Mechanical forces regulate the reactivity of a thioester bond in a bacterial adhesin.
Ontology highlight
ABSTRACT: Bacteria must withstand large mechanical shear forces when adhering to and colonizing hosts. Recent structural studies on a class of Gram-positive bacterial adhesins have revealed an intramolecular Cys-Gln thioester bond that can react with surface-associated ligands to covalently anchor to host surfaces. Two other examples of such internal thioester bonds occur in certain anti-proteases and in the immune complement system, both of which react with the ligand only after the thioester bond is exposed by a proteolytic cleavage. We hypothesized that mechanical forces in bacterial adhesion could regulate thioester reactivity to ligand analogously to such proteolytic gating. Studying the pilus tip adhesin Spy0125 of Streptococcus pyogenes, we developed a single molecule assay to unambigu
SUBMITTER: Echelman DJ
PROVIDER: S-EPMC5448130 | biostudies-literature | 2017 May
REPOSITORIES: biostudies-literature
ACCESS DATA