Sortases, Surface Proteins, and Their Roles in Staphylococcus aureus Disease and Vaccine Development.

ABSTRACT: Sortases cleave short peptide motif sequences at the C-terminal end of secreted surface protein precursors and either attach these polypeptides to the peptidoglycan of Gram-positive bacteria or promote their assembly into pilus structures that are also attached to peptidoglycan. Sortase A, the enzyme first identified in the human pathogen Staphylococcus aureus, binds LPXTG motif sorting signals, cleaves between threonine (T) and glycine (G) residues, and forms an acyl enzyme between its active-site cysteine thiol and the carboxyl group of threonine (T). Sortase A acyl enzyme is relieved by the nucleophilic attack of the cross bridge amino group within lipid II, thereby generating surface protein linked to peptidoglycan precursor. Such products are subsequently incorporated into the cell wa

SUBMITTER: Schneewind O 

PROVIDER: S-EPMC6386163 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature