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Rinderpest infection series: Difference between revisions

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{{TimeCourse
{{TimeCourse
|TCOverview=Morbilliviruses including measles virus and rinderpest virus (RPV) are one of the most important pathogens in their respective hosts. In particular, transient strong immunosuppression is the most characteristic feature. Morbillivirus infection induces cell-type-dependent immune responses. However, the molecular mechanisms have not been elucidated. Morbillivirus possesses two nonstructural accessory proteins, V and C. These proteins have been shown to inhibit interferon induction and signaling, although their full functions are unclear. To resolve the complexity and multidimensionality of virus–host interactions, we established recombinant RPV that lacked V and C proteins, and searched for the cell-type-specific transcriptional regulatory network after infection with the FANTOM5 time course analysis. Our study provides a new insight that an accessory protein is one of the virulence factors that define a cell-type-specific response of morbillivirus. This high-throughput experiment uncovers a novel host response against virus infection, and will be useful for understanding the whole picture of virus pathogenesis.<br>
|TCQuality_control=No marker genes are established yet. Infection, replication and growth of virus were verified by cytopathic effect of cells (formation of multinuclear giant cells).
|TCSample_description=We used two major target cell type for RPV infection, a lymphoid cell line (COBL-a cells) and an epithelial cell line (HEK293 cells stably expressing receptor SLAM; 293SLAM cells) [1]. In addition, we established a reverse genetics for RPV-L strain, which is highly virulent against rabbit [2,3], and succeeded in generating recombinant RPV lacking C protein. Cells were infected with each RPV at a multiplicity of infection of 2, and were harvested at 6, 12, 24 and 48 h post infection. Three biological triplicates were performed.<br><br>References:<br>[1] Measles virus induces cell-type specific changes in gene expression. Sato H1, Honma R, Yoneda M, Miura R, Tsukiyama-Kohara K, Ikeda F, Seki T, Watanabe S, Kai C. Virology. 2008 Jun 5;375(2):321-30. PMID:18374960<br>[2] Rinderpest virus H protein: role in determining host range in rabbits. Yoneda M, Bandyopadhyay SK, Shiotani M, Fujita K, Nuntaprasert A, Miura R, Baron MD, Barrett T, Kai C. J Gen Virol. 2002 Jun;83(Pt 6):1457-63. PMID:12029161<br>[3] Rinderpest virus phosphoprotein gene is a major determinant of species-specific pathogenicity. Yoneda M, Miura R, Barrett T, Tsukiyama-Kohara K, Kai C. J Virol. 2004 Jun;78(12):6676-81. PMID:15163758<br>
|Time_Course=
|Time_Course=
|category_treatment=Activation/ infection
|collaborators=Michiko Kai
|collaborators=Michiko Kai
|description=human_rinderpest
|description=human_rinderpest
|germ_layer=mesoderm
|libraryids=CNhs14406,CNhs14407,CNhs14408,CNhs14410,CNhs14411,CNhs14412,CNhs14413,CNhs14414,CNhs14415,CNhs14416,CNhs14417,CNhs14418,CNhs14419,CNhs14420,CNhs14421,CNhs14422,CNhs14423,CNhs14424,CNhs14425,CNhs14426,CNhs14427,CNhs14428,CNhs14429,CNhs14430,CNhs14431,CNhs14432,CNhs14434,CNhs14435,CNhs14436,CNhs14437,CNhs14438,CNhs14439,CNhs14440,CNhs14441,CNhs14442,CNhs14443,CNhs14444,CNhs14445,CNhs14446
|libraryids=CNhs14406,CNhs14407,CNhs14408,CNhs14410,CNhs14411,CNhs14412,CNhs14413,CNhs14414,CNhs14415,CNhs14416,CNhs14417,CNhs14418,CNhs14419,CNhs14420,CNhs14421,CNhs14422,CNhs14423,CNhs14424,CNhs14425,CNhs14426,CNhs14427,CNhs14428,CNhs14429,CNhs14430,CNhs14431,CNhs14432,CNhs14434,CNhs14435,CNhs14436,CNhs14437,CNhs14438,CNhs14439,CNhs14440,CNhs14441,CNhs14442,CNhs14443,CNhs14444,CNhs14445,CNhs14446
|number_time_points=5
|page_name=human_rinderpest
|page_name=human_rinderpest
|primary_cells=primary cells
|series=IN_VITRO DIFFERENTIATION SERIES
|series=IN_VITRO DIFFERENTIATION SERIES
|species=Human (Homo sapiens)
|species=Human (Homo sapiens)
|zenbu_config=http://fantom.gsc.riken.jp/zenbu/gLyphs/#config=F3ezuq6nIV3kT_N9qJhN2C
|tet_config=https://fantom.gsc.riken.jp/5/suppl/tet/Rinderpest.tsv.gz
|tet_file=https://fantom.gsc.riken.jp/5/tet#!/search/?filename=hg19.cage_peak_phase1and2combined_tpm_ann_decoded.osc.txt.gz&file=1&c=1&c=7&c=8&c=9&c=10&c=11&c=12&c=13&c=14&c=15&c=16&c=17&c=18&c=293&c=294&c=295&c=296&c=297&c=298&c=299&c=300&c=301&c=302&c=303&c=304&c=305&c=306&c=307&c=308&c=309&c=310&c=311&c=312&c=313&c=314&c=315&c=316&c=317&c=318&c=319
|time_points=0hr
|time_span=48 hours
|timepoint_design=Activation
|tissue_cell_type=T-cells
|zenbu_config=https://fantom.gsc.riken.jp/zenbu/gLyphs/#config=kEptg5XDGNJsccO6Tae2fC
}}
}}

Latest revision as of 17:21, 14 March 2022

Series:IN_VITRO DIFFERENTIATION SERIES
Species:Human (Homo sapiens)
Genomic View:Zenbu
Expression table:FILE
Link to TET:TET
Sample providers :Michiko Kai
Germ layer:mesoderm
Primary cells or cell line:primary cells
Time span:48 hours
Number of time points:5


Overview

Morbilliviruses including measles virus and rinderpest virus (RPV) are one of the most important pathogens in their respective hosts. In particular, transient strong immunosuppression is the most characteristic feature. Morbillivirus infection induces cell-type-dependent immune responses. However, the molecular mechanisms have not been elucidated. Morbillivirus possesses two nonstructural accessory proteins, V and C. These proteins have been shown to inhibit interferon induction and signaling, although their full functions are unclear. To resolve the complexity and multidimensionality of virus–host interactions, we established recombinant RPV that lacked V and C proteins, and searched for the cell-type-specific transcriptional regulatory network after infection with the FANTOM5 time course analysis. Our study provides a new insight that an accessory protein is one of the virulence factors that define a cell-type-specific response of morbillivirus. This high-throughput experiment uncovers a novel host response against virus infection, and will be useful for understanding the whole picture of virus pathogenesis.

Sample description

We used two major target cell type for RPV infection, a lymphoid cell line (COBL-a cells) and an epithelial cell line (HEK293 cells stably expressing receptor SLAM; 293SLAM cells) [1]. In addition, we established a reverse genetics for RPV-L strain, which is highly virulent against rabbit [2,3], and succeeded in generating recombinant RPV lacking C protein. Cells were infected with each RPV at a multiplicity of infection of 2, and were harvested at 6, 12, 24 and 48 h post infection. Three biological triplicates were performed.

References:
[1] Measles virus induces cell-type specific changes in gene expression. Sato H1, Honma R, Yoneda M, Miura R, Tsukiyama-Kohara K, Ikeda F, Seki T, Watanabe S, Kai C. Virology. 2008 Jun 5;375(2):321-30. PMID:18374960
[2] Rinderpest virus H protein: role in determining host range in rabbits. Yoneda M, Bandyopadhyay SK, Shiotani M, Fujita K, Nuntaprasert A, Miura R, Baron MD, Barrett T, Kai C. J Gen Virol. 2002 Jun;83(Pt 6):1457-63. PMID:12029161
[3] Rinderpest virus phosphoprotein gene is a major determinant of species-specific pathogenicity. Yoneda M, Miura R, Barrett T, Tsukiyama-Kohara K, Kai C. J Virol. 2004 Jun;78(12):6676-81. PMID:15163758

Quality control

No marker genes are established yet. Infection, replication and growth of virus were verified by cytopathic effect of cells (formation of multinuclear giant cells).

Profiled time course samples

Only samples that passed quality controls (Arner et al. 2015) are shown here. The entire set of samples are downloadable from FANTOM5 human / mouse samples


13541-145H4293SLAM rinderpest infection00hrbiol_rep1
13542-145H5293SLAM rinderpest infection00hrbiol_rep2
13543-145H6293SLAM rinderpest infection00hrbiol_rep3
13544-145H7293SLAM rinderpest infection06hrbiol_rep1
13545-145H8293SLAM rinderpest infection06hrbiol_rep2
13546-145H9293SLAM rinderpest infection06hrbiol_rep3
13547-145I1293SLAM rinderpest infection12hrbiol_rep1
13548-145I2293SLAM rinderpest infection12hrbiol_rep2
13549-145I3293SLAM rinderpest infection12hrbiol_rep3
13550-145I4293SLAM rinderpest infection24hrbiol_rep1
13551-145I5293SLAM rinderpest infection24hrbiol_rep2
13552-145I6293SLAM rinderpest infection24hrbiol_rep3
13553-145I7COBL-a rinderpest infection00hrbiol_rep1
13554-145I8COBL-a rinderpest infection00hrbiol_rep2
13555-145I9COBL-a rinderpest infection00hrbiol_rep3
13556-146A1COBL-a rinderpest infection06hrbiol_rep1
13557-146A2COBL-a rinderpest infection06hrbiol_rep2
13558-146A3COBL-a rinderpest infection06hrbiol_rep3
13559-146A4COBL-a rinderpest infection12hrbiol_rep1
13560-146A5COBL-a rinderpest infection12hrbiol_rep2
13561-146A6COBL-a rinderpest infection12hrbiol_rep3
13562-146A7COBL-a rinderpest infection24hrbiol_rep1
13563-146A8COBL-a rinderpest infection24hrbiol_rep2
13564-146A9COBL-a rinderpest infection24hrbiol_rep3
13565-146B1COBL-a rinderpest infection48hrbiol_rep1
13566-146B2COBL-a rinderpest infection48hrbiol_rep2
13567-146B3COBL-a rinderpest infection48hrbiol_rep3
13568-146B4COBL-a rinderpest(-C) infection06hrbiol_rep1
13569-146B5COBL-a rinderpest(-C) infection06hrbiol_rep2
13570-146B6COBL-a rinderpest(-C) infection06hrbiol_rep3
13571-146B7COBL-a rinderpest(-C) infection12hrbiol_rep1
13572-146B8COBL-a rinderpest(-C) infection12hrbiol_rep2
13573-146B9COBL-a rinderpest(-C) infection12hrbiol_rep3
13574-146C1COBL-a rinderpest(-C) infection24hrbiol_rep1
13575-146C2COBL-a rinderpest(-C) infection24hrbiol_rep2
13576-146C3COBL-a rinderpest(-C) infection24hrbiol_rep3
13577-146C4COBL-a rinderpest(-C) infection48hrbiol_rep1
13578-146C5COBL-a rinderpest(-C) infection48hrbiol_rep2
13579-146C6COBL-a rinderpest(-C) infection48hrbiol_rep3
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