The serine-rich C-terminal tail of the Listeria monocytogenes secretion chaperone PrsA2 is critical for bacterial virulence and resistance to cell-wall active antibiotics.

The serine-rich C-terminal tail of PrsA2 is essential for Listeria monocytogenes virulence, secreted toxin activity, and resistance to cell-wall antibiotics, with a critical role in folding LLO.

• Why it matters: Understanding how bacterial chaperones contribute to virulence and antibiotic resistance can reveal new targets for infection control. The specific functions of PrsA2’s unstructured regions were previously unclear, limiting insights into its role in pathogenesis.
• What they did: Researchers examined the PrsA2 C-tail by creating mutants lacking the serine-rich tail and used biophysical, biochemical, and infection models to assess its impact on bacterial virulence, toxin folding, and stress survival.
• The result: The C-tail is vital for PrsA2’s interaction with LLO, promoting toxin activity, bacterial virulence, and resistance to cell-wall-targeting antibiotics, highlighting its potential as a therapeutic target.