Legionella pneumophila inhibits immune signalling via MavC-mediated transglutaminase-induced ubiquitination of UBE2N.

ABSTRACT: The bacterial pathogen Legionella pneumophila modulates host immunity using effectors translocated by its Dot/Icm transporter to facilitate its intracellular replication. A number of these effectors employ diverse mechanisms to interfere with protein ubiquitination, a post-translational modification essential for immunity. Here, we have found that L. pneumophila induces monoubiquitination of the E2 enzyme UBE2N by its Dot/Icm substrate MavC(Lpg2147). We demonstrate that MavC is a transglutaminase that catalyses covalent linkage of ubiquitin to Lys₉₂ and Lys₉₄ of UBE2N via Gln₄₀. Similar to canonical transglutaminases, MavC possess deamidase activity that targets ubiquitin at Gln₄₀. We identified Cys₇₄ as the catalytic residue for both

SUBMITTER: Gan N 

PROVIDER: S-EPMC6294664 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature