The metalloprotease SepA governs processing of accumulation‐associated protein and shapes intercellular adhesive surface properties in Staphylococcus epidermidis

• DOI: 10.1111/mmi.13594
• Publication Date: 2016-12-20T17:49:33Z
• Authors: Alexandra E. Paharik; Marta Kotasinska; Anna Both; Tra‐My N. Hoang; Henning Büttner; Paroma Roy; Paul D. Fey; Alexander R. Hors...; Holger Rohde
• Keywords: 0301 basic medicine; 03 medical and health sciences; Bacterial Proteins; Biofilms; 4. Education; Polysaccharides, Bacterial; Staphylococcus epidermidis; Metalloendopeptidases; Adhesins, Bacterial; Protein Processing, Post-Translational; Bacterial Adhesion; 3. Good health; Protein Binding

Summary The otherwise harmless skin inhabitant Staphylococcus epidermidis is a major cause of healthcare‐associated medical device infections. species' selective pathogenic potential depends on its production surface adherent biofilms. Cell wall‐anchored protein Aap promotes biofilm formation in S. , independently from the polysaccharide intercellular adhesin PIA. requires proteolytic cleavage to act as an adhesin. Whether and which staphylococcal proteases account for processing yet unknown. Here, evidence provided that PIA‐negative 1457Δ ica metalloprotease SepA required Aap‐dependent static dynamic models. qRT‐PCR protease activity assays demonstrated under standard growth conditions, sepA repressed by global regulator SarA. Inactivation sarA increased production, turn augmented formation. Genetic biochemical analyses SepA‐related induction accumulation resulted enhanced processing. Studies using recombinant proteins able cleave A domain at residue 335 between B domains 601. This study identifies mechanism behind Aap‐mediated maturation, also demonstrates novel role secreted requirement development biofilm.