A Copper-Responsive Two-Component System Governs Lipoprotein Remodeling in Listeria monocytogenes.

ABSTRACT: Bacterial lipoproteins are membrane-associated proteins with a characteristic acylated N-terminal cysteine residue anchoring C-terminal globular domains to the membrane surface. While all lipoproteins are modified with acyl chains, the number, length, and position can vary depending on host. The acylation pattern also alters ligand recognition by the Toll-like receptor 2 (TLR2) protein family, a signaling system that is central to bacterial surveillance and innate immunity. In select Listeria monocytogenes isolates carrying certain plasmids, copper exposure converts the lipoprotein chemotype into a weak TLR2 ligand through expression of the enzyme lipoprotein intramolecular acyltransferase (Lit). In this study, we identify the response regulator (CopR) from a heavy metal-sensing two-compon

SUBMITTER: Komazin G 

PROVIDER: S-EPMC9879112 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature