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U.S.A."],"published-print":{"date-parts":[[2022,1,5]]},"abstract":"<jats:title>Significance<\/jats:title>\n                  <jats:p>\n                    Many effectors of the\n                    <jats:italic>Coxiella burnetii<\/jats:italic>\n                    Dot\/Icm transporter are important for its virulence, but the lack of understanding of their biochemical activity prevents the use of them as potential therapeutic targets. Here, we found that the effector Cbu0513 (CinF) is a protein phosphatase that attacks I\u03baB\u03b1, a key regulatory protein in NF-\u03baB signaling. Unlike its homologs such as ST0318 from the archaeon\n                    <jats:italic>Sulfolobus tokodaii<\/jats:italic>\n                    , CinF has lost the enzymatic activity as a fructose-1,6-bisphosphate aldolase\/phosphatase. Instead, it specifically targets I\u03baB\u03b1 to make it resistant to proteasome-mediated degradation in cells stimulated with NF-\u03baB agonists. Our finding has expanded the strategy used by bacterial pathogens to inhibit host immunity, which may provide leads for the development of immune modulators for disease treatment.\n                  <\/jats:p>","DOI":"10.1073\/pnas.2110877119","type":"journal-article","created":{"date-parts":[[2021,12,20]],"date-time":"2021-12-20T16:32:12Z","timestamp":1640017932000},"update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":308,"title":["<i>Coxiella burnetii<\/i>\n                    inhibits host immunity by a protein phosphatase adapted from glycolysis"],"prefix":"10.1073","volume":"119","author":[{"given":"Yong","family":"Zhang","sequence":"first","affiliation":[{"name":"Department of Respiratory Medicine, Center for Pathogen Biology and Infectious Diseases, Key Laboratory of Organ Regeneration and Transplantation of the Ministry of Education, State Key Laboratory for Zoonotic Diseases, The First Hospital of Jilin University, Changchun 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