PXD045142

PXD045142 is an original dataset announced via ProteomeXchange.

Title	Combining FAIMS based Glycoproteomic and DIA Proteomic of reveals widespread proteome alteration in response to changes in N. gonorrhoeae glycosylation occupancy.
Description	Protein glycosylation is increasingly recognized as a common protein modification across bacterial species. Within pathogenic members of the Neisseria genus O-linked protein glycosylation is associated with virulence yet the depth of the glycoproteome, or if glycosylation plays additional roles in Neisserial physiology are largely unknown. Recently it was identified that even closely related members of the Neisseria genus can possess O-Oligosaccharyltransferases, pglOs, that possess distinct targeting activities suggesting extensive glycoproteome diversity in terms of the substrates capable of being glycosylated across Neisserial species. Within this work we explore this concept using Field Asymmetric Waveform Ion Mobility Spectrometry (FAIMS) fractionation and Data-Independent Acquisition (DIA) to allow the characterization of differences in the glycoproteomes and proteomes within N. gonorrhoeae strains expressing differing pglO alleles. We demonstrate the utility of FAIMS to expand the known glycoproteome of N. gonorrhoeae enabling the characterization of the glycoproteomes of wild type N. gonorrhoeae MS11 as well as a recently reported panel of strains expressing different pglO allelic chimeras (15 PglO enzymes) with unique substrate targeting activities. Combining glycoproteomic insights with DIA proteomics we demonstrate that alterations within pglO alleles have widespread impacts on the proteome of N. gonorrhoeae. Examination of peptides known to be targeted by glycosylation using DIA analysis supports alterations in glycosylation occupancy independent of changes in protein levels and that the occupancy of glycosylation is generally low on most glycoproteins. Combined this work expands our understanding of the N. gonorrhoeae glycoproteome and the impact of glycosylation on bacterial species.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_06:28:17.479.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Nichollas Scott
SpeciesList	scientific name: Neisseria gonorrhoeae FA19; NCBI TaxID: 528352;
ModificationList	complex glycosylation
Instrument	Orbitrap Exploris 480

Revision	Datetime	Status	ChangeLog Entry
0	2023-09-06 01:26:43	ID requested
1	2024-02-01 05:33:18	announced
⏵ 2	2024-10-22 06:28:17	announced	2024-10-22: Updated project metadata.

Dataset with its publication pending

submitter keyword: FAIMS, LC-MS,glycosylation, Neisseria

Nichollas E. Scott
contact affiliation	Department of Microbiology and Immunology, University of Melbourne at the Peter Doherty Institute for Infection and Immunity, Melbourne 3000, Australia
contact email	nichollas.scott@ubnimelb.edu.au
lab head
Nichollas Scott
contact affiliation	University of Melbourne
contact email	nichollas.scott@unimelb.edu.au
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD045142
     1. Label: PRIDE project
     2. Name: Combining FAIMS based Glycoproteomic and DIA Proteomic of reveals widespread proteome alteration in response to changes in N. gonorrhoeae glycosylation occupancy.