Genome-wide analysis of deregulated gene expression by tumor cells (CD45-) or myeloid cells (CD45+) in cocultures infected with measles virus (MV)
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ABSTRACT:
ORGANISM(S): Homo sapiens
PROVIDER: GSE247526 | GEO | 2024/01/15
REPOSITORIES: GEO
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Project description:Genome-wide analysis of deregulated gene expression by tumor cells (CD45-) or myeloid cells (CD45+) in cocultures infected with measles virus (MV)
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Project description:Measles (MV) is an aerosol-transmitted virus that affects more than 10 million children each year and accounts for approximately 120,000 deaths. While it was long believed to replicate in the respiratory epithelium before disseminating, it was recently shown to initially infect macrophages and dendritic cells of the airways using the signaling lymphocytic activation molecule (SLAM, CD150) as receptor. These cells then cross the respiratory epithelium and ferry the infection to lymphatic organs where MV replicates vigorously. How and where the virus crosses back into the airways has remained unknown. However, certain carcinoma cell lines have been described to be either permissive for wt MV infection, or not (Leonard VHJ et al. 2008). Therefor, we decided to compare the expression pattern of permissive and non-permissive cell lines by micro array analysis. Based on functional analyses of surface proteins preferentially expressed on virus-permissive epithelial cell lines, we identified nectin-4 (poliovirus-receptor-like-4) as a candidate receptor.
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Project description:Measles (MV) is an aerosol-transmitted virus that affects more than 10 million children each year and accounts for approximately 120,000 deaths. While it was long believed to replicate in the respiratory epithelium before disseminating, it was recently shown to initially infect macrophages and dendritic cells of the airways using the signaling lymphocytic activation molecule (SLAM, CD150) as receptor. These cells then cross the respiratory epithelium and ferry the infection to lymphatic organs where MV replicates vigorously. How and where the virus crosses back into the airways has remained unknown. However, certain carcinoma cell lines have been described to be either permissive for wt MV infection, or not (Leonard VHJ et al. 2008). Therefor, we decided to compare the expression pattern of permissive and non-permissive cell lines by micro array analysis. Based on functional analyses of surface proteins preferentially expressed on virus-permissive epithelial cell lines, we identified nectin-4 (poliovirus-receptor-like-4) as a candidate receptor. The dataset comprises 21 samples divided into seven sample groups each representing 3 biological replicates of one out of 7 cell lines.
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Project description:To identify the respective roles of light and ROS in the photoinhibition process and detect a possible light-driven tolerance to oxidative stress, we compared the transcriptomic responses of Synechococcus sp. WH7803 acclimated to low (LL) or high light (HL) to oxidative stress, induced by hydrogen peroxide (H202) or methylviologen (MV). Cultures were acclimated during many generations to continuous low light (LL, 18 ?mol photons m-2 s-1, hereafter LL cells) and high light (HL, 250 ?mol photons m-2 s-1, hereafter HL cells) provided by Sylvania Daylight 58W/154 fluorescent bulbs. For all stress experiments performed in this study, exponentially growing cultures (1 to 3 x 107 cells mL-1), were split into subcultures and submitted to oxidative stress by addition of H2O2 or MV and harvested when PSII quantum yield fell to half of the initial value. For H2O2 experiments, this level of PSII photoinactivation was reached 2 h after submitting LL and HL cultures to 750 M and 25 M respectively. Because of the large divergence in dose and kinetics responses to MV between LL- and HL cells, it was not possible to find MV concentrations leading to 50 % decrease of quantum yield at the same time for both light acclimations. Thus, array analyses for MV were performed on HL and LL cultures incubated at the same MV concentration (50 M) but harvested once PSII quantum yield was halved, i.e. after 1 and 3.5 h of stress respectively. All hybridizations were performed on 4 independent biological replicates and using as reference sample a pool of RNA from all samples investigated in this study. Pairwise comparison were performed to analyze the stress induced by either H2O2 or MV on both LL- and HL cultures (i.e. LL-Ct vs. LL+MV, LL-Ct vs. LL+H2O2, HL-Ct vs. HL+MV, HL-Ct vs. HL+H2O2) as well as to compare the steady state acclimation to different light conditions (i.e. LL-Ct vs. HL-Ct).
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Project description:Classically, the cytidine deaminase APOBEC3G (A3G) exerts antiviral activity against transposable elements, retroviruses, and hepatitis B virus. However, we found earlier, that it also inhibits measles (MV), mumps (MuV) and respiratory syncytial virus (RSV), but the mechanism of inhibition remained unclear. Because A3G is present in RNA processing (P) bodies, where it is involved in the regulation of mRNA decay, we supposed that it may influence the expression of host cell factors, some of which may affect viral replication. Using a microarray we therefore assessed in Vero cells whether A3G expression influences the cellular gene expression. We found alterations indicating 844 up-regulated and 598 down-regulated transcripts (adjusted P values < 0.05). Of these trancripts 19 were up-regulated and 23 down-regulated by a factor of > 2. One of the down-regulated factors, MOSC2, appeared to support MV replication, since shRNA-mediated MOSC2 knock down reduced MV replication. In addition, two up-regulated factors, REDD1 and KDELR2, impaired MV replication when over-expressed in VeroREDD1 is a cellular inhibitor of mTORC1, a regulator of cellular homeostasis controlling cell growth and protein synthesis. Rapamycin also reduced MV replication confirming our findings with REDD1. The KDELR2 retains chaperons in the ER, which are required for proper folding and transport of MV glycoproteins to the cell surface, and thereby reduces MV glycoprotein expression at the cell surface, syncytium formation, and the formation of infectious virus.
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Project description:Viruses manipulate central machineries of host cells to their advantage. They prevent host cell antiviral responses in order to create a favourable environment for their survival and propagation. Measles virus (MV) encodes two non-structural proteins MV-V and MV-C, proposed to counteract the host interferon response and to regulate cell death pathways in various functional assays. Several molecular mechanisms underlining MV-V regulation of innate immunity and cell death responses have been proposed, whereas MV-C host protein partners are less studied. We suggest that some cellular factors that are controlled by MV-C protein during viral replication could be components of innate immunity and the cell death pathways. In order to determine which host factors are hijacked by MV-C, we captured both direct and indirect host protein partners of MV-C protein. For this we used a strategy based on recombinant viruses expressing tagged viral proteins followed by affinity purification and a bottom-up mass spectrometry analysis. A list of host proteins specifically interacting with MV-C protein in different cell lines was identified.
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