Aedes aegypti
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ABSTRACT:
PROVIDER: PRJNA290625 | ENA |
REPOSITORIES: ENA
Similar Datasets
Project description:In order to study heme-induced global transcriptional changes, we performed a transcriptome-wide analysis of heme influence on the A. aegypti cell line Aag2. As heme-mediated effects on gene expression are thought to be related to oxidative stress, we compared the transcriptional profiles of Aag2 cells challenged with either 50 µM heme or 100 µM of the ROS inducer paraquat, using whole genome microarrays. Three-condition experiment, CTR vs. Heme- or Paraquat incubated cells. Biological replicates: 4 control and 4 experimental replicates.
2016-07-29 | E-GEOD-71221 | biostudies-arrayexpress
Project description:In order to study heme-induced global transcriptional changes, we performed a transcriptome-wide analysis of heme influence on the A. aegypti cell line Aag2. As heme-mediated effects on gene expression are thought to be related to oxidative stress, we compared the transcriptional profiles of Aag2 cells challenged with either 50 µM heme or 100 µM of the ROS inducer paraquat, using whole genome microarrays.
2016-07-29 | GSE71221 | GEO
Project description:The study provides a comparative of transcript levels in uninfected and CHIKV-infected Aedes aegypti derived Aag2 cells using RNA Seq
2022-04-11 | GSE195852 | GEO
Project description:Aedes aegypti Aag2 cells transcriptome upon Dhx15 knockdown
| PRJNA885496 | ENA
Project description:Aedes aegypti Aag2 small RNAs +/- DENV2
| PRJNA310830 | ENA
Project description:Aedes aegypti (Aag2) Raw small RNA and PacBio sequence reads
| PRJNA398563 | ENA
Project description:After a bloodmeal, mosquitoes import heme into the midgut epithelium. Heme acts as an essential signal for oogenesis in Aedes aegypti. However, the mechanisms behind heme import in Aedes aegypti are largely unexplored. In this study, RNA sequencing data from 4 different Aedes aegypti cell culture experiments where exposure to an overabundance or deficiency of heme was examined to identify heme-responsive genes. Zinc mesoporphyrin (ZnMP), a heme fluorescent analog, was used to measure changes in heme uptake prior to mRNA sequencing. A soft cluster analysis was performed to identify genes encoding potential membrane bound importers and exporters based on expression profiles across the samples for each experiment. Stronger candidates were obtained by comparing genes in each dataset to each other. When comparing all datasets to each other, 223 candidate genes with expression pattern changes consistent with importers were found to be heme-regulated in only 2 datasets, 46 were heme-regulated in 3 datasets and 2 was heme-regulated in all 4 datasets. In contrast, 114 candidate genes with patterns consistent with exporters were common to only 2 datasets, with just 11 present in 3 of the 4 datasets. A large number of genes containing transmembrane domains were isolated across the 4 datasets which showed downregulation or upregulation in response to heme overexposure conditions indicating the possibility that heme membrane bound import and export genes were identified respectively, with the reverse trend observed in the presence of heme deficiency. However, few transporter candidate genes were identified that showed high differential expression (above 4-fold or below 1/4th fold). Ultimately, as few strong candidates were identified by these studies, we consider the possibility that each cell line could have a redundant system of heme import, whereby multiple transport proteins each contribute to the total heme accumulation in the cell. Alternatively, it is possible that these cells lines do not regulate heme transport at the transcript level, but rather do so post-translationally.
2020-08-03 | GSE140752 | GEO
Project description:The female mosquito Aedes aegypti requires amino acids and other nutrients like heme and iron from a blood meal to initiate vitellogenesis. Heme is a pro-oxidant molecule that acts as a nutrient, signaling molecule and in large quantities, as a toxin. Ae. aegypti has developed a few strategies to handle heme toxicity, as during a typical meal ~10mM is released into the midgut lumen. These strategies include heme aggregation to the peritrophic matrix and the degradation of heme by heme oxygenase in the cytosol of the midgut epithelium. However, despite the importance of heme as a nutrient and toxin, the mechanism of entry into the midgut epithelial cells is not currently known. As no heme transport proteins in have been identified in any dipteran, heme fluorescent analog studies were performed to visualize changes in expression caused by heme followed by global expression analyses performed in midgut tissues using NGS-based RNA sequencing with the end goal to identify the gene(s) that encode the membrane bound heme import proteins responsible for heme uptake during blood digestion. Examination of differential expression of mRNA transcripts at the gene level, found 65 significant DE genes at the adjusted p-value cut off of 0.0001, 38 of which are TM containing and only 2 of which showed high expression changes, AAEL019570 (-2.04 log2, ~0.243), unknown function, and AAEL000717 (3.91 log2, ~15.03), a protocadherin. This list was further reduced to 16 genes with potential heme import function and 7 genes with potential heme export function by examination of differential expression, number of TM domains and function relating to transport. As very few highly differentially expressed genes were found in the analysis, heme import may be controlled by a redundant system of multiple transport proteins instead of a single highly expressed one. Alternatively, heme transport in Ae. aegypti could be regulated post-translationally.
2020-08-03 | GSE141651 | GEO
Project description:Aag2, Aag2.wAlbB, and Aag2.tet Raw sequence reads
| PRJNA901205 | ENA
Project description:Loquacious-2 (Loqs2) is a recently identified paralog of Loquacious found in Aedes aegypti. Data presented here allowed the proteomic characterization of Loqs2 interactome in Aedes aegypti Aag2 cells. We carried out immunoprecipitation experiments where Loqs2 tagged protein was precipitated along with its partners. Immunoprecipitation of tagged eGFP protein was performed in the same conditions to verify the specificity of these associations. Experiments were performed in biological triplicates.
2018-11-21 | PXD010191 | Pride