Base de dados : MEDLINE
Pesquisa : A21 [Categoria DeCS]
Referências encontradas : 27 [refinar]
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  1 / 27 MEDLINE  
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[PMID]:28635587
[Au] Autor:García ML; Bó ED; da Graça JV; Gago-Zachert S; Hammond J; Moreno P; Natsuaki T; Pallás V; Navarro JA; Reyes CA; Luna GR; Sasaya T; Tzanetakis IE; Vaira AM; Verbeek M; Ictv Report Consortium
[Ad] Endereço:1​Instituto de Biotecnología y Biología Molecular, Universidad de La Plata, La Plata, Argentina.
[Ti] Título:ICTV Virus Taxonomy Profile: Ophioviridae.
[So] Source:J Gen Virol;98(6):1161-1162, 2017 Jun.
[Is] ISSN:1465-2099
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The Ophioviridae is a family of filamentous plant viruses, with single-stranded negative, and possibly ambisense, RNA genomes of 11.3-12.5 kb divided into 3-4 segments, each encapsidated separately. Virions are naked filamentous nucleocapsids, forming kinked circles of at least two different contour lengths. The sole genus, Ophiovirus, includes seven species. Four ophioviruses are soil-transmitted and their natural hosts include trees, shrubs, vegetables and bulbous or corm-forming ornamentals, both monocots and dicots. This is a summary of the International Committee on Taxonomy of Viruses (ICTV) Report on the taxonomy of the Ophioviridae, which is available at http://www.ictv.global/report/ophioviridae.
[Mh] Termos MeSH primário: Doenças das Plantas/virologia
Vírus de Plantas/classificação
Vírus de Plantas/genética
Plantas/virologia
Vírus de RNA/classificação
Vírus de RNA/genética
[Mh] Termos MeSH secundário: Vírus de Plantas/isolamento & purificação
Vírus de RNA/isolamento & purificação
Estruturas Virais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171115
[Lr] Data última revisão:
171115
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170622
[St] Status:MEDLINE
[do] DOI:10.1099/jgv.0.000836


  2 / 27 MEDLINE  
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[PMID]:28424284
[Au] Autor:Liu Y; Ishino S; Ishino Y; Pehau-Arnaudet G; Krupovic M; Prangishvili D
[Ad] Endereço:Department of Microbiology, BMGE, Institut Pasteur, Paris, France.
[Ti] Título:A Novel Type of Polyhedral Viruses Infecting Hyperthermophilic Archaea.
[So] Source:J Virol;91(13), 2017 Jul 01.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Encapsidation of genetic material into polyhedral particles is one of the most common structural solutions employed by viruses infecting hosts in all three domains of life. Here, we describe a new virus of hyperthermophilic archaea, polyhedral virus 1 (SPV1), which condenses its circular double-stranded DNA genome in a manner not previously observed for other known viruses. The genome complexed with virion proteins is wound up sinusoidally into a spherical coil which is surrounded by an envelope and further encased by an outer polyhedral capsid apparently composed of the 20-kDa virion protein. Lipids selectively acquired from the pool of host lipids are integral constituents of the virion. None of the major virion proteins of SPV1 show similarity to structural proteins of known viruses. However, minor structural proteins, which are predicted to mediate host recognition, are shared with other hyperthermophilic archaeal viruses infecting members of the order The SPV1 genome consists of 20,222 bp and contains 45 open reading frames, only one-fifth of which could be functionally annotated. Viruses infecting hyperthermophilic archaea display a remarkable morphological diversity, often presenting architectural solutions not employed by known viruses of bacteria and eukaryotes. Here we present the isolation and characterization of polyhedral virus 1, which condenses its genome into a unique spherical coil. Due to the original genomic and architectural features of SPV1, the virus should be considered a representative of a new viral family, "Portogloboviridae."
[Mh] Termos MeSH primário: Vírus de DNA/classificação
Vírus de DNA/isolamento & purificação
Sulfolobus/virologia
Estruturas Virais
[Mh] Termos MeSH secundário: Vírus de DNA/genética
Vírus de DNA/ultraestrutura
Ordem dos Genes
Genoma Viral
Microscopia Eletrônica
Fases de Leitura Aberta
Análise de Sequência de DNA
Homologia de Sequência de Aminoácidos
Proteínas Virais/genética
Vírion/química
Vírion/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Viral Proteins)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170421
[St] Status:MEDLINE


  3 / 27 MEDLINE  
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[PMID]:28077635
[Au] Autor:Spurny R; Pridal A; Pálková L; Kiem HK; de Miranda JR; Plevka P
[Ad] Endereço:Structural Virology, Central European Institute of Technology, Masaryk University, Brno, Czech Republic.
[Ti] Título:Virion Structure of Black Queen Cell Virus, a Common Honeybee Pathogen.
[So] Source:J Virol;91(6), 2017 Mar 15.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Viral diseases are a major threat to honeybee ( ) populations worldwide and therefore an important factor in reliable crop pollination and food security. Black queen cell virus (BQCV) is the etiological agent of a fatal disease of honeybee queen larvae and pupae. The virus belongs to the genus from the family , which is part of the order Here we present a crystal structure of BQCV determined to a resolution of 3.4 Å. The virion is formed by 60 copies of each of the major capsid proteins VP1, VP2, and VP3; however, there is no density corresponding to a 75-residue-long minor capsid protein VP4 encoded by the BQCV genome. We show that the VP4 subunits are present in the crystallized virions that are infectious. This aspect of the BQCV virion is similar to that of the previously characterized triatoma virus and supports the recent establishment of the separate genus within the family The C terminus of VP1 and CD loops of capsid proteins VP1 and VP3 of BQCV form 34-Å-tall finger-like protrusions at the virion surface. The protrusions are larger than those of related dicistroviruses. The western honeybee is the most important pollinator of all, and it is required to sustain the agricultural production and biodiversity of wild flowering plants. However, honeybee populations worldwide are suffering from virus infections that cause colony losses. One of the most common, and least known, honeybee pathogens is black queen cell virus (BQCV), which at high titers causes queen larvae and pupae to turn black and die. Here we present the three-dimensional virion structure of BQCV, determined by X-ray crystallography. The structure of BQCV reveals large protrusions on the virion surface. Capsid protein VP1 of BQCV does not contain a hydrophobic pocket. Therefore, the BQCV virion structure provides evidence that capsid-binding antiviral compounds that can prevent the replication of vertebrate picornaviruses may be ineffective against honeybee virus infections.
[Mh] Termos MeSH primário: Dicistroviridae/ultraestrutura
Vírion/ultraestrutura
[Mh] Termos MeSH secundário: Animais
Abelhas/virologia
Proteínas do Capsídeo/química
Cristalografia por Raios X
Modelos Moleculares
Conformação Proteica
Estruturas Virais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Capsid Proteins)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170518
[Lr] Data última revisão:
170518
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170113
[St] Status:MEDLINE


  4 / 27 MEDLINE  
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[PMID]:27626438
[Au] Autor:Takizawa N; Momose F; Morikawa Y; Nomoto A
[Ad] Endereço:Laboratory of Virology, Institute of Microbial Chemistry (BIKAKEN), 3-14-23 Kamiosaki, Shinagawa-ku, Tokyo 141-0021, Japan. takizawan@bikaken.or.jp.
[Ti] Título:Influenza A Virus Hemagglutinin is Required for the Assembly of Viral Components Including Bundled vRNPs at the Lipid Raft.
[So] Source:Viruses;8(9), 2016 Sep 10.
[Is] ISSN:1999-4915
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:The influenza glycoproteins, hemagglutinin (HA) and neuraminidase (NA), which are associated with the lipid raft, have the potential to initiate virion budding. However, the role of these viral proteins in infectious virion assembly is still unclear. In addition, it is not known how the viral ribonucleoprotein complex (vRNP) is tethered to the budding site. Here, we show that HA is necessary for the efficient progeny virion production and vRNP packaging in the virion. We also found that the level of HA does not affect the bundling of the eight vRNP segments, despite reduced virion production. Detergent solubilization and a subsequent membrane flotation analysis indicated that the accumulation of nucleoprotein, viral polymerases, NA, and matrix protein 1 (M1) in the lipid raft fraction was delayed without HA. Based on our results, we inferred that HA plays a role in the accumulation of viral components, including bundled vRNPs, at the lipid raft.
[Mh] Termos MeSH primário: Glicoproteínas de Hemaglutininação de Vírus da Influenza/metabolismo
Vírus da Influenza A/fisiologia
Microdomínios da Membrana/virologia
Nucleoproteínas/metabolismo
Estruturas Virais/metabolismo
Montagem de Vírus
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Hemagglutinin Glycoproteins, Influenza Virus); 0 (Nucleoproteins)
[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:160915
[St] Status:MEDLINE


  5 / 27 MEDLINE  
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[PMID]:27548201
[Au] Autor:Yin X; Li X; Feng Z
[Ad] Endereço:Center for Vaccines and Immunity, The Research Institute at Nationwide Children's Hospital, Columbus, OH 43205, USA. xin.yin@nationwidechildrens.org.
[Ti] Título:Role of Envelopment in the HEV Life Cycle.
[So] Source:Viruses;8(8), 2016 Aug 18.
[Is] ISSN:1999-4915
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Hepatitis E virus (HEV), an enterically transmitted hepatotropic virus, was thought to be non-enveloped for decades. However, recent studies have revealed that the virus circulating in the patient's blood is completely cloaked in host membranes and resistant to neutralizing antibodies. The discovery of this novel enveloped form of HEV has raised a series of questions about the fundamental biology of HEV and the way this virus, which has been understudied in the past, interacts with its host. Here, we review recent advances towards understanding this phenomenon and discuss its potential impact on various aspects of the HEV life cycle and immunity.
[Mh] Termos MeSH primário: Vírus da Hepatite E/fisiologia
Vírus da Hepatite E/ultraestrutura
Interações Hospedeiro-Patógeno
Estruturas Virais
Montagem de Vírus
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Modelos Biológicos
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[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:160823
[St] Status:MEDLINE


  6 / 27 MEDLINE  
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[PMID]:27384821
[Au] Autor:Silva LR; Souza AM
[Ad] Endereço:Departamento de Ciências Biomédicas, Universidade Salgado de Oliveira, Juiz de Fora, Minas Gerais, Brasil.
[Ti] Título:Zika virus: what do we know about the viral structure, mechanisms of transmission, and neurological outcomes?
[So] Source:Rev Soc Bras Med Trop;49(3):267-73, 2016 May-Jun.
[Is] ISSN:1678-9849
[Cp] País de publicação:Brazil
[La] Idioma:eng
[Ab] Resumo:The Zika virus epidemic that started in Brazil in 2014 has spread to >30 countries and territories in Latin America, leading to a rapid rise in the incidence of microcephalic newborns and adults with neurological complications. At the beginning of the outbreak, little was known about Zika virus morphology, genome structure, modes of transmission, and its potential to cause neurological malformations and disorders. With the advancement of basic science, discoveries of the mechanisms of strain variability, viral transfer to the fetus, and neurovirulence were published. These will certainly lead to the development of strategies to block vertical viral transmission, neuronal invasion, and pathogenesis in the near future. This paper reviews the current literature on Zika virus infections, with the aim of gaining a holistic insight into their etiology and pathogenesis. We discuss Zika virus history and epidemiology in Brazil, viral structure and taxonomy, old and newly identified transmission modes, and neurological consequences of infection.
[Mh] Termos MeSH primário: Doenças do Sistema Nervoso/virologia
Infecção pelo Zika virus
Zika virus
[Mh] Termos MeSH secundário: Adulto
Seres Humanos
Recém-Nascido
Microcefalia/virologia
Doenças do Sistema Nervoso/classificação
Estruturas Virais
Zika virus/fisiologia
Infecção pelo Zika virus/complicações
Infecção pelo Zika virus/transmissão
Infecção pelo Zika virus/virologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170302
[Lr] Data última revisão:
170302
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160708
[St] Status:MEDLINE


  7 / 27 MEDLINE  
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[PMID]:27384649
[Au] Autor:Mullapudi E; Pridal A; Pálková L; de Miranda JR; Plevka P
[Ad] Endereço:Structural Virology, Central European Institute of Technology, Masaryk University, Brno, Czech Republic.
[Ti] Título:Virion Structure of Israeli Acute Bee Paralysis Virus.
[So] Source:J Virol;90(18):8150-9, 2016 Sep 15.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:UNLABELLED: The pollination services provided by the western honeybee (Apis mellifera) are critical for agricultural production and the diversity of wild flowering plants. However, honeybees suffer from environmental pollution, habitat loss, and pathogens, including viruses that can cause fatal diseases. Israeli acute bee paralysis virus (IAPV), from the family Dicistroviridae, has been shown to cause colony collapse disorder in the United States. Here, we present the IAPV virion structure determined to a resolution of 4.0 Å and the structure of a pentamer of capsid protein protomers at a resolution of 2.7 Å. IAPV has major capsid proteins VP1 and VP3 with noncanonical jellyroll ß-barrel folds composed of only seven instead of eight ß-strands, as is the rule for proteins of other viruses with the same fold. The maturation of dicistroviruses is connected to the cleavage of precursor capsid protein VP0 into subunits VP3 and VP4. We show that a putative catalytic site formed by the residues Asp-Asp-Phe of VP1 is optimally positioned to perform the cleavage. Furthermore, unlike many picornaviruses, IAPV does not contain a hydrophobic pocket in capsid protein VP1 that could be targeted by capsid-binding antiviral compounds. IMPORTANCE: Honeybee pollination is required for agricultural production and to sustain the biodiversity of wild flora. However, honeybee populations in Europe and North America are under pressure from pathogens, including viruses that cause colony losses. Viruses from the family Dicistroviridae can cause honeybee infections that are lethal, not only to individual honeybees, but to whole colonies. Here, we present the virion structure of an Aparavirus, Israeli acute bee paralysis virus (IAPV), a member of a complex of closely related viruses that are distributed worldwide. IAPV exhibits unique structural features not observed in other picorna-like viruses. Capsid protein VP1 of IAPV does not contain a hydrophobic pocket, implying that capsid-binding antiviral compounds that can prevent the replication of vertebrate picornaviruses may be ineffective against honeybee virus infections.
[Mh] Termos MeSH primário: Abelhas/virologia
Proteínas do Capsídeo/química
Dicistroviridae/ultraestrutura
Estruturas Virais
Vírion/ultraestrutura
[Mh] Termos MeSH secundário: Animais
Proteínas do Capsídeo/metabolismo
Cristalografia por Raios X
Modelos Moleculares
Conformação Proteica
Multimerização Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Capsid Proteins)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170508
[Lr] Data última revisão:
170508
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160708
[St] Status:MEDLINE
[do] DOI:10.1128/JVI.00854-16


  8 / 27 MEDLINE  
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[PMID]:27279624
[Au] Autor:Mullapudi E; Novácek J; Pálková L; Kulich P; Lindberg AM; van Kuppeveld FJ; Plevka P
[Ad] Endereço:Central European Institute of Technology, Masaryk University, Brno, Czech Republic.
[Ti] Título:Structure and Genome Release Mechanism of the Human Cardiovirus Saffold Virus 3.
[So] Source:J Virol;90(17):7628-39, 2016 Sep 01.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:UNLABELLED: In order to initiate an infection, viruses need to deliver their genomes into cells. This involves uncoating the genome and transporting it to the cytoplasm. The process of genome delivery is not well understood for nonenveloped viruses. We address this gap in our current knowledge by studying the uncoating of the nonenveloped human cardiovirus Saffold virus 3 (SAFV-3) of the family Picornaviridae SAFVs cause diseases ranging from gastrointestinal disorders to meningitis. We present a structure of a native SAFV-3 virion determined to 2.5 Å by X-ray crystallography and an 11-Å-resolution cryo-electron microscopy reconstruction of an "altered" particle that is primed for genome release. The altered particles are expanded relative to the native virus and contain pores in the capsid that might serve as channels for the release of VP4 subunits, N termini of VP1, and the RNA genome. Unlike in the related enteroviruses, pores in SAFV-3 are located roughly between the icosahedral 3- and 5-fold axes at an interface formed by two VP1 and one VP3 subunit. Furthermore, in native conditions many cardioviruses contain a disulfide bond formed by cysteines that are separated by just one residue. The disulfide bond is located in a surface loop of VP3. We determined the structure of the SAFV-3 virion in which the disulfide bonds are reduced. Disruption of the bond had minimal effect on the structure of the loop, but it increased the stability and decreased the infectivity of the virus. Therefore, compounds specifically disrupting or binding to the disulfide bond might limit SAFV infection. IMPORTANCE: A capsid assembled from viral proteins protects the virus genome during transmission from one cell to another. However, when a virus enters a cell the virus genome has to be released from the capsid in order to initiate infection. This process is not well understood for nonenveloped viruses. We address this gap in our current knowledge by studying the genome release of Human Saffold virus 3 Saffold viruses cause diseases ranging from gastrointestinal disorders to meningitis. We show that before the genome is released, the Saffold virus 3 particle expands, and holes form in the previously compact capsid. These holes serve as channels for the release of the genome and small capsid proteins VP4 that in related enteroviruses facilitate subsequent transport of the virus genome into the cell cytoplasm.
[Mh] Termos MeSH primário: Cardiovirus/fisiologia
Cardiovirus/ultraestrutura
Estruturas Virais
Desenvelopamento do Vírus
[Mh] Termos MeSH secundário: Cardiovirus/química
Microscopia Crioeletrônica
Cristalografia por Raios X
Células HeLa
Seres Humanos
Processamento de Imagem Assistida por Computador
[Pt] Tipo de publicação:JOURNAL ARTICLE
[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:160610
[St] Status:MEDLINE
[do] DOI:10.1128/JVI.00746-16


  9 / 27 MEDLINE  
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[PMID]:27279610
[Au] Autor:Kalynych S; Pridal A; Pálková L; Levdansky Y; de Miranda JR; Plevka P
[Ad] Endereço:Structural Virology, Central European Institute of Technology, Masaryk University, Brno, Czech Republic.
[Ti] Título:Virion Structure of Iflavirus Slow Bee Paralysis Virus at 2.6-Angstrom Resolution.
[So] Source:J Virol;90(16):7444-55, 2016 Aug 15.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:UNLABELLED: The western honeybee (Apis mellifera) is the most important commercial insect pollinator. However, bees are under pressure from habitat loss, environmental stress, and pathogens, including viruses that can cause lethal epidemics. Slow bee paralysis virus (SBPV) belongs to the Iflaviridae family of nonenveloped single-stranded RNA viruses. Here we present the structure of the SBPV virion determined from two crystal forms to resolutions of 3.4 Å and 2.6 Å. The overall structure of the virion resembles that of picornaviruses, with the three major capsid proteins VP1 to 3 organized into a pseudo-T3 icosahedral capsid. However, the SBPV capsid protein VP3 contains a C-terminal globular domain that has not been observed in other viruses from the order Picornavirales The protruding (P) domains form "crowns" on the virion surface around each 5-fold axis in one of the crystal forms. However, the P domains are shifted 36 Å toward the 3-fold axis in the other crystal form. Furthermore, the P domain contains the Ser-His-Asp triad within a surface patch of eight conserved residues that constitutes a putative catalytic or receptor-binding site. The movements of the domain might be required for efficient substrate cleavage or receptor binding during virus cell entry. In addition, capsid protein VP2 contains an RGD sequence that is exposed on the virion surface, indicating that integrins might be cellular receptors of SBPV. IMPORTANCE: Pollination by honeybees is needed to sustain agricultural productivity as well as the biodiversity of wild flora. However, honeybee populations in Europe and North America have been declining since the 1950s. Honeybee viruses from the Iflaviridae family are among the major causes of honeybee colony mortality. We determined the virion structure of an Iflavirus, slow bee paralysis virus (SBPV). SBPV exhibits unique structural features not observed in other picorna-like viruses. The SBPV capsid protein VP3 has a large C-terminal domain, five of which form highly prominent protruding "crowns" on the virion surface. However, the domains can change their positions depending on the conditions of the environment. The domain includes a putative catalytic or receptor binding site that might be important for SBPV cell entry.
[Mh] Termos MeSH primário: Vírus de RNA/ultraestrutura
Estruturas Virais
Vírion/ultraestrutura
[Mh] Termos MeSH secundário: Animais
Abelhas/virologia
Capsídeo/ultraestrutura
Cristalografia por Raios X
Modelos Moleculares
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170508
[Lr] Data última revisão:
170508
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160610
[St] Status:MEDLINE
[do] DOI:10.1128/JVI.00680-16


  10 / 27 MEDLINE  
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[PMID]:26874013
[Au] Autor:Bergua M; Phelan DM; Bak A; Bloom DC; Folimonova SY
[Ad] Endereço:University of Florida, Department of Plant Pathology, Gainesville, FL 32611, USA.
[Ti] Título:Simultaneous visualization of two Citrus tristeza virus genotypes provides new insights into the structure of multi-component virus populations in a host.
[So] Source:Virology;491:10-9, 2016 Apr.
[Is] ISSN:1096-0341
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Complex Citrus tristeza virus (CTV) populations composed of mixtures of different strains of the virus are commonly found in citrus trees in the field. At present, little is known about how these populations are formed, maintained, and how they are structured within a host. Here we used a novel in situ hybridization approach allowing simultaneous visualization of two different RNA targets with high sensitivity and specificity to examine the distribution of two isolates, T36 and T68-1, representing phylogenetically distinct strains of CTV, in a citrus host in single and mixed infections. Remarkably, in doubly inoculated plants the two virus variants appeared to be well mixed within the infected tissue and showed no spatial segregation. In addition, both CTV variants were often found occupying the same cells. Possible mechanisms involved in shaping CTV populations and the biological significance of the observed lack of structural separation of the individual components are discussed.
[Mh] Termos MeSH primário: Citrus/virologia
Closterovirus/isolamento & purificação
Hibridização In Situ/métodos
Doenças das Plantas/virologia
[Mh] Termos MeSH secundário: Closterovirus/classificação
Closterovirus/genética
Variação Genética
Genótipo
Filogenia
RNA Viral/genética
Estruturas Virais/classificação
Estruturas Virais/genética
Estruturas Virais/isolamento & purificação
[Pt] Tipo de publicação:EVALUATION STUDIES; JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (RNA, Viral)
[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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