Journal
INFECTION AND IMMUNITY
Volume 84, Issue 1, Pages 99-107Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/IAI.01165-15
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- HHS\ NIH\ National Institute of Allergy and Infectious Diseases (NIAID) [1R01AI120244]
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The fate of the polyubiquitinated protein is determined by the lysine linkages involved in the polymerization of the ubiquitin monomers, which has seven lysine residues (K-6, K-11, K-27, K-29, K-33, K-48, and K-63). The translocated AnkB effector of the intravacuolar pathogen Legionella pneumophila is a bona fide F-box protein, which is localized to the cytosolic side of the Legionella-containing vacuole (LCV) and is essential for intravacuolar proliferation within macrophages and amoebae. The F-box domain of AnkB interacts with the host SCF1 E3 ubiquitin ligase that triggers the decoration of the LCV with K-48-linked polyubiquitinated proteins that are targeted for proteasomal degradation. Here we report that AnkB becomes rapidly polyubiquitinated within the host cell, and this modification is independent of the F-box domain of AnkB, indicating host-mediated polyubiquitination. We show that the AnkB effector interacts specifically with the host E3 ubiquitin ligase Trim21. Mass spectrometry analyses have shown that AnkB is modified by K-11-linked polyubiquitination, which has no effect on its stability. This work shows the first example of K-11-linked polyubiquitination of a bacterial effector and its interaction with the host Trim21 ubiquitin ligase.
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