FN Archimer Export Format
PT J
TI Sweet and Sour Ehrlichia: Glycoproteomics and Phosphoproteomics Reveal New Players in Ehrlichia ruminantium Physiology and Pathogenesis
BT 
AF MARCELINO, Isabel
   COLOME-CALLS, Nuria
   HOLZMULLER, Philippe
   LISACEK, Frederique
   REYNAUD, Yann
   CANALS, Francesc
   VACHIERY, Nathalie
AS 1:1,2,3;2:4;3:2,5;4:6,7,8;5:3;6:4;7:2,5;
FF 1:;2:;3:;4:;5:;6:;7:;
C1 UMR ASTRE, CIRAD, Petit Bourg, Guadeloupe, France.
   Univ Montpellier, INRA, CIRAD, ASTRE, Montpellier, France.
   Inst Pasteur Guadeloupe, Unite TReD Path Transmiss Reservoirs & Diversite, Les Abymes, Guadeloupe, France.
   VHIO, Prote Lab, Barcelona, Spain.
   UMR ASTRE, CIRAD, Montpellier, France.
   Swiss Inst Bioinformat, Proteome Informat, Geneva, Switzerland.
   Univ Geneva, Comp Sci Dept, Geneva, Switzerland.
   Univ Geneva, Sect Biol, Geneva, Switzerland.
C2 CIRAD, FRANCE
   UNIV MONTPELLIER, FRANCE
   INST PASTEUR GUADELOUPE, FRANCE
   PROTE LAB, SPAIN
   CIRAD, FRANCE
   SWISS INST BIOINFORMAT, SWITZERLAND
   UNIV GENEVA, SWITZERLAND
   UNIV GENEVA, SWITZERLAND
IN DOAJ
IF 4.235
TC 6
UR https://archimer.ifremer.fr/doc/00771/88282/93896.pdf
   https://archimer.ifremer.fr/doc/00771/88282/93897.xlsx
   https://archimer.ifremer.fr/doc/00771/88282/93898.xlsx
   https://archimer.ifremer.fr/doc/00771/88282/93899.xlsx
   https://archimer.ifremer.fr/doc/00771/88282/93900.xlsx
   https://archimer.ifremer.fr/doc/00771/88282/93901.xlsx
   https://archimer.ifremer.fr/doc/00771/88282/93902.xlsx
LA English
DT Article
DE ;Ehrlichia ruminantium;phosphoproteins;S/T/Y phosphorylation;N-glycoproteins;O-GIcNAcylated proteins;bacteria physiology;pathogenesis
AB Unraveling which proteins and post-translational modifications (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-GIcNAcylated. 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-GIcNAcylation 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. The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium with the data set identifier PXDO12589.
PY 2019
PD MAR
SO Frontiers In Microbiology
SN 1664-302X
PU Frontiers Media Sa
VL 10
UT 000461256500001
DI 10.3389/fmicb.2019.00450
ID 88282
ER

EF