Listeria monocytogenes was known to induce histone H3 deacetylation in infected epithelial cells, but the underlying mechanisms were unclear. A new study shows that L. monocytogenes infection leads to the deacetylation of H3 lysine 18 (H3K18) and that this modification depends on nuclear translocation of the host histone deacetylase SIRT2. Mutant L. monocytogenes lacking the surface protein internalin B (InlB) did not induce SIRT2 translocation or H3K18 deacetylation. Importantly, inlB-null L. monocytogenes also produced fewer colony-forming units than wild-type bacteria in mice, indicating that histone deacetylation is central for virulence.
Eskandarian, H. A. et al. A role for SIRT2-dependent histone H3K18 deacetylation in bacterial infection. Science 341, 6145 (2013)