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Staphylococcal SplA and SplB serine proteases target ubiquitin(-like) specific proteases

ABSTRACT: Staphylococcus aureus is a gram-positive opportunistic pathogen that has colonized nearly 30% of the human population and can cause life-threatening infections. The antibiotic treatment of S. aureus infection is often hindered by several resistances expressed by the pathogen, and therefore alternative therapies are much-needed. S. aureus exports a variety of virulence factors, among them numerous proteases. In 1996, a novel set of extracellular serine proteases was discovered: the serine protease-like proteins (Spls). Spl proteins are expressed by most clinical isolates of S. aureus, but their pathophysiological substrates and role during the infection are largely unknown. Using SplA and SplB recombinantly expressed in E. coli, we identified a group of proteins until now unknown to be targeted by SplA and SplB: ubiquitin(-like) specific proteases. Distinct cleavage sites within these targets of SplA and SplB were identified by mass spectrometry and confirmed by site-directed mutagenesis of the target proteins. Since many cellular immune responses are tightly regulated by ubiquitylation, the specific cleavage of involved proteins could represent a role of Spls during infection.

INSTRUMENT(S): Q Exactive Plus, Orbitrap Exploris 480

ORGANISM(S): Staphylococcus Arlettae (ncbitaxon:29378)

SUBMITTER: Leif Steil

PROVIDER: MSV000096077 | MassIVE | Mon Oct 14 05:56:00 BST 2024

REPOSITORIES: MassIVE

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