{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T11:54:26Z","timestamp":1790855666650,"version":"4.1.0"},"reference-count":62,"publisher":"Public Library of Science (PLoS)","issue":"9","license":[{"start":{"date-parts":[[2025,9,25]],"date-time":"2025-09-25T00:00:00Z","timestamp":1758758400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"the National Key Research and Development Program of China","award":["2021YFD1800400"],"award-info":[{"award-number":["2021YFD1800400"]}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["32373018"],"award-info":[{"award-number":["32373018"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.plospathogens.org"],"crossmark-restriction":false},"short-container-title":["PLoS Pathog"],"abstract":"<jats:p>\n                    The phagolysosomes of macrophages play a crucial role in eradicating pathogenic microorganisms, but bacteria have evolved sophisticated mechanisms to survive in the acidic environment of phagolysosomes, leading to host infection and subsequent dissemination. However, it is largely unknown how bacteria sense the extracellular stimuli and regulate their acid tolerance capacity to resist the killing by host immune cells. Here, we report the new substrate FadR of the serine\/threonine kinase (STK) in\n                    <jats:italic>Streptococcus suis<\/jats:italic>\n                    serotype 2 (SS2) and demonstrate that the phosphorylation site is Thr230. Notably, FadR phosphorylation significantly enhances the acid resistance of SS2, leading to an increase in the lethality of SS2 in mice, and a marked increase in bacterial load in the blood and various organs, and more severe pathological changes in various organs of the mice. Interestingly, this study further indicated that FadR protein can bind to the promoter of arginine deiminase (\n                    <jats:italic>adi<\/jats:italic>\n                    ), and FadR phosphorylation enhances its binding ability to the\n                    <jats:italic>\n                      <jats:italic>adi<\/jats:italic>\n                    <\/jats:italic>\n                    promoter and increases\n                    <jats:italic>\n                      <jats:italic>adi<\/jats:italic>\n                    <\/jats:italic>\n                    transcription levels. The increase of ADI in SS2 promotes the metabolism of arginine and increases the ammonia content, thus enhancing the acid resistance and intracellular survival capacity of the bacteria in macrophages. Altogether, the research reveals an acid resistance regulatory mechanism that bacteria can utilize the STK-FadR signaling axis to sense changes in the external acidic environment, and then manipulate the ADI system to enhance bacterial resistance to acidic environment or host immunity.\n                  <\/jats:p>","DOI":"10.1371\/journal.ppat.1013534","type":"journal-article","created":{"date-parts":[[2025,9,25]],"date-time":"2025-09-25T17:26:54Z","timestamp":1758821214000},"page":"e1013534","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":4,"title":["STK-mediated FadR phosphorylation regulates the acid resistance and virulence of Streptococcus suis"],"prefix":"10.1371","volume":"21","author":[{"given":"Sen","family":"Li","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhe","family":"Ma","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Huixing","family":"Lin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fei","family":"Pan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hong","family":"Zhou","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jinsheng","family":"Tang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3001-0133","authenticated-orcid":true,"given":"Hongjie","family":"Fan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2025,9,25]]},"reference":[{"issue":"12","key":"ppat.1013534.ref001","doi-asserted-by":"crossref","first-page":"979","DOI":"10.1016\/j.tcb.2020.09.006","article-title":"Lipid Metabolism in Regulation of Macrophage Functions","volume":"30","author":"J Yan","year":"2020","journal-title":"Trends Cell Biol"},{"issue":"4","key":"ppat.1013534.ref002","doi-asserted-by":"crossref","first-page":"767","DOI":"10.1016\/j.cell.2006.01.034","article-title":"Anti-immunology: evasion of the host immune system by bacterial and viral pathogens","volume":"124","author":"BB Finlay","year":"2006","journal-title":"Cell"},{"issue":"8","key":"ppat.1013534.ref003","doi-asserted-by":"crossref","first-page":"1289","DOI":"10.1016\/j.celrep.2015.07.043","article-title":"Genome-wide Reconstruction of OxyR and SoxRS Transcriptional Regulatory Networks under Oxidative Stress in Escherichia coli K-12 MG1655","volume":"12","author":"SW Seo","year":"2015","journal-title":"Cell Rep"},{"issue":"4","key":"ppat.1013534.ref004","doi-asserted-by":"crossref","first-page":"536","DOI":"10.15252\/embj.201695028","article-title":"Mycobacterium tuberculosis protease MarP activates a peptidoglycan hydrolase during acid stress","volume":"36","author":"H Botella","year":"2017","journal-title":"The EMBO Journal"},{"issue":"1","key":"ppat.1013534.ref005","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1016\/j.cell.2013.06.004","article-title":"A bacterial virulence protein promotes pathogenicity by inhibiting the bacterium\u2019s own F1Fo ATP synthase","volume":"154","author":"E-J Lee","year":"2013","journal-title":"Cell"},{"issue":"6","key":"ppat.1013534.ref006","doi-asserted-by":"crossref","DOI":"10.1093\/femsre\/fuac037","article-title":"Bacterial battle against acidity","volume":"46","author":"J Schwarz","year":"2022","journal-title":"FEMS Microbiol Rev"},{"issue":"7","key":"ppat.1013534.ref007","doi-asserted-by":"crossref","first-page":"1484","DOI":"10.1016\/j.biotechadv.2015.06.001","article-title":"Mechanisms of acid tolerance in bacteria and prospects in biotechnology and bioremediation","volume":"33","author":"Y Liu","year":"2015","journal-title":"Biotechnol Adv"},{"issue":"5","key":"ppat.1013534.ref008","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1038\/cr.2013.13","article-title":"L-glutamine provides acid resistance for Escherichia coli through enzymatic release of ammonia","volume":"23","author":"P Lu","year":"2013","journal-title":"Cell Res"},{"issue":"39","key":"ppat.1013534.ref009","doi-asserted-by":"crossref","first-page":"10872","DOI":"10.1073\/pnas.1606360113","article-title":"Comparative proteomics reveal distinct chaperone-client interactions in supporting bacterial acid resistance","volume":"113","author":"S Zhang","year":"2016","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ppat.1013534.ref010","doi-asserted-by":"crossref","first-page":"131227","DOI":"10.1016\/j.biortech.2024.131227","article-title":"An acid-tolerant Clostridium sp. 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