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Crucial to the pathogenesis of this intracellular pathogen is its ability to subvert host cell defenses, permitting intracellular replication in specialized vacuoles within host cells. The Dot\/Icm type IV secretion system (T4SS), which translocates a large number of bacterial effectors into host cell, is absolutely required for rerouting the\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Legionella<\/jats:named-content>\n            phagosome. Many\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Legionella<\/jats:named-content>\n            effectors display distinctive eukaryotic domains, among which are protein kinase domains.\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">In silico<\/jats:named-content>\n            analysis and\n            <jats:italic>in vitro<\/jats:italic>\n            phosphorylation assays identified five functional protein kinases, LegK1 to LegK5, encoded by the epidemic\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">L. pneumophila<\/jats:named-content>\n            Lens strain. Except for LegK5, the\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Legionella<\/jats:named-content>\n            protein kinases are all T4SS effectors. LegK2 plays a key role in bacterial virulence, as demonstrated by gene inactivation. The\n            <jats:italic>legK2<\/jats:italic>\n            mutant containing vacuoles displays less-efficient recruitment of endoplasmic reticulum markers, which results in delayed intracellular replication. Considering that a kinase-dead substitution mutant of\n            <jats:italic>legK2<\/jats:italic>\n            exhibits the same virulence defects, we highlight here a new molecular mechanism, namely, protein phosphorylation, developed by\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">L. pneumophila<\/jats:named-content>\n            to establish a replicative niche and evade host cell defenses.\n          <\/jats:p>","DOI":"10.1128\/iai.00805-10","type":"journal-article","created":{"date-parts":[[2011,2,15]],"date-time":"2011-02-15T09:12:54Z","timestamp":1297761174000},"page":"1936-1950","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":96,"title":["Protein Kinase LegK2 Is a Type IV Secretion System Effector Involved in Endoplasmic Reticulum Recruitment and Intracellular Replication of Legionella 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