Subcellular distribution of swine vesicular disease virus proteins and alterations induced in infected cells: A comparative study with foot-and-mouth disease virus and vesicular stomatitis virus

Martin-Acebes, Miguel A; Gonzalez-Magaldi, Monica; Rosas, Maria F; Borrego, Belen; Brocchi, Emiliana; Armas-Portela, Rosario; Sobrino, Francisco

doi:10.1016/j.virol.2007.12.042

Title: Subcellular distribution of swine vesicular disease virus proteins and alterations induced in infected cells: A comparative study with foot-and-mouth disease virus and vesicular stomatitis virus

Full Record
Other Related Research

Abstract

The intracellular distribution of swine vesicular disease virus (SVDV) proteins and the induced reorganization of endomembranes in IBRS-2 cells were analyzed. Fluorescence to new SVDV capsids appeared first upon infection, concentrated in perinuclear circular structures and colocalized to dsRNA. As in foot-and-mouth disease virus (FMDV)-infected cells, a vesicular pattern was predominantly found in later stages of SVDV capsid morphogenesis that colocalized with those of non-structural proteins 2C, 2BC and 3A. These results suggest that assembly of capsid proteins is associated to the replication complex. Confocal microscopy showed a decreased fluorescence to ER markers (calreticulin and protein disulfide isomerase), and disorganization of cis-Golgi gp74 and trans-Golgi caveolin-1 markers in SVDV- and FMDV-, but not in vesicular stomatitis virus (VSV)-infected cells. Electron microscopy of SVDV-infected cells at an early stage of infection revealed fragmented ER cisternae with expanded lumen and accumulation of large Golgi vesicles, suggesting alterations of vesicle traffic through Golgi compartments. At this early stage, FMDV induced different patterns of ER fragmentation and Golgi alterations. At later stages of SVDV cytopathology, cells showed a completely vacuolated cytoplasm containing vesicles of different sizes. Cell treatment with brefeldin A, which disrupts the Golgi complex, reduced SVDV ({approx} 5 log) and VSV ({approx}more »« less

Authors:

Martin-Acebes, Miguel A; Gonzalez-Magaldi, Monica; Rosas, Maria F ^[1]; Borrego, Belen ^[2]; Brocchi, Emiliana ^[3]; Armas-Portela, Rosario ^[1]; Sobrino, Francisco ^[1]

Centro de Biologia Molecular 'Severo Ochoa' (CSIC-UAM), Cantoblanco 28049, Madrid (Spain)
Centro de Investigacion en Sanidad Animal, INIA, Valdeolmos, 28130 Madrid (Spain)
Istituto Zooprofilattico Sperimentale della Lombardia e dell'Emilia Romagna (IZSLER), 25124 Brescia (Italy)

Publication Date:: Sat May 10 00:00:00 EDT 2008

OSTI Identifier:: 21140983

Resource Type:: Journal Article

Journal Name:: Virology

Additional Journal Information:: Journal Volume: 374; Journal Issue: 2; Other Information: DOI: 10.1016/j.virol.2007.12.042; PII: S0042-6822(08)00008-1; Copyright (c) 2008 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0042-6822

Country of Publication:: United States

Language:: English

Subject:: 60 APPLIED LIFE SCIENCES; CYTOPLASM; DISULFIDES; ELECTRON MICROSCOPY; FLUORESCENCE; GOLGI COMPLEXES; MORPHOGENESIS; ORAL CAVITY; PROTEINS; SUBCELLULAR DISTRIBUTION; SWINE; VIRAL DISEASES; VIRUSES

Citation Formats


                    Martin-Acebes, Miguel A, Gonzalez-Magaldi, Monica, Rosas, Maria F, Borrego, Belen, Brocchi, Emiliana, Armas-Portela, Rosario, Departamento de Biologia, Facultad de Ciencias, Universidad Autonoma de Madrid, Sobrino, Francisco, and Centro de Investigacion en Sanidad Animal, INIA, Valdeolmos, 28130 Madrid. Subcellular distribution of swine vesicular disease virus proteins and alterations induced in infected cells: A comparative study with foot-and-mouth disease virus and vesicular stomatitis virus.  United States: N. p., 2008. 
        Web.  doi:10.1016/j.virol.2007.12.042.

Copy to clipboard


                    Martin-Acebes, Miguel A, Gonzalez-Magaldi, Monica, Rosas, Maria F, Borrego, Belen, Brocchi, Emiliana, Armas-Portela, Rosario, Departamento de Biologia, Facultad de Ciencias, Universidad Autonoma de Madrid, Sobrino, Francisco, & Centro de Investigacion en Sanidad Animal, INIA, Valdeolmos, 28130 Madrid. Subcellular distribution of swine vesicular disease virus proteins and alterations induced in infected cells: A comparative study with foot-and-mouth disease virus and vesicular stomatitis virus.  United States.  https://doi.org/10.1016/j.virol.2007.12.042

Copy to clipboard


                    Martin-Acebes, Miguel A, Gonzalez-Magaldi, Monica, Rosas, Maria F, Borrego, Belen, Brocchi, Emiliana, Armas-Portela, Rosario, Departamento de Biologia, Facultad de Ciencias, Universidad Autonoma de Madrid, Sobrino, Francisco, and Centro de Investigacion en Sanidad Animal, INIA, Valdeolmos, 28130 Madrid. 2008.  
        "Subcellular distribution of swine vesicular disease virus proteins and alterations induced in infected cells: A comparative study with foot-and-mouth disease virus and vesicular stomatitis virus".  United States.  https://doi.org/10.1016/j.virol.2007.12.042.

Copy to clipboard


                    
@article{osti_21140983,

  title        = {Subcellular distribution of swine vesicular disease virus proteins and alterations induced in infected cells: A comparative study with foot-and-mouth disease virus and vesicular stomatitis virus},

  author       = {Martin-Acebes, Miguel A and Gonzalez-Magaldi, Monica and Rosas, Maria F and Borrego, Belen and Brocchi, Emiliana and Armas-Portela, Rosario and Departamento de Biologia, Facultad de Ciencias, Universidad Autonoma de Madrid and Sobrino, Francisco and Centro de Investigacion en Sanidad Animal, INIA, Valdeolmos, 28130 Madrid},

  abstractNote = {The intracellular distribution of swine vesicular disease virus (SVDV) proteins and the induced reorganization of endomembranes in IBRS-2 cells were analyzed. Fluorescence to new SVDV capsids appeared first upon infection, concentrated in perinuclear circular structures and colocalized to dsRNA. As in foot-and-mouth disease virus (FMDV)-infected cells, a vesicular pattern was predominantly found in later stages of SVDV capsid morphogenesis that colocalized with those of non-structural proteins 2C, 2BC and 3A. These results suggest that assembly of capsid proteins is associated to the replication complex. Confocal microscopy showed a decreased fluorescence to ER markers (calreticulin and protein disulfide isomerase), and disorganization of cis-Golgi gp74 and trans-Golgi caveolin-1 markers in SVDV- and FMDV-, but not in vesicular stomatitis virus (VSV)-infected cells. Electron microscopy of SVDV-infected cells at an early stage of infection revealed fragmented ER cisternae with expanded lumen and accumulation of large Golgi vesicles, suggesting alterations of vesicle traffic through Golgi compartments. At this early stage, FMDV induced different patterns of ER fragmentation and Golgi alterations. At later stages of SVDV cytopathology, cells showed a completely vacuolated cytoplasm containing vesicles of different sizes. Cell treatment with brefeldin A, which disrupts the Golgi complex, reduced SVDV ({approx} 5 log) and VSV ({approx} 4 log) titers, but did not affect FMDV growth. Thus, three viruses, which share target tissues and clinical signs in natural hosts, induce different intracellular effects in cultured cells.},

  doi          = {10.1016/j.virol.2007.12.042},

  url          = {https://www.osti.gov/biblio/21140983},
  journal      = {Virology},

  issn         = {0042-6822},

  number       = 2,

  volume       = 374,

  place        = {United States},

  year         = {Sat May 10 00:00:00 EDT 2008},

  month        = {Sat May 10 00:00:00 EDT 2008}

}

Copy to clipboard

Journal Article:

https://doi.org/10.1016/j.virol.2007.12.042

Other availability

Find in Google Scholar

Search WorldCat to find libraries that may hold this journal

Save / Share:

Export Metadata

Save to My Library

Similar records in OSTI.GOV collections:

Differential distribution of non-structural proteins of foot-and-mouth disease virus in BHK-21 cells

Journal Article Garcia-Briones, Mercedes; Rosas, Maria; Gonzalez-Magaldi, Monica; ... - Virology

Differences in the kinetics of expression and cell distribution among FMDV non-structural proteins (NSPs) have been observed in BHK-21-infected cells. 3D{sup pol} was the first protein detected by immunofluorescence (1.5 h p.i.), showing a perinuclear distribution. At 2-2.5 h p.i., 2B, 2C, 3B and 3C were detected, mostly exhibiting a punctuated, scattered pattern, while 3A and 3D{sup pol} appeared concentrated at one side of the nucleus. This distribution was exhibited by all the NSPs from 3 h p.i., being 2C and, to a lesser extent, precursors 2BC and 3ABBB, the only proteins detected by Western blotting at that infection time.more »« less
https://doi.org/10.1016/j.virol.2006.02.042
Development and Characterization of A Multiplexed RT-PCR Species Specific Assay for Bovine and one for Porcine Foot-and-Mouth Disease Virus Rule-Out

Technical Report Smith, S; Danganan, L; Tammero, L; ...

Lawrence Livermore National Laboratory (LLNL), in collaboration with the Department of Homeland Security (DHS) and the United States Department of Agriculture (USDA), Animal and Plant Health Inspection Services (APHIS) has developed candidate multiplexed assays that may potentially be used within the National Animal Health Laboratory Network (NAHLN), the National Veterinary Services Laboratory (Ames, Iowa) and the Plum Island Animal Disease Center (PIADC). This effort has the ability to improve our nation's capability to discriminate between foreign animal diseases and those that are endemic using a single assay, thereby increasing our ability to protect food and agricultural resources with a diagnosticmore »« less
https://doi.org/10.2172/973852

Full Text Available
Analysis of the interaction between host factor Sam68 and viral elements during foot-and-mouth disease virus infections

Journal Article Rai, Devendra; Lawrence, Paul; Kloc, Anna; ... - Virology Journal

Background: The nuclear protein Src-associated protein of 68 kDa in mitosis (Sam68) is known to bind RNA and be involved in cellular processes triggered in response to environmental stresses, including virus infection. Interestingly, Sam68 is a multi-functional protein implicated in the life cycle of retroviruses and picornaviruses and is also considered a marker of virus-induced stress granules (SGs). Recently, we demonstrated the partial redistribution of Sam68 to the cytoplasm in FMDV infected cells, its interaction with viral protease 3C^pro, and found a significant reduction in viral titers as consequence of Sam68-specific siRNA knockdowns. Despite of that, details of how itmore »« less
https://doi.org/10.1186/s12985-015-0452-8

Full Text Available
Early Events in the Pathogenesis of Foot-and-Mouth Disease in Pigs; Identification of Oropharyngeal Tonsils as Sites of Primary and Sustained Viral Replication

Journal Article Stenfeldt, Carolina; Pacheco, Juan; Rodriguez, Luis; ... - PLoS ONE

A time-course study was performed to elucidate the early events of foot-and-mouth disease virus (FMDV) infection in pigs subsequent to simulated natural, intra-oropharyngeal, inoculation. The earliest detectable event was primary infection in the lingual and paraepiglottic tonsils at 6 hours post inoculation (hpi) characterized by regional localization of viral RNA, viral antigen, and infectious virus. At this time FMDV antigen was localized in cytokeratin-positive epithelial cells and CD172a-expressing leukocytes of the crypt epithelium of the paraepiglottic tonsils. De novo replication of FMDV was first detected in oropharyngeal swab samples at 12 hpi and viremia occurred at 18–24 hpi, approximately 24more »« less
https://doi.org/10.1371/journal.pone.0106859

Full Text Available
Susceptibility to viral infection is enhanced by stable expression of 3A or 3AB proteins from foot-and-mouth disease virus

Journal Article Rosas, Maria; Vieira, Yuri; Postigo, Raul; ... - Virology

The foot-and-mouth disease virus (FMDV) 3A protein is involved in virulence and host range. A distinguishing feature of FMDV 3B among picornaviruses is that three non-identical copies are encoded in the viral RNA and required for optimal replication in cell culture. Here, we have studied the involvement of the 3AB region on viral infection using constitutive and transient expression systems. BHK-21 stably transformed clones expressed low levels of FMDV 3A or 3A(B) proteins in the cell cytoplasm. Transformed cells stably expressing these proteins did not exhibit inner cellular rearrangements detectable by electron microscope analysis. Upon FMDV infection, clones expressing eithermore »« less
https://doi.org/10.1016/j.virol.2008.06.040

Similar Records