PXD012589

PXD012589 is an original dataset announced via ProteomeXchange.

Title	Sweet and sour Ehrlichia: glycoproteomics and phosphoproteomics reveal new players in Ehrlichia ruminantium physiology and pathogenesis
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.
HostingRepository	PRIDE
AnnounceDate	2019-03-01
AnnouncementXML	Submission_2019-05-14_07:16:41.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Isabel Marcelino
SpeciesList	scientific name: Ehrlichia ruminantium str. Gardel; NCBI TaxID: 302409;
ModificationList	phosphorylated residue; monohydroxylated residue; iodoacetamide derivatized residue; deamidated residue
Instrument	LTQ Orbitrap Velos

Revision	Datetime	Status	ChangeLog Entry
0	2019-02-01 05:49:00	ID requested
1	2019-03-01 00:01:39	announced
⏵ 2	2019-05-14 07:16:42	announced	Updated publication reference for PubMed record(s): 30930869.

Marcelino I, Colom, é, -Calls N, Holzmuller P, Lisacek F, Reynaud Y, Canals F, Vachi, é, ry N, Physiology and Pathogenesis. Front Microbiol, 10():450(2019) [pubmed]

curator keyword: Biological

submitter keyword: Ehrlichia species

phosphoproteins

S/T/Y phosphorylation

N-glycoproteins

O-GlcNAcylated proteins

bacteria physiology

pathogenesis

Nathalie Vachiery
contact affiliation	ASTRE, Univ Montpellier, CIRAD, INRA, Montpellier, France & CIRAD, UMR ASTRE, F-34398, Montpellier, France
contact email	nathalie.vachiery@cirad.fr
lab head
Isabel Marcelino
contact affiliation	Institut Pasteur de Guadeloupe
contact email	isabel.marcelino.im@gmail.com
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD012589
     1. Label: PRIDE project
     2. Name: Sweet and sour Ehrlichia: glycoproteomics and phosphoproteomics reveal new players in Ehrlichia ruminantium physiology and pathogenesis