Drosophila melanogaster
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA605943 | ENA |
REPOSITORIES: ENA
Similar Datasets
Project description:D.melanogaster Nonsense-Mediated mRNA Decay study
| PRJNA205865 | ENA
Project description:The goal of this study was to generate a high-quality dataset of gene expression in Drosophila melanogaster 3 hours after infection with Gram-positive (M luteus) or Gram-negative (E coli) bacteria.
2023-10-31 | GSE216042 | GEO
Project description:Host recognition of pathogen-associated molecular patterns (PAMPs) initiates an innate immune response that is critical for pathogen elimination and engagement of adaptive immunity. Here we show that mammalian cells can detect and respond to the bacterial-derived monosaccharide heptose-1,7-bisphosphate (HBP). A metabolic intermediate in lipopolysaccharide (LPS) biosynthesis, HBP is highly conserved in Gram-negative bacteria, yet absent from eukaryotic cells. Detection of HBP within the host cytosol activated the NF-?B pathway in vitro, and induced innate and adaptive immune responses in vivo. Moreover, we used a genome-wide RNAi screen to uncover an innate immune signaling axis, mediated by phosphorylation-dependent oligomerization of the TRAF-interacting protein with forkhead-associated domain (TIFA) that is triggered by HBP. Thus, HBP is a PAMP that activates TIFA-dependent immunity to Gram-negative bacteria. We used a microarray to characterize the gene expression signature induced by HBP. We treated two clonal Jurkat T cell lines with culture supernatants prepared from N. gonorrhoeae, a HBP shedding Gram-negative bacteria, or M. catarrhalis, a naturally HBP deficient Gram-negative bacteria. Genes upregulated by N. gonorrhoeae supernatants compared to M. catarrhalis supernatants were considered induced by HBP
2015-04-15 | E-GEOD-67840 | biostudies-arrayexpress
Project description:Co-expression of genes that physically cluster together is a common characteristic of eukaryotic transcriptomes. Identifying these groups of co-expressed genes is important to the functional annotation of genomes and understanding the evolutionary fates of the clustered genes. We used microarrays to measure gene expression in seven closely related Drosophila species, to identify domains clusters within a species of Drosophila (D. simulans) and that are evolving among species in the D. melanogater subgroup. Experiment Overall Design: Assays were carried out on three independent (biological) replicates per species for a single line of the following five species: D.yakuba (Tuscon Stock Center Number: 14021-0261.00), D.santomea (TSCN: 14021-0271.00), D.teissieri (TSCN: 14021-0257.00), D.mauritiana (David 105, TSCN: 14021-0241.01), D.sechellia (Roberstson, TSCN: 14021-0248.21). Three biological replicates for D.melanogaster. The samples assayed for D.melanogaster reflect an even genotypic contribution of 10 isogenic lines developed from a wild population (Winters, CA) and crossed in a round-robin design.For D. simulans, three replicate arrays were used to assay each of 10 round-robin crosses between 10 isogenic lines developed from the same population. the entire data set therefore included a total of 48 independent transcript assays covering seven Drosophila species in the D.melanogaster subgroup
2008-06-16 | E-GEOD-7873 | biostudies-arrayexpress
Project description:Expression data from D.melanogaster guts with a constitutively active Imd in the presence or absence of a microbiome
| PRJNA352228 | ENA
Project description:Host recognition of pathogen-associated molecular patterns (PAMPs) initiates an innate immune response that is critical for pathogen elimination and engagement of adaptive immunity. Here we show that mammalian cells can detect and respond to the bacterial-derived monosaccharide heptose-1,7-bisphosphate (HBP). A metabolic intermediate in lipopolysaccharide (LPS) biosynthesis, HBP is highly conserved in Gram-negative bacteria, yet absent from eukaryotic cells. Detection of HBP within the host cytosol activated the NF-κB pathway in vitro, and induced innate and adaptive immune responses in vivo. Moreover, we used a genome-wide RNAi screen to uncover an innate immune signaling axis, mediated by phosphorylation-dependent oligomerization of the TRAF-interacting protein with forkhead-associated domain (TIFA) that is triggered by HBP. Thus, HBP is a PAMP that activates TIFA-dependent immunity to Gram-negative bacteria. We used a microarray to characterize the gene expression signature induced by HBP.
2015-04-15 | GSE67840 | GEO
Project description:Quantitative comparation of the tagmata of body and head using iTRAQ based on HCD Fragmentation. The 8-plex iTRAQ Multiplex Buffer Kit (AB SCIEX, Foster City, CA) was used to label different peptide fractions, in which iTRAQ reagents dissolved in isopropyl alcohol. Another internal standard of D.melanogaster body and head mixed with 1:1 (B+H) was also used when doing iTRAQ labeling. Therefore the same amount of B (body), H1 (head), H2 (head), B+H (internal standard) peptide fractions prepared as described above were labeled by equal but different iTRAQ reagents and incubated for 5 h at room temperature. The four different labeled peptide fractions (B:113, H1:114, H2:115, B+H:116 ) were then mixed with 1:1 and dried in a speedvac followed by desalting purification using stage tip. All prepared peptides were further analyzed on an LTQ-Orbitrap Velos hybrid mass spectrometer (Thermo Electron, San Jose, CA) coupled with UPLC (nano Acquity Ultra Performance LC, Waters). For HCD raw files, the profile data was firstly centralized by ReAdW.exe in TPP and then deisotoped and deconvoluted using in-house made scripts to improve the identification rate of spectra. All MGF files were searched using Mascot 2.3 against a Drosophila melanogaster database with 24,043 entries (http://flybase.org/, release 5.4, 24,043 entries). The target-decoy based strategy was used to control the peptide false discovery rate (FDR).
2013-11-25 | PXD000454 | Pride