PXD056653

PXD056653 is an original dataset announced via ProteomeXchange.

Title	The secreted proteases Aur, ScpA, SspA and SspB suppress virulence of Staphylococcus aureus USA300 by shaping the extracellular proteome
Description	Surface-located and secreted virulence factors of the Gram-positive bacterial pathogen Staphylococcus aureus are key drivers for infection of the human host. Proteolytic enzymes may contribute to virulence by breaking primary barriers and host immune defenses. Therefore, the objective of our present study was to chart the contributions of different proteases to S. aureus virulence, and to assess their roles in shaping the staphylococcal surface proteome (the ‘surfacome’) and extracellular proteome (the ‘secretome’). To this end, we applied 12 protease mutants of the S. aureus USA300 lineage. Four mutants lacking the metalloprotease aureolysin (Aur), the cysteine proteases staphopain A (ScpA) and SspB, or the serine protease SspA displayed enhanced cytotoxicity towards human lung epithelial cells, showing that they serve to suppress virulence. Profiling of the surfacomes and secretomes of the four mutants allowed correlation of their increased cytotoxicity to altered virulence factor profiles. Furthermore, enhanced levels of virulence factors were detected in the mutants’ surfacomes, which was shown to be relevant as all four mutants displayed enhanced lung epithelial cell invasion. Enhanced levels of cytoplasmic and membrane proteins in the mutant’s surfacomes showed that Aur, ScpA, SspA and SspB set limits to autolysis by reducing the levels of peptidoglycan hydrolases. We conclude that Aur, ScpA, SspA and SspB have major roles in shaping the surfacome and secretome of S. aureus, thereby controlling the virulence of this major pathogen. This implies that novel antimicrobial agents or vaccines should not target these proteases.
HostingRepository	PRIDE
AnnounceDate	2025-04-22
AnnouncementXML	Submission_2025-04-22_05:00:01.415.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Sandra Maass
SpeciesList	scientific name: Staphylococcus aureus; NCBI TaxID: 1280;
ModificationList	acetylated residue; monohydroxylated residue
Instrument	LTQ Orbitrap Elite

Revision	Datetime	Status	ChangeLog Entry
0	2024-10-09 05:57:05	ID requested
⏵ 1	2025-04-22 05:00:01	announced

Dataset with its publication pending

submitter keyword: Staphylococcus aureus

virulence

proteases

peptidoglycan hydrolase

cell lysis

Dörte Becher
contact affiliation	Department of Microbial Proteomics, University of Greifswald, Centre of Functional Genomics of Microbes, Institute of Microbiology, Greifswald, Germany
contact email	dbecher@uni-greifswald.de
lab head
Sandra Maass
contact affiliation	University of Greifswald, Department for Microbial Proteomics
contact email	sandra.maass@uni-greifswald.de
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD056653
     1. Label: PRIDE project
     2. Name: The secreted proteases Aur, ScpA, SspA and SspB suppress virulence of Staphylococcus aureus USA300 by shaping the extracellular proteome