{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,22]],"date-time":"2026-10-22T06:50:17Z","timestamp":1792651817946,"version":"4.5.0"},"reference-count":45,"publisher":"National Academy of Sciences","issue":"20","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2012,5,15]]},"abstract":"<jats:p>\n                    The intracellular pathogen\n                    <jats:italic>Mycobacterium tuberculosis<\/jats:italic>\n                    (\n                    <jats:italic>Mtb<\/jats:italic>\n                    ) causes tuberculosis. Enhanced intracellular survival (Eis) protein, secreted by\n                    <jats:italic>Mtb<\/jats:italic>\n                    , enhances survival of\n                    <jats:italic>Mycobacterium smegmatis<\/jats:italic>\n                    (\n                    <jats:italic>Msm<\/jats:italic>\n                    ) in macrophages.\n                    <jats:italic>Mtb<\/jats:italic>\n                    Eis was shown to suppress host immune defenses by negatively modulating autophagy, inflammation, and cell death through JNK-dependent inhibition of reactive oxygen species (ROS) generation.\n                    <jats:italic>Mtb<\/jats:italic>\n                    Eis was recently demonstrated to contribute to drug resistance by acetylating multiple amines of aminoglycosides. However, the mechanism of enhanced intracellular survival by\n                    <jats:italic>Mtb<\/jats:italic>\n                    Eis remains unanswered. Therefore, we have characterized both\n                    <jats:italic>Mtb<\/jats:italic>\n                    and\n                    <jats:italic>Msm<\/jats:italic>\n                    Eis proteins biochemically and structurally. We have discovered that\n                    <jats:italic>Mtb<\/jats:italic>\n                    Eis is an efficient\n                    <jats:italic>N<\/jats:italic>\n                    <jats:sup>\u025b<\/jats:sup>\n                    -acetyltransferase, rapidly acetylating Lys55 of dual-specificity protein phosphatase 16 (DUSP16)\/mitogen-activated protein kinase phosphatase-7 (MKP-7), a JNK-specific phosphatase. In contrast,\n                    <jats:italic>Msm<\/jats:italic>\n                    Eis is more efficient as an\n                    <jats:italic>N<\/jats:italic>\n                    <jats:sup>\u03b1<\/jats:sup>\n                    -acetyltransferase. We also show that\n                    <jats:italic>Msm<\/jats:italic>\n                    Eis acetylates aminoglycosides as readily as\n                    <jats:italic>Mtb<\/jats:italic>\n                    Eis. Furthermore,\n                    <jats:italic>Mtb<\/jats:italic>\n                    Eis, but not\n                    <jats:italic>Msm<\/jats:italic>\n                    Eis, inhibits LPS-induced JNK phosphorylation. This functional difference against DUSP16\/MKP-7 can be understood by comparing the structures of two Eis proteins. The active site of\n                    <jats:italic>Mtb<\/jats:italic>\n                    Eis with a narrow channel seems more suitable for sequence-specific recognition of the protein substrate than the pocket-shaped active site of\n                    <jats:italic>Msm<\/jats:italic>\n                    Eis. We propose that\n                    <jats:italic>Mtb<\/jats:italic>\n                    Eis initiates the inhibition of JNK-dependent autophagy, phagosome maturation, and ROS generation by acetylating DUSP16\/MKP-7. Our work thus provides insight into the mechanism of suppressing host immune responses and enhancing mycobacterial survival within macrophages by\n                    <jats:italic>Mtb<\/jats:italic>\n                    Eis.\n                  <\/jats:p>","DOI":"10.1073\/pnas.1120251109","type":"journal-article","created":{"date-parts":[[2012,5,1]],"date-time":"2012-05-01T00:46:44Z","timestamp":1335833204000},"page":"7729-7734","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":192,"title":["<i>Mycobacterium tuberculosis<\/i>\n                    Eis protein initiates suppression of host immune responses by acetylation of DUSP16\/MKP-7"],"prefix":"10.1073","volume":"109","author":[{"given":"Kyoung Hoon","family":"Kim","sequence":"first","affiliation":[{"name":"Departments of aChemistry and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Doo Ri","family":"An","sequence":"additional","affiliation":[{"name":"Biophysics and Chemical Biology, College of Natural Sciences, Seoul National University, Seoul 151-742, Korea;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jinsu","family":"Song","sequence":"additional","affiliation":[{"name":"Departments of aChemistry and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ji Young","family":"Yoon","sequence":"additional","affiliation":[{"name":"Departments of aChemistry and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hyoun Sook","family":"Kim","sequence":"additional","affiliation":[{"name":"Departments of aChemistry and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hye Jin","family":"Yoon","sequence":"additional","affiliation":[{"name":"Departments of aChemistry and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ha Na","family":"Im","sequence":"additional","affiliation":[{"name":"Biophysics and Chemical Biology, College of Natural Sciences, Seoul National University, Seoul 151-742, Korea;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jieun","family":"Kim","sequence":"additional","affiliation":[{"name":"Biophysics and Chemical Biology, College of Natural Sciences, Seoul National University, Seoul 151-742, Korea;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Do Jin","family":"Kim","sequence":"additional","affiliation":[{"name":"Departments of aChemistry and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sang Jae","family":"Lee","sequence":"additional","affiliation":[{"name":"Departments of aChemistry and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ki-Hye","family":"Kim","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Chungnam National University School of Medicine, Daejeon 301-747, Korea; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hye-Mi","family":"Lee","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Chungnam National University School of Medicine, Daejeon 301-747, Korea; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hie-Joon","family":"Kim","sequence":"additional","affiliation":[{"name":"Departments of aChemistry and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eun-Kyeong","family":"Jo","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Chungnam National University School of Medicine, Daejeon 301-747, Korea; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jae Young","family":"Lee","sequence":"additional","affiliation":[{"name":"Department of Life Science, Dongguk University-Seoul, Seoul 100-712, Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Se Won","family":"Suh","sequence":"additional","affiliation":[{"name":"Departments of aChemistry and"},{"name":"Biophysics and Chemical Biology, College of Natural Sciences, Seoul National University, Seoul 151-742, Korea;"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2012,4,30]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"856","DOI":"10.1126\/science.1185449","article-title":"The population dynamics and control of tuberculosis","volume":"328","author":"Dye C","year":"2010","unstructured":"C Dye, BG Williams, The population dynamics and control of tuberculosis. 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