{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T21:24:50Z","timestamp":1791149090372,"version":"4.1.0"},"reference-count":42,"publisher":"American Society for Microbiology","issue":"6","license":[{"start":{"date-parts":[[2013,6,1]],"date-time":"2013-06-01T00:00:00Z","timestamp":1370044800000},"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":[[2013,6]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            When the bacterium\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Legionella pneumophila<\/jats:named-content>\n            , the causative agent of Legionnaires' disease, is phagocytosed by alveolar macrophages, it delivers a large number of effector proteins through its Dot\/Icm type IV secretion system into the host cell cytosol. Among those proteins is LidA, an effector that interacts with several host GTPases of the Rab family, including Rab6A\u2032, a regulator of retrograde vesicle trafficking within eukaryotic cells. The effect of LidA on Rab6A\u2032 function and the role of Rab6A\u2032 for\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            growth within host cells has been unclear. Here, we show that LidA preferentially binds Rab6A\u2032 in the active GTP-bound conformation. Rab6 binding occurred through the central region of LidA and followed a stoichiometry for LidA and Rab6A\u2032 of 1:2. LidA maintained Rab6A\u2032 in the active conformation by efficiently blocking the hydrolysis of GTP by Rab6A\u2032, even in the presence of cellular GTPase-activating proteins, suggesting that the function of Rab6A\u2032 must be important for efficient intracellular replication of\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            . Accordingly, we found that production of constitutively inactive Rab6A\u2032(T27N) but not constitutively active Rab6A\u2032(Q72L) significantly reduced the ability of\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 initiate intracellular replication in human macrophages. Thus, the presence of an active pool of Rab6 within host cells early during infection is required to support efficient intracellular growth of\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            .\n          <\/jats:p>","DOI":"10.1128\/iai.00157-13","type":"journal-article","created":{"date-parts":[[2013,4,9]],"date-time":"2013-04-09T02:22:40Z","timestamp":1365474160000},"page":"2226-2235","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":23,"title":["Targeting of the Small GTPase Rab6A\u2032 by the Legionella pneumophila Effector LidA"],"prefix":"10.1128","volume":"81","author":[{"given":"Yang","family":"Chen","sequence":"first","affiliation":[{"name":"Cell Biology and Metabolism Program, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes 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