Ehrlichia sp. Wisconsin_h
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA242629 | ENA |
REPOSITORIES: ENA
Similar Datasets
Project description:Ehrlichia sp. HF strain:HF Genome sequencing
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Project description:Ehrlichia ruminantium Genome sequencing and assembly
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Project description:Ehrlichia ruminantium strain:Senegalp63 Genome sequencing and assembly
| PRJNA356062 | ENA
Project description:Unraveling which proteins and PTMs affect bacterial pathogenesis and physiology in diverse environments is a tough challenge. Herein, we used mass spectrometry-based assays to study protein phosphorylation and glycosylation in Ehrlichia ruminantium Gardel virulent (ERGvir) and attenuated (ERGatt) variants and, how they can modulate Ehrlichia biological processes. The characterization of the S/T/Y phosphoproteome revealed that both strains share the same set of phosphoproteins (n=58), 36% being overexpressed in ERGvir. The percentage of tyrosine phosphorylation is high (23%) and 66% of the identified peptides are multi-phosphorylated. Glycoproteomics revealed a high percentage of glycoproteins (67% in ERGvir) with a subset of glycoproteins being specific to ERGvir (n=64/371) and ERGatt (n=36/343). These glycoproteins are involved in key biological processes such as protein, amino-acid and purine biosynthesis, translation, virulence, DNA repair and replication. Label-free quantitative analysis revealed over-expression in 31 proteins in ERGvir and 8 in ERGatt. While further PNGase digestion confidently localized 2 and 5 N-glycoproteins in ERGvir and ERGatt, respectively, western blotting suggests that many glycoproteins are O-GlcNAcylated. Twenty three-proteins were detected in both the phospho- and glycoproteome, for the two variants. This work represents the first comprehensive assessment of PTMs on Ehrlichia biology, rising interesting questions regarding ER-host interactions. Phosphoproteome characterization demonstrates an increased versatility of ER phosphoproteins to participate in different mechanisms. The high number of glycoproteins and the lack of glycosyltransferases-coding genes highlight ER dependence on the host and/or vector cellular machinery for its own protein glycosylation. Moreover, these glycoproteins could be crucial to interact and respond to changes in ER environment. PTMs crosstalk between of O-GlcNAcylation and phosphorylation could be used as a major cellular signaling mechanism in ER. As little is known about the Ehrlichia proteins/proteome and its signaling biology, the results presented herein provide a useful resource for further hypothesis-driven exploration of Ehrlichia protein regulation by phosphorylation and glycosylation events.
2019-03-01 | PXD012589 | Pride
Project description:Ehrlichia ruminantium strain:Senegal virulent Genome sequencing and assembly
| PRJNA355590 | ENA
Project description:In order to study the transcriptome of the pathogen, Ehrlichia ruminantium, specific microoarray was designed and validated using genomic DNA of Gardel and Welgevonden strains. Gardel strain was isolated in Guadeloupe and Welgevonden strain in South Africa. DNA from Ehrlichia ruminantium was extracted from cell culture infected with Gardel passage 40 and Welgevonden passage 11, using QIAmp kit (Qiagen). Ehrlichia ruminantium DNA was labeled using BioPrime array CGH labeling system kit (Invitrogen) and Cy3-dCTP (Amersham). Arrays were incubated at 60°C for 20 hours in hybridization chamber. After hybridization, arrays were washed according to the Agilent protocol. Arrays were scanned and the signal intensity of all spots were quantified by Genepix pro 6.0 (Molecular Device Corporation) and data were saved for further analysis.
2009-12-01 | GSE19208 | GEO