Dataset Information

TgPOFUT2 mediated glycosylation_pft line controls

ABSTRACT: Characterisation of glycosylation events within the key adhesin MIC2 of Toxoplasma gondii and the confirmation of tgPOFUT2 as being responsible for Fucosylation of MIC2

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Toxoplasma Gondii Gt1

SUBMITTER: Nichollas Scott

LAB HEAD: Nichollas Scott

PROVIDER: PXD011440 | Pride | 2018-12-04

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	Nsco_20181019_M2AP_B1_SDB_RPS.raw	Raw
	Nsco_20181019_M2AP_B2_SDB_RPS.raw	Raw
	Nsco_20181019_M2AP_B3_SDB_RPS.raw	Raw
	Nsco_20181019_M2AP_B4_SDB_RPS.raw	Raw
	Nsco_20181019_pft_B1_SDB_RPS.raw	Raw

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Publications

Protein O-fucosyltransferase 2-mediated O-glycosylation of the adhesin MIC2 is dispensable for Toxoplasma gondii tachyzoite infection.

Khurana Sachin S Coffey Michael J MJ John Alan A Uboldi Alessandro D AD Huynh My-Hang MH Stewart Rebecca J RJ Carruthers Vern B VB Tonkin Christopher J CJ Goddard-Borger Ethan D ED Scott Nichollas E NE

The Journal of biological chemistry 20181204 5

Toxoplasma gondii is a ubiquitous, obligate intracellular eukaryotic parasite that causes congenital birth defects, disease in immunocompromised individuals, and blindness. Protein glycosylation plays an important role in the infectivity and evasion of immune responses of many eukaryotic parasites and is also of great relevance to vaccine design. Here we demonstrate that micronemal protein 2 (MIC2), a motility-associated adhesin of T. gondii, has highly glycosylated thrombospondin ...[more]

PMID: 30514763

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Project description:Many Gram-negative bacterial pathogens interact with mammalian cells by using type III secretion systems (T3SS) to inject virulence proteins directly into infected host cells. A subset of these injected protein ‘effectors’ are enzymes that modify the structure and inhibit the function of human proteins by catalyzing the addition of unusual post-translational modifications. T3SS effectors play essential roles in bacterial virulence and their modes of action have provided great insight into the functions and the components of the innate immune system. The E. coli and Citrobacter rodentium NleB effectors, as well as the Salmonella enterica SseK effectors are glycosyltransferases that modify host protein substrates with N-acetyl glucosamine (GlcNAc) on arginine residues. Arginine glycosylation is unusual because it occurs on the guanidinium groups of arginines, which are poor nucleophiles. This post-translational modification disrupts the normal functioning of host immune response proteins. T3SS effectors are chaperoned in the bacterium to keep the effectors partially unfolded and competent for secretion, as well as for targeting the effectors to the T3SS sorting platform. The chaperones are then stripped from their effector substrates at the sorting platform and the effectors are secreted in an unfolded conformation. T3SS effectors are thought to be inactive within the bacterium and fold into their active conformations after they are injected into host cells. While performing mass spectrometry experiments to identify glycosylation substrates of NleB orthologs, we unexpectedly observed that the E. coli glutathione synthetase (GshB) is glycosylated on an arginine residue (R256) by NleB. NleB glycosyltransferase activity is essential to C. rodentium survival in oxidative stress conditions because glycosylation of GshB results in enhanced glutathione production. These data represent, to our knowledge, the first intra-bacterial activity for a T3SS effector and show that effector activities thought to be restricted to host cell compartments additionally play important roles in regulating bacterial physiology.

Dataset Information

TgPOFUT2 mediated glycosylation_pft line controls

Dataset's files

Publications

Protein <i>O</i>-fucosyltransferase 2-mediated <i>O</i>-glycosylation of the adhesin MIC2 is dispensable for <i>Toxoplasma gondii</i> tachyzoite infection.

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