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O-fucosylated glycoproteins of Toxoplasma gondii

ABSTRACT: The fucose-binding Aleuria aurantia lectin (AAL) labels punctiform structures in proximity to the nuclei of Toxoplasma gondii tachyzoites. We have utilized AAL-lectin affinity purification in conjunction with LC MS/MS to identify a set of proteins modified with fucose on serines and threonines

INSTRUMENT(S): Agilent instrument model, Q Exactive

ORGANISM(S): Toxoplasma Gondii

SUBMITTER: John Haserick

LAB HEAD: Catherine E. Costello

PROVIDER: PXD004426 | Pride | 2016-10-11

REPOSITORIES: pride

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			Action	DRS
	07-15-2015_Tg_AAL_E1_In-sol (peptides_1_0_0.mzid).pride.mztab.gz	Mztab
	07-15-2015_Tg_AAL_E1_In-sol.raw	Raw
	07-15-2015_Tg_AAL_E1_In-sol_45V.raw	Raw
	07-15-2015_Tg_AAL_E1_In-sol_45V_re-run.raw	Raw
	07-15-2015_Tg_AAL_E1_In-sol_45V_re-runpeptides_1_0_0.mzid.mzid.gz	Mzid

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Publications

O-fucosylated glycoproteins form assemblies in close proximity to the nuclear pore complexes of Toxoplasma gondii.

Bandini Giulia G Haserick John R JR Motari Edwin E Ouologuem Dinkorma T DT Lourido Sebastian S Roos David S DS Costello Catherine E CE Robbins Phillips W PW Samuelson John J

Proceedings of the National Academy of Sciences of the United States of America 20160923 41

Toxoplasma gondii is an intracellular parasite that causes disseminated infections in fetuses and immunocompromised individuals. Although gene regulation is important for parasite differentiation and pathogenesis, little is known about protein organization in the nucleus. Here we show that the fucose-binding Aleuria aurantia lectin (AAL) binds to numerous punctate structures in the nuclei of tachyzoites, bradyzoites, and sporozoites but not oocysts. AAL also binds to Hammondia and Neospora nucle ...[more]

PMID: 27663739

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Proteomic and Glycoproteomic Analyses of Fucosylated Glycoproteins in Head and Neck Cancer Cell Lines

Project description:Peptide and glycopeptide level LC-MS/MS analysis of whole cell lysate and Aleuria aurantia Lectin (AAL)-enriched glycoproteins.

2022-02-14 | PXD029420 | Pride

Arabidopsis thaliana LC-MS/MS in mock and AAL treated plants

Project description:AAL toxin (the major virulence factor of Alternaria alternata f. sp. lycopersici)was treated to wild type(Col-0)and transgenic Arabidopsis with enhanced GSH (AtECS1). A proteomic profile was obtained by nano LC-MS/MS analysis.Among the identified proteins, a few proteins were selected for qRT-PCR and western blot analysis. It was found that AAL mediated resistance in plants can be conferred by GSH through SA and ET mediated pathways, in addition to several stress responsive molecules.

2020-08-07 | PXD017124 | Pride

LC-MS/MS analysis of pancreatic cancer plasma

Project description:Pancreatic cancer (PC) is an aggressive cancer with a high mortality rate, necessitating the de-velopment of effective diagnostic, prognostic and predictive biomarkers for disease manage-ment. Aberrantly fucosylated proteins in PC are considered a valuable resource of clinically useful biomarkers. The main objective of the present study was to identify novel plasma glyco-biomarkers of PC using the iTRAQ quantitative proteomics approach coupled with Aleuria au-rantia lectin (AAL)-based glycopeptide enrichment and isotope-coded glycosylation site-specific tagging, with a view to analyzing the glycoproteome profiles of plasma samples from patients with non-metastatic and metastatic PC and gallstones (GS). As a result, 22 glycopeptides with significantly elevated levels in plasma samples of PC were identified. Fucosylated SERPINA1 (fuco-SERPINA1) was selected for further validation in 121 plasma samples (50 GS and 71 PC) using an AAL-based reverse lectin ELISA technique developed in-house. Our analyses revealed significantly higher plasma levels of fuco-SERPINA1 in PC than GS subjects (310.7 ng/ml v.s. 153.6 ng/ml, p = 0.0114). Elevated fuco-SERPINA1 levels were associated with higher TNM stage (p = 0.024) and poorer prognosis for overall survival (log-rank test, p = 0.0083). The increased plasma fuco-SERPINA1 levels support the utility of this protein as a novel prognosticator for PC.

2021-09-10 | PXD025150 | Pride

Electron-based dissociation is needed for O-glycopeptides derived from OpeRATOR proteolysis

Project description:The recently described O-glycoprotease OpeRATOR presents exciting opportunities for O-glycoproteomics. This bacterial enzyme purified from A. muciniphila cleaves N-terminally to serine and threonine residues that are modified with (preferably asialylated) O-glycans, providing orthogonal cleavage relative to canonical proteases (e.g., trypsin) to improve O-glycopeptide characterization with tandem mass spectrometry (MS/MS). O-glycopeptides with a modified N-terminal residue, such as those generated by OpeRATOR, present several potential benefits, perhaps the most notable being de facto O-glycosite localization without the need of glycan-retaining fragments in MS/MS spectra. Indeed, O-glycopeptides modified exclusively at the N-terminus would enable O-glycoproteomic methods to rely solely on collision-based fragmentation rather than electron-driven dissociation, but modified peptides would need to reliably contain only a single O-glycosite. Here we characterize the number of O-glycosites (i.e., missed cleavages) that are present in OpeRATOR-derived O-glycopeptides using methods that combine collision- and electron-based fragmentation. Our data show that over 50% of O-glycopeptides generated from combined digestion using OpeRATOR and trypsin contain multiple O-glycosites, indicating that collision-based fragmentation is not sufficient for OpeRATOR-centric studies and that electron-driven dissociation remains a requirement for site-specific O-glycopeptide characterization.

2020-11-03 | PXD020077 | Pride

Comparative proteomics of defense response to AAL toxin

Project description:A comparative proteomics analysis on AAL toxin treated jai1 mutant and its wild type revealed that JA pathway promoted AAL toxin induced PCD by regulating the relevant PCD components and/or through other hormone pathways in a SlCOI1 dependent manner.</br></br>Additional contact: <a href="mailto:xixizhangmin@123.com" target="_top">Min Zhang</a>, Zhejiang University.

2016-06-27 | PXD002864 | Pride

Comparative characterization of microRNA profiles of different genotypes of Toxoplasma gondii

Project description:The present study characterized comparatively the miRNA profiles of three different genotypes of T. gondii, identified genotype-shared miRNAs and strain-specific miRNAs. Compared the miRNA expression profiles of five T. gondii strains

2013-10-29 | E-GEOD-45007 | biostudies-arrayexpress

Protamine characterization by top-down proteomics: Boosting proteoform identification with DBSCAN

Project description:Protamines replace histones as the main nuclear protein in sperm cells having a crucial role in compacting the paternal genome. Human spermatozoa contain the protamine 1 (P1) and the family of protamine 2 (P2) proteins. Alterations in protamine PTMs or on the P1/P2 ratio could be associated with male infertility. Top-down proteomics enables large-scale analysis of intact proteforms derived from alternative splicing, missense or nonsense genetic variants or PTMs. In contrast to current gold standard techniques, top-down allows a more in-depth analysis of protamine PTMs and proteoforms, opening up new perspectives to unravel their impact on male fertility. We analyzed two normozoospermic semen samples by top-down and discussed in detail the difficulties we found in the data analysis and the suggested solutions, as this step is one of the current bottlenecks in top-down proteomics with currently available bioinformatic tools. Our strategy for the data analysis combines two different software, ProSight PD (PS) and TopPIC suite (TP), with a clustering algorithm to decipher protamine proteoforms. We identified up to 32 protamine proteoforms at different levels of characterization. This in-depth analysis of the protamine proteoform landscape of an individual boosts personalized diagnosis of male infertility.

2021-05-13 | PXD024405 | Pride

A dynamic and combinatorial histone code drives malaria parasite asexual and sexual development

Project description:Histone post-translational modifications (PTMs) are frequently co-occurring on the same chromatin domains or even the same molecule. It is now established that these ‘histone codes’ are the result of cross-talk between enzymes that catalyse multiple PTMs with univocal readout as compared to these PTMs in isolation. Here, we performed a comprehensive identification and quantification of histone codes of the malaria parasite, Plasmodium falciparum. We used advanced quantitative middle-down proteomics to identify combinations of PTMs in both the proliferative, asexual stages and transmissible, sexual gametocyte stages of P. falciparum. We provide an updated, high-resolution compendium of 72 PTMs on H3 and H3.3, of which 30 newly identified. Several co-existing PTMs with unique stage distinction was identified, indicating that many of these combinatorial PTMs are associated to specific stages of the parasite life cycle. We focused on the code H3R17me2K18acK23ac for its unique presence in mature gametocytes; chromatin proteomics identified a gametocyte-specific SAGA-like effector complex including the transcription factor AP2-G2 which we associated to this specific histone code, as involved in regulating gene expression in mature gametocytes. Ultimately, this study unveils previously undiscovered histone PTMs and their functional relationship with co-existing partners. These results highlight that investigating chromatin regulation in the parasite using single histone PTM assays might overlook higher order gene regulation for distinct proliferation and differentiation processes.

2022-05-19 | PXD030181 | Pride

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