{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T01:31:11Z","timestamp":1791250271488,"version":"4.1.0"},"reference-count":57,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2013,4,8]],"date-time":"2013-04-08T00:00:00Z","timestamp":1365379200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Eur J Immunol"],"published-print":{"date-parts":[[2013,5]]},"abstract":"<jats:p><jats:italic>Legionella pneumophila<\/jats:italic> (<jats:italic>L<\/jats:italic><jats:italic>. pneumophila<\/jats:italic>) is an intracellular bacterium of human alveolar macrophages that causes Legionnaires\u2019 disease. In contrast to humans, most inbred mouse strains are restrictive to <jats:italic>L<\/jats:italic>. <jats:italic>pneumophila<\/jats:italic> replication. We demonstrate that autophagy targets <jats:italic>L<\/jats:italic>. <jats:italic>pneumophila<\/jats:italic> vacuoles to lysosomes and that this process requires ubiquitination of <jats:italic>L<\/jats:italic>. <jats:italic>pneumophila<\/jats:italic> vacuoles and the subsequent binding of the autophagic adaptor p62\/<jats:styled-content style=\"fixed-case\">SQSTM<\/jats:styled-content>1 to ubiquitinated vacuoles. The <jats:italic>L<\/jats:italic>. <jats:italic>pneumophila leg<\/jats:italic><jats:italic>A<\/jats:italic><jats:italic>9<\/jats:italic> encodes for an ankyrin\u2010containing protein with unknown role. We show that the <jats:italic>leg<\/jats:italic><jats:italic>A<\/jats:italic><jats:italic>9<\/jats:italic> mutant replicate in <jats:styled-content style=\"fixed-case\">WT<\/jats:styled-content> mice and their bone marrow\u2010derived macrophages. This is the first <jats:italic>L<\/jats:italic>. <jats:italic>pneumophila<\/jats:italic> mutant to be found to replicate in <jats:styled-content style=\"fixed-case\">WT<\/jats:styled-content> bone marrow\u2010derived macrophages other than the <jats:styled-content style=\"fixed-case\">F<\/jats:styled-content>la mutant. Less <jats:italic>leg<\/jats:italic><jats:italic>A<\/jats:italic><jats:italic>9<\/jats:italic> mutant\u2010containing vacuoles acquired ubiquitin labeling and p62\/<jats:styled-content style=\"fixed-case\">SQSTM<\/jats:styled-content>1 staining, evading autophagy uptake and avoiding lysosomal fusion. Thus, we describe a bacterial protein that targets the <jats:italic>L<\/jats:italic>. <jats:italic>pneumophila<\/jats:italic>\u2010containing vacuole for autophagy uptake.<\/jats:p>","DOI":"10.1002\/eji.201242835","type":"journal-article","created":{"date-parts":[[2013,2,19]],"date-time":"2013-02-19T16:35:53Z","timestamp":1361291753000},"page":"1333-1344","source":"Crossref","is-referenced-by-count":53,"title":["A bacterial protein promotes the recognition of the <i>L<\/i><i>egionella pneumophila<\/i> vacuole by autophagy"],"prefix":"10.1002","volume":"43","author":[{"given":"Arwa A.","family":"Khweek","sequence":"first","affiliation":[{"name":"Department of Microbial Infection and Immunity Center for Microbial Interface Biology  Columbus OH USA"},{"name":"Department of Internal Medicine College of Medicine, and The Ohio State University  Columbus OH 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