{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T03:47:12Z","timestamp":1790048832128,"version":"4.0.1"},"reference-count":43,"publisher":"American Society for Microbiology","issue":"7","license":[{"start":{"date-parts":[[2017,7,1]],"date-time":"2017-07-01T00:00:00Z","timestamp":1498867200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"name":"University of Otago Research Committee"},{"name":"Otago School of Medical Sciences Dean's bequest fund"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Infect Immun"],"published-print":{"date-parts":[[2017,7]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The bacterial pathogen\n            <jats:named-content content-type=\"genus-species\">Listeria monocytogenes<\/jats:named-content>\n            causes foodborne illnesses resulting in gastroenteritis, meningitis, or abortion.\n            <jats:named-content content-type=\"genus-species\">Listeria<\/jats:named-content>\n            induces its internalization into some human cells through interaction of the bacterial surface protein InlB with the host receptor tyrosine kinase Met. InlB-dependent entry requires localized polymerization of the host actin cytoskeleton. The signal transduction pathways that act downstream of Met to regulate actin filament assembly or other processes during\n            <jats:named-content content-type=\"genus-species\">Listeria<\/jats:named-content>\n            uptake remain incompletely characterized. Here, we demonstrate important roles for the human serine\/threonine kinases mTOR and protein kinase C-\u03b1 (PKC-\u03b1) in InlB-dependent entry. Experiments involving RNA interference (RNAi) indicated that two multiprotein complexes containing mTOR, mTORC1 and mTORC2, are each needed for efficient internalization of\n            <jats:named-content content-type=\"genus-species\">Listeria<\/jats:named-content>\n            into cells of the human cell line HeLa. InlB stimulated Met-dependent phosphorylation of mTORC1 or mTORC2 substrates, demonstrating activation of both mTOR-containing complexes. RNAi studies indicated that the mTORC1 effectors 4E-BP1 and hypoxia-inducible factor 1\u03b1 (HIF-1\u03b1) and the mTORC2 substrate PKC-\u03b1 each control\n            <jats:named-content content-type=\"genus-species\">Listeria<\/jats:named-content>\n            uptake. Genetic or pharmacological inhibition of PKC-\u03b1 reduced the internalization of\n            <jats:named-content content-type=\"genus-species\">Listeria<\/jats:named-content>\n            and the accumulation of actin filaments that normally accompanies InlB-mediated entry. Collectively, our results identify mTOR and PKC-\u03b1 to be host factors exploited by\n            <jats:named-content content-type=\"genus-species\">Listeria<\/jats:named-content>\n            to promote infection. PKC-\u03b1 controls\n            <jats:named-content content-type=\"genus-species\">Listeria<\/jats:named-content>\n            entry, at least in part, by regulating the actin cytoskeleton downstream of the Met receptor.\n          <\/jats:p>","DOI":"10.1128\/iai.00087-17","type":"journal-article","created":{"date-parts":[[2017,5,2]],"date-time":"2017-05-02T00:20:41Z","timestamp":1493684441000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":25,"title":["Host Serine\/Threonine Kinases mTOR and Protein Kinase C-\u03b1 Promote InlB-Mediated Entry of Listeria monocytogenes"],"prefix":"10.1128","volume":"85","author":[{"given":"Manmeet","family":"Bhalla","sequence":"first","affiliation":[{"name":"Department of Microbiology and Immunology, University of Otago, Dunedin, New 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