Type IX Secretion Substrates Are Cleaved and Modified by a Sortase-Like Mechanism

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Chronic periodontitis, associated with the pathogen Porphyromonas gingivalis, is a major public health problem. P. gingivalis secretes virulence factors including the gingipains via the type IX secretion system (T9SS). These proteins contain a C-terminal signal that allows their secretion through the T9SS and it is cleaved by the protein PG0026 at the cell surface. Here we identify a mechanism by which gingipains and other proteins attach to the cell surface of this bacterium. We found that after removal of the C-terminal signal, the proteins were modified via a peptide linkage to either a putative component of anionic lipopolysaccharide (A-LPS) in the wild type or peptides from the growth medium in mutants lacking A-LPS, which has been suggested to anchor the proteins to the cell surface. Results from this study provide evidence for the exact site of modification of these proteins with A-LPS. Furthermore, our results also demonstrate for the first time that the anchoring mechanism of this secretion system involves a substitution between the signal and the anchor (A-LPS) which can be explained by the action of a single enzyme known as a sortase, which we believe is PG0026. This is the first evidence for a sortase-like mechanism in Gram-negative bacteria.

Vyšlo v časopise: Type IX Secretion Substrates Are Cleaved and Modified by a Sortase-Like Mechanism. PLoS Pathog 11(9): e32767. doi:10.1371/journal.ppat.1005152
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.ppat.1005152

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