Toll-like receptor (TLR) agonists, are also discussed. In this Perspective, we hope to provide an overview, albeit by no means being comprehensive, for the recent development of novel therapeutic agents for the treatment of chronic HBV infection, which not only are able to sustainably suppress viral DNA but also aim to achieve functional cure warranted by HBsAg loss and ultimately lead to virus eradication and cure of hepatitis B.
[Mh] Termos MeSH primário: Antivirais/uso terapêutico
Vírus da Hepatite B/efeitos dos fármacos
Hepatite B Crônica/tratamento farmacológico
[Mh] Termos MeSH secundário: Antígeno B7-H1/antagonistas & inibidores
Produtos Biológicos/uso terapêutico
Reposicionamento de Medicamentos
Proteínas de Choque Térmico HSC70/antagonistas & inibidores
Proteínas de Choque Térmico HSP90/antagonistas & inibidores
Antígenos de Superfície da Hepatite B/metabolismo
Vírus da Hepatite B/fisiologia
Seres Humanos
Nucleocapsídeo/antagonistas & inibidores
Oligonucleotídeos Antissenso/uso terapêutico
Receptor de Morte Celular Programada 1/antagonistas & inibidores
Terapêutica com RNAi
Ribonuclease H/antagonistas & inibidores
Receptores Toll-Like/agonistas
Internalização do Vírus/efeitos dos fármacos
Replicação Viral/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antiviral Agents); 0 (B7-H1 Antigen); 0 (Biological Products); 0 (CD274 protein, human); 0 (HSC70 Heat-Shock Proteins); 0 (HSP90 Heat-Shock Proteins); 0 (HSPA8 protein, human); 0 (Hepatitis B Surface Antigens); 0 (Oligonucleotides, Antisense); 0 (PDCD1 protein, human); 0 (Programmed Cell Death 1 Receptor); 0 (Toll-Like Receptors); EC 3.1.26.4 (Ribonuclease H)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170407
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jmedchem.6b01442


  8 / 1040 MEDLINE  
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[PMID]:28359901
[Au] Autor:Lu G; Li J; Zhou Y; Zhou X; Tao X
[Ad] Endereço:Department of Plant Pathology, Nanjing Agricultural University, Nanjing 210095, PR China.
[Ti] Título:Model-based structural and functional characterization of the Rice stripe tenuivirus nucleocapsid protein interacting with viral genomic RNA.
[So] Source:Virology;506:73-83, 2017 Jun.
[Is] ISSN:1096-0341
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Rice stripe tenuivirus (RSV) is a filamentous, negative-strand RNA virus causing severe diseases on rice in Asian countries. The viral particle is composed predominantly of a nucleocapsid protein (NP) and genomic RNA. However, the molecular details of how the RSV NP interacts with genomic RNA during particle assembly remain largely unknown. Here, we modeled the NP-RNA complex and show that polar amino acids within a predicted groove of NP are critical for RNA binding and protecting the RNA from RNase digestion. RSV NP formed pentamers, hexamers, heptamers, and octamers. By modeling the higher-order structures, we found that oligomer formation was driven by the N-terminal amino arm of the NP. Deletion of this arm abolished oligomerization; the N-terminally truncated NP was less able to interact with RNA and protect RNA than was the wild type. These findings afford valuable new insights into molecular mechanism of RSV NPs interacting with genomic RNA.
[Mh] Termos MeSH primário: Nucleocapsídeo/metabolismo
Oryza/virologia
Doenças das Plantas/virologia
RNA Viral/metabolismo
Tenuivirus/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Modelos Moleculares
Dados de Sequência Molecular
Nucleocapsídeo/química
Nucleocapsídeo/genética
Ligação Proteica
RNA Viral/química
RNA Viral/genética
Alinhamento de Sequência
Tenuivirus/química
Tenuivirus/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Viral)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170705
[Lr] Data última revisão:
170705
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170401
[St] Status:MEDLINE


  9 / 1040 MEDLINE  
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[PMID]:28356536
[Au] Autor:Maeda F; Arii J; Hirohata Y; Maruzuru Y; Koyanagi N; Kato A; Kawaguchi Y
[Ad] Endereço:Division of Molecular Virology, Department of Microbiology and Immunology, The Institute of Medical Science, The University of Tokyo, Tokyo, Japan.
[Ti] Título:Herpes Simplex Virus 1 UL34 Protein Regulates the Global Architecture of the Endoplasmic Reticulum in Infected Cells.
[So] Source:J Virol;91(12), 2017 Jun 15.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Upon herpes simplex virus 1 (HSV-1) infection, the CD98 heavy chain (CD98hc) is redistributed around the nuclear membrane (NM), where it promotes viral de-envelopment during the nuclear egress of nucleocapsids. In this study, we attempted to identify the factor(s) involved in CD98hc accumulation and demonstrated the following: (i) the null mutation of HSV-1 UL34 caused specific dispersion throughout the cytoplasm of CD98hc and the HSV-1 de-envelopment regulators, glycoproteins B and H (gB and gH); (ii) as observed with CD98hc, gB, and gH, wild-type HSV-1 infection caused redistribution of the endoplasmic reticulum (ER) markers calnexin and ERp57 around the NM, whereas the UL34-null mutation caused cytoplasmic dispersion of these markers; (iii) the ER markers colocalized efficiently with CD98hc, gB, and gH in the presence and absence of UL34 in HSV-1-infected cells; (iv) at the ultrastructural level, wild-type HSV-1 infection caused ER compression around the NM, whereas the UL34-null mutation caused cytoplasmic dispersion of the ER; and (v) the UL34-null mutation significantly decreased the colocalization efficiency of lamin protein markers of the NM with CD98hc and gB. Collectively, these results indicate that HSV-1 infection causes redistribution of the ER around the NM, with resulting accumulation of ER-associated CD98hc, gB, and gH around the NM and that UL34 is required for ER redistribution, as well as for efficient recruitment to the NM of the ER-associated de-envelopment factors. Our study suggests that HSV-1 induces remodeling of the global ER architecture for recruitment of regulators mediating viral nuclear egress to the NM. The ER is an important cellular organelle that exists as a complex network extending throughout the cytoplasm. Although viruses often remodel the ER to facilitate viral replication, information on the effects of herpesvirus infections on ER morphological integrity is limited. Here, we showed that HSV-1 infection led to compression of the global ER architecture around the NM, resulting in accumulation of ER-associated regulators associated with nuclear egress of HSV-1 nucleocapsids. We also identified HSV-1 UL34 as a viral factor that mediated ER remodeling. Furthermore, we demonstrated that UL34 was required for efficient targeting of these regulators to the NM. To our knowledge, this is the first report showing that a herpesvirus remodels ER global architecture. Our study also provides insight into the mechanism by which the regulators for HSV-1 nuclear egress are recruited to the NM, where this viral event occurs.
[Mh] Termos MeSH primário: Retículo Endoplasmático/ultraestrutura
Retículo Endoplasmático/virologia
Herpesvirus Humano 1/genética
Herpesvirus Humano 1/fisiologia
Proteínas Virais/metabolismo
[Mh] Termos MeSH secundário: Transporte Ativo do Núcleo Celular
Animais
Calnexina/metabolismo
Cercopithecus aethiops
Retículo Endoplasmático/metabolismo
Retículo Endoplasmático/patologia
Proteína-1 Reguladora de Fusão/metabolismo
Herpesvirus Humano 1/química
Seres Humanos
Mutação
Membrana Nuclear/fisiologia
Membrana Nuclear/virologia
Nucleocapsídeo/metabolismo
Ligação Proteica
Células Vero
Proteínas Virais/genética
Montagem de Vírus
Liberação de Vírus
Replicação Viral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fusion Regulatory Protein-1); 0 (UL34 protein, Human herpesvirus 1); 0 (Viral Proteins); 139873-08-8 (Calnexin)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171126
[Lr] Data última revisão:
171126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170331
[St] Status:MEDLINE


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[PMID]:28179533
[Au] Autor:Matsumoto Y; Ohta K; Kolakofsky D; Nishio M
[Ad] Endereço:Department of Microbiology, School of Medicine, Wakayama Medical University, Wakayama, Japan ymatsu@wakayama-med.ac.jp.
[Ti] Título:A Point Mutation in the RNA-Binding Domain of Human Parainfluenza Virus Type 2 Nucleoprotein Elicits Abnormally Enhanced Polymerase Activity.
[So] Source:J Virol;91(9), 2017 May 01.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The genome RNA of human parainfluenza virus type 2 (hPIV2) that acts as the template for the polymerase complex is entirely encapsidated by the nucleoprotein (NP). Recently, the crystal structure of NP of PIV5, a virus closely related to hPIV2, was resolved in association with RNA. Ten amino acids that contact the bound RNA were identified and are strictly conserved between PIV5 and hPIV2 NP. Mutation of hPIV2 NP Q202 (which contacts a base rather than the RNA backbone) to various amino acids resulted in an over 30-fold increase of polymerase activity as evidenced by a minireplicon assay, even though the RNA-binding affinity was unaltered. Using various modified minireplicons, we found that the enhanced reporter gene expression could be accounted for by increased minigenome replication, whereas mRNA synthesis itself was not affected by Q202 mutation. Moreover, the enhanced activities were still observed in minigenomes partially lacking the leader sequence and which were not of hexamer genome length. Unexpectedly, recombinant hPIV2 possessing the NP Q202A mutation could not be recovered from cDNA. We examined the importance of amino acids in the putative RNA-binding domain of hPIV2 NP for polymerase activity using minireplicons. Abnormally enhanced genome replication was observed upon substitution mutation of the NP Q202 position to various amino acids. Surprisingly, this mutation enabled polymerase to use minigenomes that were partially lacking the leader sequence and not of hexamer genome length. This mutation does not affect fundamental properties of NP, e.g., recognition of gene junctional and editing signals. However, the strongly enhanced polymerase activity may not be viable for the infectious life cycle. This report highlights the potential of the polymerase complex with point mutations in NP and helps our detailed understanding of the molecular basis of gene expression.
[Mh] Termos MeSH primário: Nucleocapsídeo/metabolismo
Nucleoproteínas/genética
Vírus da Parainfluenza 2 Humana/genética
RNA Replicase/metabolismo
Motivos de Ligação ao RNA/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sítios de Ligação/genética
Linhagem Celular
Genoma Viral/genética
Seres Humanos
Mutação Puntual/genética
RNA Replicase/genética
RNA Viral/biossíntese
RNA Viral/genética
Transcrição Genética
Proteínas Virais/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nucleoproteins); 0 (RNA, Viral); 0 (Viral Proteins); EC 2.7.7.48 (RNA Replicase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171013
[Lr] Data última revisão:
171013
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170210
[St] Status:MEDLINE



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