Publications by authors named "Natalia Stach"

Article Synopsis
  • Research suggests that six proteases in a pathogen's operon are linked to its virulence, with SplA, B, D, and E showing unique substrate preferences while SplF's characteristics were previously unclear.
  • The study establishes a method for expressing the SplF protease and investigates its substrate specificity using peptide libraries, highlighting its preference for long aliphatic sidechains and aromatic residues.
  • A high-resolution crystal structure of SplF was created to explain its substrate specificity, revealing that this operon contains a distinct extracellular proteolytic system compared to other known Spl proteases.
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Staphylococcus aureus is a dangerous human pathogen characterized by alarmingly increasing antibiotic resistance. Accumulating evidence suggests the role of Spl proteases in staphylococcal virulence. Spl proteases have restricted, non-overlapping substrate specificity, suggesting that they may constitute a first example of a proteolytic system in bacteria.

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Objective: Staphylococcus aureus (S. aureus) infection is known to contribute to the severity and recalcitrance of chronic rhinosinusitis (CRS), and its secreted products have been shown to alter the airway barrier. Extracellular proteases secreted by S.

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Staphylococcal SplB protease belongs to the chymotrypsin family. Chymotrypsin zymogen is activated by proteolytic processing at the N terminus, resulting in significant structural rearrangement at the active site. Here, we demonstrate that the molecular mechanism of SplB protease activation differs significantly and we characterize the novel mechanism in detail.

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Staphylococcus aureus is a dangerous human pathogen characterized by growing antibiotic resistance. Virulence of S. aureus relies on a variety of secreted and cell surface associated virulence factors among which certain proteolytic enzymes play an important role.

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Staphylococcus aureus is a dangerous human pathogen. A number of the proteins secreted by this bacterium are implicated in its virulence, but many of the components of its secretome are poorly characterized. Strains of S.

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