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  1 / 177 MEDLINE  
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[PMID]:28880890
[Au] Autor:Eichwald C; Kim J; Nibert ML
[Ad] Endereço:Department of Microbiology & Immunobiology, Harvard Medical School, Boston, Massachusetts, United States of America.
[Ti] Título:Dissection of mammalian orthoreovirus µ2 reveals a self-associative domain required for binding to microtubules but not to factory matrix protein µNS.
[So] Source:PLoS One;12(9):e0184356, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mammalian orthoreovirus protein µ2 is a component of the viral core particle. Its activities include RNA binding and hydrolysis of the γ-phosphate from NTPs and RNA 5´-termini, suggesting roles as a cofactor for the viral RNA-dependent RNA polymerase, λ3, first enzyme in 5´-capping of viral plus-strand RNAs, and/or prohibitory of RNA-5´-triphosphate-activated antiviral signaling. Within infected cells, µ2 also contributes to viral factories, cytoplasmic structures in which genome replication and particle assembly occur. By associating with both microtubules (MTs) and viral factory matrix protein µNS, µ2 can anchor the factories to MTs, the full effects of which remain unknown. In this study, a protease-hypersensitive region allowed µ2 to be dissected into two large fragments corresponding to residues 1-282 and 283-736. Fusions with enhanced green fluorescent protein revealed that these amino- and carboxyl-terminal regions of µ2 associate in cells with either MTs or µNS, respectively. More exhaustive deletion analysis defined µ2 residues 1-325 as the minimal contiguous region that associates with MTs in the absence of the self-associating tag. A region involved in µ2 self-association was mapped to residues 283-325, and self-association involving this region was essential for MT-association as well. Likewise, we mapped that µNS-binding site in µ2 relates to residues 290-453 which is independent of µ2 self-association. These findings suggest that µ2 monomers or oligomers can bind to MTs and µNS, but that self-association involving µ2 residues 283-325 is specifically relevant for MT-association during viral factories formation.
[Mh] Termos MeSH primário: Microtúbulos/metabolismo
Orthoreovirus de Mamíferos/metabolismo
Proteínas não Estruturais Virais/metabolismo
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Cercopithecus aethiops
Citoplasma/metabolismo
Microscopia de Fluorescência
Ligação Proteica
RNA Viral/metabolismo
Proteínas do Core Viral/metabolismo
Replicação Viral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Viral); 0 (Viral Core Proteins); 0 (Viral Nonstructural Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170908
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184356


  2 / 177 MEDLINE  
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[PMID]:28878073
[Au] Autor:Bussiere LD; Choudhury P; Bellaire B; Miller CL
[Ad] Endereço:Department of Veterinary Microbiology and Preventive Medicine, College of Veterinary Medicine, Iowa State University, Ames, Iowa, USA.
[Ti] Título:Characterization of a Replicating Mammalian Orthoreovirus with Tetracysteine-Tagged µNS for Live-Cell Visualization of Viral Factories.
[So] Source:J Virol;91(22), 2017 Nov 15.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Within infected host cells, mammalian orthoreovirus (MRV) forms viral factories (VFs), which are sites of viral transcription, translation, assembly, and replication. The MRV nonstructural protein µNS comprises the structural matrix of VFs and is involved in recruiting other viral proteins to VF structures. Previous attempts have been made to visualize VF dynamics in live cells, but due to current limitations in recovery of replicating reoviruses carrying large fluorescent protein tags, researchers have been unable to directly assess VF dynamics from virus-produced µNS. We set out to develop a method to overcome this obstacle by utilizing the 6-amino-acid (CCPGCC) tetracysteine (TC) tag and FlAsH-EDT2 reagent. The TC tag was introduced into eight sites throughout µNS, and the capacity of the TC-µNS fusion proteins to form virus factory-like (VFL) structures and colocalize with virus proteins was characterized. Insertion of the TC tag interfered with recombinant virus rescue in six of the eight mutants, likely as a result of loss of VF formation or important virus protein interactions. However, two recombinant (r)TC-µNS viruses were rescued and VF formation, colocalization with associating virus proteins, and characterization of virus replication were subsequently examined. Furthermore, the rTC-µNS viruses were utilized to infect cells and examine VF dynamics using live-cell microscopy. These experiments demonstrate active VF movement with fusion events as well as transient interactions between individual VFs and demonstrate the importance of microtubule stability for VF fusion during MRV infection. This work provides important groundwork for future in-depth studies of VF dynamics and host cell interactions. MRV has historically been used as a model to study the double-stranded RNA (dsRNA) family, the members of which infect and cause disease in humans, animals, and plants. During infection, MRV forms VFs that play a critical role in virus infection but remain to be fully characterized. To study VFs, researchers have focused on visualizing the nonstructural protein µNS, which forms the VF matrix. This work provides the first evidence of recovery of replicating reoviruses in which VFs can be labeled in live cells via introduction of a TC tag into the µNS open reading frame. Characterization of each recombinant reovirus sheds light on µNS interactions with viral proteins. Moreover, utilizing the TC-labeling FlAsH-EDT2 biarsenical reagent to visualize VFs, evidence is provided of dynamic VF movement and interactions at least partially dependent on intact microtubules.
[Mh] Termos MeSH primário: Proteínas do Capsídeo/metabolismo
Exossomos/virologia
Orthoreovirus de Mamíferos/fisiologia
RNA Viral/metabolismo
Replicação Viral/fisiologia
[Mh] Termos MeSH secundário: Anticorpos Monoclonais Murinos/química
Anticorpos Antivirais/química
Proteínas do Capsídeo/genética
Linhagem Celular
Exossomos/genética
Exossomos/metabolismo
Seres Humanos
RNA Viral/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Monoclonal, Murine-Derived); 0 (Antibodies, Viral); 0 (Capsid Proteins); 0 (RNA, Viral)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170908
[St] Status:MEDLINE


  3 / 177 MEDLINE  
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[PMID]:28407327
[Au] Autor:Rahal A; Musher B
[Ad] Endereço:Division of Hematology-Oncology, Department of Medicine, Baylor College of Medicine, Houston, Texas.
[Ti] Título:Oncolytic viral therapy for pancreatic cancer.
[So] Source:J Surg Oncol;116(1):94-103, 2017 Jul.
[Is] ISSN:1096-9098
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Outcomes of pancreatic adenocarcinoma (PDA) remain dismal despite extensive clinical investigation. Combination chemotherapy provides modest improvements in survival above best supportive care, and immunotherapy has thus far not proven effective. Nevertheless, growing insight into antitumor immunity and the tumor microenvironment has inspired the discovery of novel agents targeting PDA. Oncolytic viruses represent an emerging class of immunotherapeutic agents that have undergone extensive preclinical investigation and warrant further investigation in well-designed clinical trials.
[Mh] Termos MeSH primário: Terapia Viral Oncolítica
Neoplasias Pancreáticas/terapia
[Mh] Termos MeSH secundário: Adenocarcinoma/imunologia
Adenocarcinoma/terapia
Adenoviridae
Animais
Ensaios Clínicos como Assunto
Seres Humanos
Vírus do Sarampo
Myxoma virus
Orthoreovirus de Mamíferos
Neoplasias Pancreáticas/imunologia
Parvovirus
Simplexvirus
Microambiente Tumoral
Vírus Vaccinia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[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:170414
[St] Status:MEDLINE
[do] DOI:10.1002/jso.24626


  4 / 177 MEDLINE  
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[PMID]:28298603
[Au] Autor:Eaton HE; Kobayashi T; Dermody TS; Johnston RN; Jais PH; Shmulevitz M
[Ad] Endereço:Department of Medical Microbiology and Immunology, Li Ka Shing Institute of Virology, University of Alberta, Edmonton, Alberta, Canada.
[Ti] Título:African Swine Fever Virus NP868R Capping Enzyme Promotes Reovirus Rescue during Reverse Genetics by Promoting Reovirus Protein Expression, Virion Assembly, and RNA Incorporation into Infectious Virions.
[So] Source:J Virol;91(11), 2017 Jun 01.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Reoviruses, like many eukaryotic viruses, contain an inverted 7-methylguanosine (m7G) cap linked to the 5' nucleotide of mRNA. The traditional functions of capping are to promote mRNA stability, protein translation, and concealment from cellular proteins that recognize foreign RNA. To address the role of mRNA capping during reovirus replication, we assessed the benefits of adding the African swine fever virus NP868R capping enzyme during reovirus rescue. C3P3, a fusion protein containing T7 RNA polymerase and NP868R, was found to increase protein expression 5- to 10-fold compared to T7 RNA polymerase alone while enhancing reovirus rescue from the current reverse genetics system by 100-fold. Surprisingly, RNA stability was not increased by C3P3, suggesting a direct effect on protein translation. A time course analysis revealed that C3P3 increased protein synthesis within the first 2 days of a reverse genetics transfection. This analysis also revealed that C3P3 enhanced processing of outer capsid µ1 protein to µ1C, a previously described hallmark of reovirus assembly. Finally, to determine the rate of infectious-RNA incorporation into new virions, we developed a new recombinant reovirus S1 gene that expressed the fluorescent protein UnaG. Following transfection of cells with UnaG and infection with wild-type virus, passage of UnaG through progeny was significantly enhanced by C3P3. These data suggest that capping provides nontraditional functions to reovirus, such as promoting assembly and infectious-RNA incorporation. Our findings expand our understanding of how viruses utilize capping, suggesting that capping provides nontraditional functions to reovirus, such as promoting assembly and infectious-RNA incorporation, in addition to enhancing protein translation. Beyond providing mechanistic insight into reovirus replication, our findings also show that reovirus reverse genetics rescue is enhanced 100-fold by the NP868R capping enzyme. Since reovirus shows promise as a cancer therapy, efficient reovirus reverse genetics rescue will accelerate production of recombinant reoviruses as candidates to enhance therapeutic potency. NP868R-assisted reovirus rescue will also expedite production of recombinant reovirus for mechanistic insights into reovirus protein function and structure.
[Mh] Termos MeSH primário: Vírus da Febre Suína Africana/enzimologia
Nucleotidiltransferases/metabolismo
Orthoreovirus de Mamíferos/genética
Orthoreovirus de Mamíferos/fisiologia
RNA Viral/metabolismo
Vírion/fisiologia
Montagem de Vírus
[Mh] Termos MeSH secundário: Vírus da Febre Suína Africana/genética
Linhagem Celular
Proteínas Recombinantes de Fusão/metabolismo
Genética Reversa
Vírion/genética
Replicação Viral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Viral); 0 (Recombinant Fusion Proteins); EC 2.7.7.- (Nucleotidyltransferases); EC 2.7.7.50 (mRNA guanylyltransferase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171112
[Lr] Data última revisão:
171112
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170317
[St] Status:MEDLINE


  5 / 177 MEDLINE  
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[PMID]:28077658
[Au] Autor:Rivera-Serrano EE; Fritch EJ; Scholl EH; Sherry B
[Ad] Endereço:Department of Molecular Biomedical Sciences, College of Veterinary Medicine, North Carolina State University, Raleigh, North Carolina, USA.
[Ti] Título:A Cytoplasmic RNA Virus Alters the Function of the Cell Splicing Protein SRSF2.
[So] Source:J Virol;91(7), 2017 Apr 01.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:To replicate efficiently, viruses must create favorable cell conditions and overcome cell antiviral responses. We previously reported that the reovirus protein µ2 from strain T1L, but not strain T3D, represses one antiviral response: alpha/beta interferon signaling. We report here that T1L, but not T3D, µ2 localizes to nuclear speckles, where it forms a complex with the mRNA splicing factor SRSF2 and alters its subnuclear localization. Reovirus replicates in cytoplasmic viral factories, and there is no evidence that reovirus genomic or messenger RNAs are spliced, suggesting that T1L µ2 might target splicing of cell RNAs. Indeed, RNA sequencing revealed that reovirus T1L, but not T3D, infection alters the splicing of transcripts for host genes involved in mRNA posttranscriptional modifications. Moreover, depletion of SRSF2 enhanced reovirus replication and cytopathic effect, suggesting that T1L µ2 modulation of splicing benefits the virus. This provides the first report of viral antagonism of the splicing factor SRSF2 and identifies the viral protein that determines strain-specific differences in cell RNA splicing. Efficient viral replication requires that the virus create favorable cell conditions. Many viruses accomplish this by repressing specific antiviral responses. We demonstrate here that some mammalian reoviruses, RNA viruses that replicate strictly in the cytoplasm, express a protein variant that localizes to nuclear speckles, where it targets a cell mRNA splicing factor. Infection with a reovirus strain that targets this splicing factor alters splicing of cell mRNAs involved in the maturation of many other cell mRNAs. Depletion of this cell splicing factor enhances reovirus replication and cytopathic effect. Our results provide the first evidence of viral antagonism of this splicing factor and suggest that downstream consequences to the cell are global and benefit the virus.
[Mh] Termos MeSH primário: Orthoreovirus de Mamíferos/fisiologia
Fatores de Processamento de Serina-Arginina/fisiologia
Proteínas Virais/metabolismo
Replicação Viral
[Mh] Termos MeSH secundário: Transporte Ativo do Núcleo Celular
Sequência de Aminoácidos
Animais
Núcleo Celular/virologia
Citoplasma/virologia
Células HEK293
Seres Humanos
Camundongos
Microtúbulos/metabolismo
Ligação Proteica
Multimerização Proteica
Processamento de RNA
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Messenger); 0 (Sfrs2 protein, mouse); 0 (Viral Proteins); 0 (mu2 protein, Reovirus); 170974-22-8 (Serine-Arginine Splicing Factors)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170913
[Lr] Data última revisão:
170913
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170113
[St] Status:MEDLINE


  6 / 177 MEDLINE  
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[PMID]:28077655
[Au] Autor:Baldridge MT; Lee S; Brown JJ; McAllister N; Urbanek K; Dermody TS; Nice TJ; Virgin HW
[Ad] Endereço:Department of Pathology and Immunology, Washington University School of Medicine, St. Louis, Missouri, USA.
[Ti] Título:Expression of on Intestinal Epithelial Cells Is Critical to the Antiviral Effects of Interferon Lambda against Norovirus and Reovirus.
[So] Source:J Virol;91(7), 2017 Apr 01.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lambda interferon (IFN-λ) has potent antiviral effects against multiple enteric viral pathogens, including norovirus and rotavirus, in both preventing and curing infection. Because the intestine includes a diverse array of cell types, however, the cell(s) upon which IFN-λ acts to exert its antiviral effects is unclear. Here, we sought to identify IFN-λ-responsive cells by generation of mice with lineage-specific deletion of the receptor for IFN-λ, We found that expression of IFNLR1 on intestinal epithelial cells (IECs) in the small intestine and colon is required for enteric IFN-λ antiviral activity. IEC expression also determines the efficacy of IFN-λ in resolving persistent murine norovirus (MNoV) infection and regulates fecal shedding and viral titers in tissue. Thus, the expression of by IECs is necessary for the response to both endogenous and exogenous IFN-λ. We further demonstrate that IEC expression is required for the sterilizing innate immune effects of IFN-λ by extending these findings in -deficient mice. Finally, we assessed whether our findings pertained to multiple viral pathogens by infecting mice specifically lacking IEC expression with reovirus. These mice phenocopied -null animals, exhibiting increased intestinal tissue titers and enhanced reovirus fecal shedding. Thus, IECs are the critical cell type responding to IFN-λ to control multiple enteric viruses. This is the first genetic evidence that supports an essential role for IECs in IFN-λ-mediated control of enteric viral infection, and these findings provide insight into the mechanism of IFN-λ-mediated antiviral activity. Human noroviruses (HNoVs) are the leading cause of epidemic gastroenteritis worldwide. Type III interferons (IFN-λ) control enteric viral infections in the gut and have been shown to cure mouse norovirus, a small-animal model for HNoVs. Using a genetic approach with conditional knockout mice, we identified IECs as the dominant IFN-λ-responsive cells in control of enteric virus infection Upon murine norovirus or reovirus infection, depletion in IECs largely recapitulated the phenotype seen in mice of higher intestinal tissue viral titers and increased viral shedding in the stool. Moreover, IFN-λ-mediated sterilizing immunity against murine norovirus requires the capacity of IECs to respond to IFN-λ. These findings clarify the mechanism of action of this cytokine and emphasize the therapeutic potential of IFN-λ for treating mucosal viral infections.
[Mh] Termos MeSH primário: Células Epiteliais/metabolismo
Norovirus/fisiologia
Orthoreovirus de Mamíferos/fisiologia
Receptores de Interferon/metabolismo
[Mh] Termos MeSH secundário: Animais
Infecções por Caliciviridae/imunologia
Infecções por Caliciviridae/metabolismo
Infecções por Caliciviridae/virologia
Linhagem Celular
Células Epiteliais/imunologia
Células Epiteliais/virologia
Imunidade Inata
Mucosa Intestinal/imunologia
Mucosa Intestinal/metabolismo
Intestino Grosso/imunologia
Intestino Grosso/metabolismo
Intestino Grosso/virologia
Intestino Delgado/imunologia
Intestino Delgado/metabolismo
Intestino Delgado/virologia
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Especificidade de Órgãos
Infecções por Reoviridae/imunologia
Infecções por Reoviridae/metabolismo
Infecções por Reoviridae/virologia
Eliminação de Partículas Virais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (IFNLR1 protein, mouse); 0 (Receptors, Interferon)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170914
[Lr] Data última revisão:
170914
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170113
[St] Status:MEDLINE


  7 / 177 MEDLINE  
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[PMID]:27806369
[Au] Autor:Portales-Cervantes L; Haidl ID; Lee PW; Marshall JS
[Ad] Endereço:Department of Microbiology and Immunology, Dalhousie University, Halifax, N.S., Canada.
[Ti] Título:Virus-Infected Human Mast Cells Enhance Natural Killer Cell Functions.
[So] Source:J Innate Immun;9(1):94-108, 2017.
[Is] ISSN:1662-8128
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Mucosal surfaces are protected from infection by both structural and sentinel cells, such as mast cells. The mast cell's role in antiviral responses is poorly understood; however, they selectively recruit natural killer (NK) cells following infection. Here, the ability of virus-infected mast cells to enhance NK cell functions was examined. Cord blood-derived human mast cells infected with reovirus (Reo-CBMC) and subsequent mast cell products were used for the stimulation of human NK cells. NK cells upregulated the CD69 molecule and cytotoxicity-related genes, and demonstrated increased cytotoxic activity in response to Reo-CBMC soluble products. NK cell interferon (IFN)-γ production was also promoted in the presence of interleukin (IL)-18. In vivo, SCID mice injected with Reo-CBMC in a subcutaneous Matrigel model, could recruit and activate murine NK cells, a property not shared by normal human fibroblasts. Soluble products of Reo-CBMC included IL-10, TNF, type I and type III IFNs. Blockade of the type I IFN receptor abrogated NK cell activation. Furthermore, reovirus-infected mast cells expressed multiple IFN-α subtypes not observed in reovirus-infected fibroblasts or epithelial cells. Our data define an important mast cell IFN response, not shared by structural cells, and a subsequent novel mast cell-NK cell immune axis in human antiviral host defense.
[Mh] Termos MeSH primário: Imunidade nas Mucosas
Células Matadoras Naturais/imunologia
Mastócitos/imunologia
Orthoreovirus de Mamíferos/imunologia
Infecções por Reoviridae/imunologia
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Citotoxicidade Imunológica
Sangue Fetal/citologia
Seres Humanos
Interferons/metabolismo
Interleucina-18/metabolismo
Mastócitos/transplante
Mastócitos/virologia
Camundongos
Camundongos SCID
Especificidade de Órgãos
Comunicação Parácrina
Receptor de Interferon alfa e beta/antagonistas & inibidores
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Interleukin-18); 156986-95-7 (Receptor, Interferon alpha-beta); 9008-11-1 (Interferons)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161103
[St] Status:MEDLINE
[do] DOI:10.1159/000450576


  8 / 177 MEDLINE  
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[PMID]:27681135
[Au] Autor:Thete D; Snyder AJ; Mainou BA; Danthi P
[Ad] Endereço:Department of Biology, Indiana University, Bloomington, Indiana, USA.
[Ti] Título:Reovirus µ1 Protein Affects Infectivity by Altering Virus-Receptor Interactions.
[So] Source:J Virol;90(23):10951-10962, 2016 Dec 01.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Proteins that form the reovirus outer capsid play an active role in the entry of reovirus into host cells. Among these, the σ1 protein mediates attachment of reovirus particles to host cells via interaction with cell surface glycans or the proteinaceous receptor junctional adhesion molecule A (JAM-A). The µ1 protein functions to penetrate the host cell membrane to allow delivery of the genome-containing viral core particle into the cytoplasm to initiate viral replication. We demonstrate that a reassortant virus that expresses the M2 gene-encoded µ1 protein derived from prototype strain T3D in an otherwise prototype T1L background (T1L/T3DM2) infects cells more efficiently than parental T1L. Unexpectedly, the enhancement in infectivity of T1L/T3DM2 is due to its capacity to attach to cells more efficiently. We present genetic data implicating the central region of µ1 in altering the cell attachment property of reovirus. Our data indicate that the T3D µ1-mediated enhancement in infectivity of T1L is dependent on the function of σ1 and requires the expression of JAM-A. We also demonstrate that T1L/T3DM2 utilizes JAM-A more efficiently than T1L. These studies revealed a previously unknown relationship between two nonadjacent reovirus outer capsid proteins, σ1 and µ1. IMPORTANCE: How reovirus attaches to host cells has been extensively characterized. Attachment of reovirus to host cells is mediated by the σ1 protein, and properties of σ1 influence the capacity of reovirus to target specific host tissues and produce disease. Here, we present new evidence indicating that the cell attachment properties of σ1 are influenced by the nature of µ1, a capsid protein that does not physically interact with σ1. These studies could explain the previously described role for µ1 in influencing reovirus pathogenesis. These studies are also of broader significance because they highlight an example of how genetic reassortment between virus strains could produce phenotypes that are distinct from those of either parent.
[Mh] Termos MeSH primário: Proteínas do Capsídeo/fisiologia
Orthoreovirus Mamífero 3/fisiologia
Orthoreovirus Mamífero 3/patogenicidade
[Mh] Termos MeSH secundário: Animais
Proteínas do Capsídeo/genética
Moléculas de Adesão Celular/fisiologia
Linhagem Celular
Interações Hospedeiro-Patógeno/genética
Interações Hospedeiro-Patógeno/fisiologia
Orthoreovirus Mamífero 3/genética
Camundongos
Orthoreovirus de Mamíferos/genética
Orthoreovirus de Mamíferos/patogenicidade
Orthoreovirus de Mamíferos/fisiologia
Receptores de Superfície Celular/fisiologia
Receptores Virais/fisiologia
Infecções por Reoviridae/etiologia
Infecções por Reoviridae/virologia
Virulência/genética
Virulência/fisiologia
Ligação Viral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Capsid Proteins); 0 (Cell Adhesion Molecules); 0 (F11r protein, mouse); 0 (Receptors, Cell Surface); 0 (Receptors, Virus); 0 (mu1 protein, Reovirus); 0 (reovirus type 3 receptor); 0 (sigma 1 protein, reovirus)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170515
[Lr] Data última revisão:
170515
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160930
[St] Status:MEDLINE


  9 / 177 MEDLINE  
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[PMID]:27279006
[Au] Autor:Stanifer ML; Rippert A; Kazakov A; Willemsen J; Bucher D; Bender S; Bartenschlager R; Binder M; Boulant S
[Ad] Endereço:Schaller research group at CellNetworks, Department of Infectious Diseases, Virology, Heidelberg University, Germany.
[Ti] Título:Reovirus intermediate subviral particles constitute a strategy to infect intestinal epithelial cells by exploiting TGF-ß dependent pro-survival signaling.
[So] Source:Cell Microbiol;18(12):1831-1845, 2016 Dec.
[Is] ISSN:1462-5822
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Intestinal epithelial cells (IECs) constitute the primary barrier that separates us from the outside environment. These cells, lining the surface of the intestinal tract, represent a major challenge that enteric pathogens have to face. How IECs respond to viral infection and whether enteric viruses have developed strategies to subvert IECs innate immune response remains poorly characterized. Using mammalian reovirus (MRV) as a model enteric virus, we found that the intermediate subviral particles (ISVPs), which are formed in the gut during the natural course of infection by proteolytic digestion of the reovirus virion, trigger reduced innate antiviral immune response in IECs. On the contrary, infection of IECs by virions induces a strong antiviral immune response that leads to cellular death. Additionally, we determined that virions can be sensed by both TLR and RLR pathways while ISVPs are sensed by RLR pathways only. Interestingly, we found that ISVP infected cells secrete TGF-ß acting as a pro-survival factor that protects IECs against virion induced cellular death. We propose that ISVPs represent a reovirus strategy to initiate primary infection of the gut by subverting IECs innate immune system and by counteracting cellular-death pathways.
[Mh] Termos MeSH primário: Colo/imunologia
Células Epiteliais/imunologia
Interações Hospedeiro-Patógeno
Orthoreovirus de Mamíferos/imunologia
Fator de Crescimento Transformador beta/imunologia
Vírion/imunologia
[Mh] Termos MeSH secundário: Morte Celular
Colo/virologia
Células Epiteliais/virologia
Regulação da Expressão Gênica
Hepatócitos/imunologia
Hepatócitos/virologia
Seres Humanos
Interleucina-6/genética
Interleucina-6/imunologia
Interleucina-8/genética
Interleucina-8/imunologia
Orthoreovirus de Mamíferos/crescimento & desenvolvimento
Transdução de Sinais
Fator de Crescimento Transformador beta/genética
Vírion/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (IL6 protein, human); 0 (Interleukin-6); 0 (Interleukin-8); 0 (Transforming Growth Factor beta)
[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:160610
[St] Status:MEDLINE
[do] DOI:10.1111/cmi.12626


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[PMID]:27259366
[Au] Autor:Li Z; Liu D; Ran X; Liu C; Guo D; Hu X; Tian J; Zhang X; Shao Y; Liu S; Qu L
[Ad] Endereço:State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin 150001, China.
[Ti] Título:Characterization and pathogenicity of a novel mammalian orthoreovirus from wild short-nosed fruit bats.
[So] Source:Infect Genet Evol;43:347-53, 2016 09.
[Is] ISSN:1567-7257
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Mammalian orthoreoviruses (MRVs) have a wide range of geographic distribution and have been isolated from humans and various animals. This study describes the isolation, molecular characterization and analysis of pathogenicity of MRV variant B/03 from wild short-nosed fruit bats. Negative stain electron microscopy illustrated that the B/03 strain is a non-enveloped icosahedral virus with a diameter of 70nm. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) migration patterns showed that the B/03 viral genome contains 10 segments in a 3:3:4 arrangement. The isolate belongs to MRV serotype 1 based on S1 gene nucleotide sequence data. BALB/c mice experimentally infected with B/03 virus by intranasal inoculation developed severe respiratory distress with tissue damage and inflammation. Lastly, B/03 virus has an increased transmission risk between bats and humans or animals.
[Mh] Termos MeSH primário: Quirópteros/virologia
Genoma Viral
Orthoreovirus de Mamíferos/genética
Orthoreovirus de Mamíferos/patogenicidade
Filogenia
Infecções por Reoviridae/epidemiologia
[Mh] Termos MeSH secundário: Animais
China/epidemiologia
Feminino
Seres Humanos
Camundongos
Camundongos Endogâmicos BALB C
Orthoreovirus de Mamíferos/classificação
Orthoreovirus de Mamíferos/ultraestrutura
Tamanho da Partícula
Pneumonia Viral/mortalidade
Pneumonia Viral/patologia
Pneumonia Viral/virologia
Infecções por Reoviridae/patologia
Infecções por Reoviridae/transmissão
Infecções por Reoviridae/virologia
Análise de Sequência de DNA
Análise de Sobrevida
Vírion/patogenicidade
Vírion/ultraestrutura
Virulência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171122
[Lr] Data última revisão:
171122
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160605
[St] Status:MEDLINE



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