Structure Activity Relationship of the Stem Peptide in Sortase A Mediated Ligation from Staphylococcus aureus.

ABSTRACT: The surfaces of most Gram-positive bacterial cells, including that of Staphylococcus aureus (S. aureus), are heavily decorated with proteins that coordinate cellular interactions with the extracellular space. In S. aureus, sortase A is the principal enzyme responsible for covalently anchoring proteins, which display the sorting signal LPXTG, onto the peptidoglycan (PG) matrix. Considerable efforts have been made to understand the role of this signal peptide in the sortase-mediated reaction. In contrast, much less is known about how the primary structure of the other substrate involved in the reaction (PG stem peptide) could impact sortase activity. To assess the sortase activity, a library of synthetic analogs of the stem peptide that mimic naturally existing variations found in the S. aur

SUBMITTER: Apostolos AJ 

PROVIDER: S-EPMC9632411 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature