Base de dados : MEDLINE
Pesquisa : B04.715.081.080 [Categoria DeCS]
Referências encontradas : 417 [refinar]
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[PMID]:29334364
[Au] Autor:Losdorfer Bozic A; Micheletti C; Podgornik R; Tubiana L
[Ad] Endereço:Department of Theoretical Physics, Jozef Stefan Institute, SI-1000 Ljubljana, Slovenia.
[Ti] Título:Compactness of viral genomes: effect of disperse and localized random mutations.
[So] Source:J Phys Condens Matter;30(8):084006, 2018 Feb 28.
[Is] ISSN:1361-648X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Genomes of single-stranded RNA viruses have evolved to optimize several concurrent properties. One of them is the architecture of their genomic folds, which must not only feature precise structural elements at specific positions, but also allow for overall spatial compactness. The latter was shown to be disrupted by random synonymous mutations, a disruption which can consequently negatively affect genome encapsidation. In this study, we use three mutation schemes with different degrees of locality to mutate the genomes of phage MS2 and Brome Mosaic virus in order to understand the observed sensitivity of the global compactness of their folds. We find that mutating local stretches of their genomes' sequence or structure is less disruptive to their compactness compared to inducing randomly-distributed mutations. Our findings are indicative of a mechanism for the conservation of compactness acting on a global scale of the genomes, and have several implications for understanding the interplay between local and global architecture of viral RNA genomes.
[Mh] Termos MeSH primário: Bromovirus/genética
Levivirus/genética
Conformação de Ácido Nucleico
[Mh] Termos MeSH secundário: Genoma Viral
RNA
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
63231-63-0 (RNA)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180208
[Lr] Data última revisão:
180208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180116
[St] Status:MEDLINE
[do] DOI:10.1088/1361-648X/aaa7b0


  2 / 417 MEDLINE  
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[PMID]:28711172
[Au] Autor:Beren C; Dreesens LL; Liu KN; Knobler CM; Gelbart WM
[Ad] Endereço:Department of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, California.
[Ti] Título:The Effect of RNA Secondary Structure on the Self-Assembly of Viral Capsids.
[So] Source:Biophys J;113(2):339-347, 2017 Jul 25.
[Is] ISSN:1542-0086
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Previous work has shown that purified capsid protein (CP) of cowpea chlorotic mottle virus (CCMV) is capable of packaging both purified single-stranded RNA molecules of normal composition (comparable numbers of A, U, G, and C nucleobases) and of varying length and sequence, and anionic synthetic polymers such as polystyrene sulfonate. We find that CCMV CP is also capable of packaging polyU RNAs, which-unlike normal-composition RNAs-do not form secondary structures and which act as essentially structureless linear polymers. Following our canonical two-step assembly protocol, polyU RNAs ranging in length from 1000 to 9000 nucleotides (nt) are completely packaged. Surprisingly, negative-stain electron microscopy shows that all lengths of polyU are packaged into 22-nm-diameter particles despite the fact that CCMV CP prefers to form 28-nm-diameter (T = 3) particles when packaging normal-composition RNAs. PolyU RNAs >5000 nt in length are packaged into multiplet capsids, in which a single RNA molecule is shared between two or more 22-nm-diameter capsids, in analogy with the multiplets of 28-nm-diameter particles formed with normal-composition RNAs >5000 nt long. Experiments in which viral RNA competes for viral CP with polyUs of equal length show that polyU, despite its lack of secondary structure, is packaged more efficiently than viral RNA. These findings illustrate that the secondary structure of the RNA molecule-and its absence-plays an essential role in determining capsid structure during the self-assembly of CCMV-like particles.
[Mh] Termos MeSH primário: Bromovirus/fisiologia
Proteínas do Capsídeo/metabolismo
Capsídeo/metabolismo
Conformação de Ácido Nucleico
RNA Viral
Montagem de Vírus
[Mh] Termos MeSH secundário: Bromovirus/química
Bromovirus/genética
Bromovirus/ultraestrutura
Capsídeo/química
Capsídeo/ultraestrutura
Proteínas do Capsídeo/química
Ensaio de Desvio de Mobilidade Eletroforética
Microscopia Eletrônica de Transmissão
RNA Viral/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Capsid Proteins); 0 (RNA, Viral)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170821
[Lr] Data última revisão:
170821
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170717
[St] Status:MEDLINE


  3 / 417 MEDLINE  
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[PMID]:28383276
[Au] Autor:Antal Z; Szoverfi J; Fejer SN
[Ad] Endereço:Provitam Foundation , 16 Caisului Street, Cluj-Napoca, Romania.
[Ti] Título:Predicting the Initial Steps of Salt-Stable Cowpea Chlorotic Mottle Virus Capsid Assembly with Atomistic Force Fields.
[So] Source:J Chem Inf Model;57(4):910-917, 2017 Apr 24.
[Is] ISSN:1549-960X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Computational prediction of native protein-protein interfaces still remains a challenging task. In virus capsids, each protein unit is in contact with copies of itself through several interfaces. The relative strengths of the different contacts affect the dynamics of the assembly, especially if the process is hierarchical. We investigate the dimerization of the salt-stable cowpea chlorotic mottle virus (CCMV) capsid protein using a combination of different computational tools. The best predictions of dimer configurations provided by blind docking with ZDOCK are rescored using geometry optimization with the Amber and Rosetta force fields. We also evaluate the relative stabilities of the three main interfaces present in the icosahedral capsid using locally restricted docking with Rosetta. Both the rescoring and locally restricted docking results report a particularly stable protein-protein interface, which is the most likely intermediate during the first stage of the hierarchical capsid assembly. The blind docking results rescored with both Amber and Rosetta yield docking funnels, i.e., three or more near-native structures among the top five predictions. The results support experimental observations on in vitro assembly of CCMV capsids. The cross-validation of the results suggests that energy-landscape-based methods with biomolecular force fields have the potential to improve existing docking procedures.
[Mh] Termos MeSH primário: Bromovirus/química
Proteínas do Capsídeo/química
Simulação de Acoplamento Molecular
Agregados Proteicos/efeitos dos fármacos
Sais/farmacologia
[Mh] Termos MeSH secundário: Simulação de Dinâmica Molecular
Conformação Proteica
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Capsid Proteins); 0 (Protein Aggregates); 0 (Salts)
[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:170407
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jcim.7b00078


  4 / 417 MEDLINE  
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[PMID]:28009841
[Au] Autor:Jungfleisch J; Blasco-Moreno B; Díez J
[Ad] Endereço:Molecular Virology Laboratory, Department of Experimental and Health Sciences, Universitat Pompeu Fabra, Barcelona 08003, Spain. Jennifer.Jungfleisch@upf.edu.
[Ti] Título:Use of Cellular Decapping Activators by Positive-Strand RNA Viruses.
[So] Source:Viruses;8(12), 2016 Dec 21.
[Is] ISSN:1999-4915
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Positive-strand RNA viruses have evolved multiple strategies to not only circumvent the hostile decay machinery but to trick it into being a priceless collaborator supporting viral RNA translation and replication. In this review, we describe the versatile interaction of positive-strand RNA viruses and the 5'-3' mRNA decay machinery with a focus on the viral subversion of decapping activators. This highly conserved viral trickery is exemplified with the plant Brome mosaic virus, the animal Flock house virus and the human hepatitis C virus.
[Mh] Termos MeSH primário: Bromovirus/fisiologia
Endorribonucleases/metabolismo
Hepacivirus/fisiologia
Interações Hospedeiro-Patógeno
Nodaviridae/fisiologia
Biossíntese de Proteínas
Replicação Viral
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Estabilidade de RNA
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (mRNA decapping enzymes); EC 3.1.- (Endoribonucleases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170913
[Lr] Data última revisão:
170913
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161224
[St] Status:MEDLINE


  5 / 417 MEDLINE  
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[PMID]:27572730
[Au] Autor:DiMaio F; Chiu W
[Ad] Endereço:University of Washington, Seattle, WA, United States; Institute for Protein Design, University of Washington, Seattle, WA, United States. Electronic address: dimaio@u.washington.edu.
[Ti] Título:Tools for Model Building and Optimization into Near-Atomic Resolution Electron Cryo-Microscopy Density Maps.
[So] Source:Methods Enzymol;579:255-76, 2016.
[Is] ISSN:1557-7988
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Electron cryo-microscopy (cryoEM) has advanced dramatically to become a viable tool for high-resolution structural biology research. The ultimate outcome of a cryoEM study is an atomic model of a macromolecule or its complex with interacting partners. This chapter describes a variety of algorithms and software to build a de novo model based on the cryoEM 3D density map, to optimize the model with the best stereochemistry restraints and finally to validate the model with proper protocols. The full process of atomic structure determination from a cryoEM map is described. The tools outlined in this chapter should prove extremely valuable in revealing atomic interactions guided by cryoEM data.
[Mh] Termos MeSH primário: Algoritmos
Microscopia Crioeletrônica/métodos
Processamento de Imagem Assistida por Computador/estatística & dados numéricos
Software
[Mh] Termos MeSH secundário: Antígenos Virais/ultraestrutura
Proteínas de Bactérias/ultraestrutura
Bromovirus/ultraestrutura
Proteínas do Capsídeo/ultraestrutura
Microscopia Crioeletrônica/instrumentação
Processamento de Imagem Assistida por Computador/métodos
Imagem Tridimensional/instrumentação
Imagem Tridimensional/métodos
Modelos Moleculares
Conformação Proteica
beta-Galactosidase/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antigens, Viral); 0 (Bacterial Proteins); 0 (Capsid Proteins); 0 (VP6 protein, Rotavirus); EC 3.2.1.23 (beta-Galactosidase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170811
[Lr] Data última revisão:
170811
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160831
[St] Status:MEDLINE


  6 / 417 MEDLINE  
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[PMID]:27539921
[Au] Autor:Li J; Fuchs S; Zhang J; Wellford S; Schuldiner M; Wang X
[Ad] Endereço:Department of Plant Pathology, Physiology, and Weed Science, Virginia Tech, Blacksburg, VA 24061, USA.
[Ti] Título:An unrecognized function for COPII components in recruiting the viral replication protein BMV 1a to the perinuclear ER.
[So] Source:J Cell Sci;129(19):3597-3608, 2016 Oct 01.
[Is] ISSN:1477-9137
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Positive-strand RNA viruses invariably assemble their viral replication complexes (VRCs) by remodeling host intracellular membranes. How viral replication proteins are targeted to specific organelle membranes to initiate VRC assembly remains elusive. Brome mosaic virus (BMV), whose replication can be recapitulated in Saccharomyces cerevisiae, assembles its VRCs by invaginating the outer perinuclear endoplasmic reticulum (ER) membrane. Remarkably, BMV replication protein 1a (BMV 1a) is the only viral protein required for such membrane remodeling. We show that ER-vesicle protein of 14 kD (Erv14), a cargo receptor of coat protein complex II (COPII), interacts with BMV 1a. Moreover, the perinuclear ER localization of BMV 1a is disrupted in cells lacking ERV14 or expressing dysfunctional COPII coat components (Sec13, Sec24 or Sec31). The requirement of Erv14 for the localization of BMV 1a is bypassed by addition of a Sec24-recognizable sorting signal to BMV 1a or by overexpressing Sec24, suggesting a coordinated effort by both Erv14 and Sec24 for the proper localization of BMV 1a. The COPII pathway is well known for being involved in protein secretion; our data suggest that a subset of COPII coat proteins have an unrecognized role in targeting proteins to the perinuclear ER membrane.
[Mh] Termos MeSH primário: Vesículas Revestidas pelo Complexo de Proteína do Envoltório/metabolismo
Núcleo Celular/metabolismo
Retículo Endoplasmático/metabolismo
Proteínas Virais/metabolismo
Replicação Viral/fisiologia
[Mh] Termos MeSH secundário: Bromovirus/fisiologia
Bromovirus/ultraestrutura
Deleção de Genes
Genoma Viral
Proteínas de Fluorescência Verde/metabolismo
Membranas Intracelulares/metabolismo
Proteínas de Membrana/metabolismo
Proteínas de Plantas/metabolismo
Ligação Proteica
RNA Viral
Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/ultraestrutura
Saccharomyces cerevisiae/virologia
Proteínas de Saccharomyces cerevisiae/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Erv14 protein, S cerevisiae); 0 (Membrane Proteins); 0 (Plant Proteins); 0 (RNA, Viral); 0 (Saccharomyces cerevisiae Proteins); 0 (Viral Proteins); 147336-22-9 (Green Fluorescent Proteins)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170731
[Lr] Data última revisão:
170731
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160820
[St] Status:MEDLINE


  7 / 417 MEDLINE  
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[PMID]:27334588
[Au] Autor:Hoover HS; Wang JC; Middleton S; Ni P; Zlotnick A; Vaughan RC; Kao CC
[Ad] Endereço:Department of Molecular & Cellular Biochemistry, Indiana University, Bloomington, Indiana, USA.
[Ti] Título:Phosphorylation of the Brome Mosaic Virus Capsid Regulates the Timing of Viral Infection.
[So] Source:J Virol;90(17):7748-60, 2016 Sep 01.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:UNLABELLED: The four brome mosaic virus (BMV) RNAs (RNA1 to RNA4) are encapsidated in three distinct virions that have different disassembly rates in infection. The mechanism for the differential release of BMV RNAs from virions is unknown, since 180 copies of the same coat protein (CP) encapsidate each of the BMV genomic RNAs. Using mass spectrometry, we found that the BMV CP contains a complex pattern of posttranslational modifications. Treatment with phosphatase was found to not significantly affect the stability of the virions containing RNA1 but significantly impacted the stability of the virions that encapsidated BMV RNA2 and RNA3/4. Cryo-electron microscopy reconstruction revealed dramatic structural changes in the capsid and the encapsidated RNA. A phosphomimetic mutation in the flexible N-terminal arm of the CP increased BMV RNA replication and virion production. The degree of phosphorylation modulated the interaction of CP with the encapsidated RNA and the release of three of the BMV RNAs. UV cross-linking and immunoprecipitation methods coupled to high-throughput sequencing experiments showed that phosphorylation of the BMV CP can impact binding to RNAs in the virions, including sequences that contain regulatory motifs for BMV RNA gene expression and replication. Phosphatase-treated virions affected the timing of CP expression and viral RNA replication in plants. The degree of phosphorylation decreased when the plant hosts were grown at an elevated temperature. These results show that phosphorylation of the capsid modulates BMV infection. IMPORTANCE: How icosahedral viruses regulate the release of viral RNA into the host is not well understood. The selective release of viral RNA can regulate the timing of replication and gene expression. Brome mosaic virus (BMV) is an RNA virus, and its three genomic RNAs are encapsidated in separate virions. Through proteomic, structural, and biochemical analyses, this work shows that posttranslational modifications, specifically, phosphorylation, on the capsid protein regulate the capsid-RNA interaction and the stability of the virions and affect viral gene expression. Mutational analysis confirmed that changes in modification affected virion stability and the timing of viral infection. The mechanism for modification of the virion has striking parallels to the mechanism of regulation of chromatin packaging by nucleosomes.
[Mh] Termos MeSH primário: Bromovirus/fisiologia
Proteínas do Capsídeo/metabolismo
Processamento de Proteína Pós-Traducional
[Mh] Termos MeSH secundário: Bromovirus/ultraestrutura
Proteínas do Capsídeo/química
Microscopia Crioeletrônica
Espectrometria de Massas
Fosforilação
Plantas
Vírion/ultraestrutura
Viroses
Replicação Viral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Capsid Proteins); 0 (coat protein, Brome mosaic virus)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170509
[Lr] Data última revisão:
170509
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160624
[St] Status:MEDLINE
[do] DOI:10.1128/JVI.00833-16


  8 / 417 MEDLINE  
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[PMID]:27244559
[Au] Autor:Smith GR; Xie L; Schwartz R
[Ad] Endereço:Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania, United States of America.
[Ti] Título:Modeling Effects of RNA on Capsid Assembly Pathways via Coarse-Grained Stochastic Simulation.
[So] Source:PLoS One;11(5):e0156547, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The environment of a living cell is vastly different from that of an in vitro reaction system, an issue that presents great challenges to the use of in vitro models, or computer simulations based on them, for understanding biochemistry in vivo. Virus capsids make an excellent model system for such questions because they typically have few distinct components, making them amenable to in vitro and modeling studies, yet their assembly can involve complex networks of possible reactions that cannot be resolved in detail by any current experimental technology. We previously fit kinetic simulation parameters to bulk in vitro assembly data to yield a close match between simulated and real data, and then used the simulations to study features of assembly that cannot be monitored experimentally. The present work seeks to project how assembly in these simulations fit to in vitro data would be altered by computationally adding features of the cellular environment to the system, specifically the presence of nucleic acid about which many capsids assemble. The major challenge of such work is computational: simulating fine-scale assembly pathways on the scale and in the parameter domains of real viruses is far too computationally costly to allow for explicit models of nucleic acid interaction. We bypass that limitation by applying analytical models of nucleic acid effects to adjust kinetic rate parameters learned from in vitro data to see how these adjustments, singly or in combination, might affect fine-scale assembly progress. The resulting simulations exhibit surprising behavioral complexity, with distinct effects often acting synergistically to drive efficient assembly and alter pathways relative to the in vitro model. The work demonstrates how computer simulations can help us understand how assembly might differ between the in vitro and in vivo environments and what features of the cellular environment account for these differences.
[Mh] Termos MeSH primário: Bromovirus/genética
Capsídeo/metabolismo
Vírus da Hepatite B/genética
Papillomaviridae/genética
RNA Viral/metabolismo
Montagem de Vírus/genética
[Mh] Termos MeSH secundário: Proteínas do Capsídeo/metabolismo
Simulação por Computador
Modelos Biológicos
Modelos Moleculares
RNA Viral/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Capsid Proteins); 0 (RNA, Viral)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170718
[Lr] Data última revisão:
170718
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160601
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0156547


  9 / 417 MEDLINE  
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[PMID]:26871111
[Au] Autor:Aggarwal A; May ER; Brooks CL; Klug WS
[Ad] Endereço:Zienkiewicz Centre for Computational Engineering, Swansea University, Swansea SA1 8EN, United Kigdom.
[Ti] Título:Nonuniform elastic properties of macromolecules and effect of prestrain on their continuum nature.
[So] Source:Phys Rev E;93(1):012417, 2016 Jan.
[Is] ISSN:2470-0053
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Many experimental and theoretical methods have been developed to calculate the coarse-grained continuum elastic properties of macromolecules. However, all of those methods assume uniform elastic properties. Following the continuum mechanics framework, we present a systematic way of calculating the nonuniform effective elastic properties from atomic thermal fluctuations obtained from molecular dynamics simulation at any coarse-grained scale using a potential of the mean-force approach. We present the results for a mutant of Sesbania mosaic virus capsid, where we calculate the elastic moduli at different scales and observe an apparent problem with the chosen reference configuration in some cases. We present a possible explanation using an elastic network model, where inducing random prestrain results in a similar behavior. This phenomenon provides a novel insight into the continuum nature of macromolecules and defines the limits on details that the elasticity theory can capture. Further investigation into prestrains could elucidate important aspects of conformational dynamics of macromolecules.
[Mh] Termos MeSH primário: Elasticidade
Simulação de Dinâmica Molecular
[Mh] Termos MeSH secundário: Bromovirus/química
Capsídeo/química
Microscopia de Força Atômica
Conformação Molecular
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.; VALIDATION STUDIES
[Em] Mês de entrada:1608
[Cu] Atualização por classe:160213
[Lr] Data última revisão:
160213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160213
[St] Status:MEDLINE
[do] DOI:10.1103/PhysRevE.93.012417


  10 / 417 MEDLINE  
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[PMID]:26858414
[Au] Autor:Zhang J; Zhang Z; Chukkapalli V; Nchoutmboube JA; Li J; Randall G; Belov GA; Wang X
[Ad] Endereço:Department of Plant Pathology, Physiology, and Weed Science, Virginia Tech, Blacksburg, VA 24061;
[Ti] Título:Positive-strand RNA viruses stimulate host phosphatidylcholine synthesis at viral replication sites.
[So] Source:Proc Natl Acad Sci U S A;113(8):E1064-73, 2016 Feb 23.
[Is] ISSN:1091-6490
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:All positive-strand RNA viruses reorganize host intracellular membranes to assemble their viral replication complexes (VRCs); however, how these viruses modulate host lipid metabolism to accommodate such membrane proliferation and rearrangements is not well defined. We show that a significantly increased phosphatidylcholine (PC) content is associated with brome mosaic virus (BMV) replication in both natural host barley and alternate host yeast based on a lipidomic analysis. Enhanced PC levels are primarily associated with the perinuclear ER membrane, where BMV replication takes place. More specifically, BMV replication protein 1a interacts with and recruits Cho2p (choline requiring 2), a host enzyme involved in PC synthesis, to the site of viral replication. These results suggest that PC synthesized at the site of VRC assembly, not the transport of existing PC, is responsible for the enhanced accumulation. Blocking PC synthesis by deleting the CHO2 gene resulted in VRCs with wider diameters than those in wild-type cells; however, BMV replication was significantly inhibited, highlighting the critical role of PC in VRC formation and viral replication. We further show that enhanced PC levels also accumulate at the replication sites of hepatitis C virus and poliovirus, revealing a conserved feature among a group of positive-strand RNA viruses. Our work also highlights a potential broad-spectrum antiviral strategy that would disrupt PC synthesis at the sites of viral replication but would not alter cellular processes.
[Mh] Termos MeSH primário: Bromovirus/fisiologia
Hordeum/metabolismo
Fosfatidilcolinas/biossíntese
Doenças das Plantas/virologia
Replicação Viral/fisiologia
[Mh] Termos MeSH secundário: Retículo Endoplasmático/genética
Retículo Endoplasmático/metabolismo
Retículo Endoplasmático/virologia
Hordeum/genética
Hordeum/virologia
Membranas Intracelulares/metabolismo
Membranas Intracelulares/virologia
Fosfatidilcolinas/genética
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Phosphatidylcholines)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160210
[St] Status:MEDLINE
[do] DOI:10.1073/pnas.1519730113



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