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FIH-mediated post-translational modification through asparaginyl hydroxylation of eukaryotic proteins impacts regulation of protein-protein interaction. We have identified the FIH recognition motif in 11  Legionella pneumophila  translocated effectors, YopM of  Yersinia , IpaH4.5 of  Shigella  and an ankyrin protein of  Rickettsia . Mass spectrometry analyses of the AnkB and AnkH effectors of  L. pneumophila  confirm their asparaginyl hydroxylation. Consistent with localization of the AnkB effector to the  Legionella -containing vacuole (LCV) membrane and its modification by FIH, our data show that FIH and its two interacting proteins, Mint3 and MT1-MMP are acquired by the LCV in a Dot/Icm type IV secretion-dependent manner. Chemical inhibition or RNAi-mediated knockdown of FIH promotes LCV-lysosomes fusion, diminishes decoration of the LCV with polyubiquitinated proteins, and abolishes intra-vacuolar replication of  L. pneumophila . These data show acquisition of the host FIH by a pathogen-containing vacuole and that asparaginyl-hydroxylation of translocated effectors is indispensable for their function.

Host FIH-Mediated Asparaginyl Hydroxylation of Translocated Legionella pneumophila Effectors