Ehrlichia sp. JZT12
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA757527 | ENA |
REPOSITORIES: ENA
Similar Datasets
Project description:Ehrlichia sp. Wisconsin_h Genome sequencing and assembly
| PRJNA242629 | ENA
Project description:Ehrlichia ruminantium Genome sequencing and assembly
| PRJNA493174 | ENA
Project description:Ehrlichia japonica strain:HF Genome sequencing
| PRJNA187357 | 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 chaffeensis is an obligately intracellular bacterium that establishes infection in mononuclear phagocytes through largely undefined reprogramming strategies. Recently, E. chaffeensis effectors Ank200, TRP120, and TRP32 have been shown to function as nucleomodulins that enter the host nucleus and directly modulate transcription of genes implicated in cellular processes such as transcription regulation, apoptosis, phosphorylation, and immune cell activation. In this study, we found that E. chaffeensis TRP47 enters the host cell nucleus and binds regulatory regions of multiple host genes relevant to infection.
2018-08-14 | GSE118453 | GEO