{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,25]],"date-time":"2026-03-25T00:45:22Z","timestamp":1774399522446,"version":"3.50.1"},"reference-count":47,"publisher":"American Society for Microbiology","issue":"5","license":[{"start":{"date-parts":[[2010,5,1]],"date-time":"2010-05-01T00:00:00Z","timestamp":1272672000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Infect Immun"],"published-print":{"date-parts":[[2010,5]]},"abstract":"<jats:title>ABSTRACT<\/jats:title><jats:p>The Dot\/Icm-translocated ankyrin B (AnkB) effector of<jats:italic>Legionella pneumophila<\/jats:italic>exhibits molecular mimicry of eukaryotic F-box proteins and is essential for intracellular replication in macrophages and protozoa. In addition to two eukaryotic-like ankyrin (ANK) domains, AnkB harbors a conserved eukaryotic F-box domain, which is involved in polyubiquitination of proteins throughout the eukaryotic kingdom. We have recently shown that the F-box domain of the AnkB effector is essential for decoration of the<jats:italic>Legionella<\/jats:italic>-containing vacuole (LCV) with polyubiquitinated proteins within macrophages and protozoan hosts. To decipher the role of the two ANK domains in the function of AnkB, we have constructed in-frame deletion of either or both of the ANK domain-encoding regions (<jats:italic>ankB<\/jats:italic>\u0394<jats:italic>A1<\/jats:italic>,<jats:italic>ankB<\/jats:italic>\u0394<jats:italic>A2<\/jats:italic>, and<jats:italic>ankB<\/jats:italic>\u0394<jats:italic>A1A2<\/jats:italic>) to<jats:italic>trans<\/jats:italic>-complement the<jats:italic>ankB<\/jats:italic>null mutant. Deletion of the ANK domains results in defects in intracellular proliferation and decoration of the LCV with polyubiquitinated proteins. Export of the truncated variants of AnkB was reduced, and this may account for the observed defects. However, while full-length AnkB ectopically expressed in mammalian cells<jats:italic>trans<\/jats:italic>-rescues the<jats:italic>ankB<\/jats:italic>null mutant for intracellular proliferation, ectopic expression of AnkB\u0394A1, AnkB\u0394A2, and AnkB\u0394A1A2 fails to<jats:italic>trans<\/jats:italic>-rescue the<jats:italic>ankB<\/jats:italic>null mutant. Importantly, ectopically expressed full-length AnkB is targeted to the host cell plasma membrane, where it recruits polyubiquitinated proteins. In contrast, AnkB\u0394A1, AnkB\u0394A2, and AnkB\u0394A1A2 are diffusely distributed throughout the cytosol and fail to recruit polyubiquitinated proteins. We conclude that the two eukaryotic-like ANK domains of AnkB are essential for intracellular proliferation, for targeting AnkB to the host membranes, and for decoration of the LCV with polyubiquitinated proteins.<\/jats:p>","DOI":"10.1128\/iai.01450-09","type":"journal-article","created":{"date-parts":[[2010,3,2]],"date-time":"2010-03-02T04:34:14Z","timestamp":1267504454000},"page":"2079-2088","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":50,"title":["Indispensable Role for the Eukaryotic-Like Ankyrin Domains of the Ankyrin B Effector of<i>Legionella pneumophila<\/i>within Macrophages and Amoebae"],"prefix":"10.1128","volume":"78","author":[{"given":"Christopher T. 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