PXD057551-1

PXD057551 is an original dataset announced via ProteomeXchange.

Title	Development of a New N-Terminomic Method to Study the Pathodegradome of the Staphylococcus aureus V8 Protease in Human Neutrophils
Description	Staphylococcus aureus is a notorious human pathogen that relies on an array of virulence factors to engender infection and evade the host-immune system. Among these are the secreted proteases, which promote pathogenesis by degrading host proteins and modulating host-defenses. Human neutrophils play a pivotal role in these defenses, acting as the first responders against invading bacteria. While many S. aureus effectors of virulence have been shown to target leukocytes, there is limited knowledge on how the extracellular proteases modulate neutrophil fate. Typically, protease substrates have been identified in isolated settings using one at a time approaches; with neutrophil targets few and far between. Herein, we have developed a novel N-terminomic methodology termed TAGS-CR that can facilitate global substrate characterization in streamlined manner. We thus present the application of TAGS-CR to unravelling the human neutrophil pathodegradome of the S. aureus V8 protease. In so doing, we captured ~350 V8 targets, revealing critical insight into how this virulence factor can modulate neutrophil functionality on various levels relevant to S. aureus disease progression. We recorded cleavage of proteins necessary for neutrophil adhesion and migration, a fundamental process necessary for pathogen clearance. Furthermore, we highlight V8 cleavage of proteins involved in important neutrophil defense tactics, such as degranulation and reactive oxygen species production. This protease may also facilitate bacterial dissemination via the intentional activation of neutrophil apoptosis. Collectively, this work deepens our understanding of host-pathogen interaction and begins to unravel how S. aureus proteases can induce immune dysregulation through the targeting of leukocytes.
HostingRepository	PRIDE
AnnounceDate	2025-05-30
AnnouncementXML	Submission_2025-05-30_10:17:01.027.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Emilee Mustor
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	L-homoarginine; acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2024-11-05 14:19:54	ID requested
⏵ 1	2025-05-30 10:17:01	announced

10.1101/2024.11.08.622692;

submitter keyword: Degradomics, Neutrophils, TAGS-CR, Immune dysregulation.,Staphylococcus aureus, V8 protease

Lindsey N. Shaw
contact affiliation	Department of Molecular Biosciences, University of South Florida, Tampa, FL, USA Center for Antimicrobial Resistance, University of South Florida, Tampa, FL, USA
contact email	shaw@usf.edu
lab head
Emilee Mustor
contact affiliation	University of South Florida
contact email	emileemustor@usf.edu
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2025/05/PXD057551

PRIDE project URI

• PRIDE
  1. PXD057551
     1. Label: PRIDE project
     2. Name: Development of a New N-Terminomic Method to Study the Pathodegradome of the Staphylococcus aureus V8 Protease in Human Neutrophils