Anchoring surface proteins to the bacterial cell wall by sortase enzymes: how it started and what we know now

Curr Opin Microbiol. 2021 Feb 18;60:73-79. doi: 10.1016/j.mib.2021.01.013. Online ahead of print.ABSTRACTIn Gram-positive bacteria, the peptidoglycan serves as a placeholder for surface display of a unique class of monomeric and polymeric proteins, or pili - the precursors of which harbor a cell wall sorting signal with LPXTG motif that is recognized by a conserved transpeptidase enzyme called sortase. Since this original discovery over two decades ago, extensive genetic, biochemical and structural studies have illuminated the basic mechanisms of sortase-mediated cell wall anchoring of surface proteins and pili. We now know how LPXTG-containing surface proteins are folded post-translocationally, how sortase enzymes recognize substrates, and how a remnant of the cell wall sorting signal modulates intramembrane signaling. In this review, we will highlight new findings from a few model experimental paradigms and present future prospects for the field.PMID:33611145 | DOI:10.1016/j.mib.2021.01.013

Source: Current Opinion in Microbiology - February 21, 2021 Category: Microbiology Authors: Aadil H Bhat Minh Tan Nguyen Asis Das Hung Ton-That Source Type: research