{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,26]],"date-time":"2026-08-26T08:21:00Z","timestamp":1787732460846,"version":"build-2784847793"},"reference-count":79,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2026,8,16]],"date-time":"2026-08-16T00:00:00Z","timestamp":1786838400000},"content-version":"vor","delay-in-days":15,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/100008439","name":"Texas Christian University","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100008439","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["MicrobiologyOpen"],"published-print":{"date-parts":[[2026,8]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    ClpX functions as a component of the ClpXP protease, a conserved intracellular protease that regulates protein turnover, stress responses, and virulence in multiple bacterial species. Our lab has established that\n                    <jats:italic>clpX<\/jats:italic>\n                    is necessary for resistance to cell envelope targeting antibiotics, such as penicillin and daptomycin in\n                    <jats:italic>Bacillus anthracis<\/jats:italic>\n                    Sterne. Previous microarray data identified the\n                    <jats:italic>msrA\/B<\/jats:italic>\n                    gene encoding a bifunctional methionine sulfoxide reductase as upregulated in the \u0394\n                    <jats:italic>clpX<\/jats:italic>\n                    mutant. Methionine sulfoxide reductases (Msr) repair oxidatively damaged proteins by reducing methionine sulfoxide residues back to methionine. While Msr enzymes are primarily associated with oxidative stress, cell wall antibiotics induce expression of\n                    <jats:italic>msrA1<\/jats:italic>\n                    and\n                    <jats:italic>msrB<\/jats:italic>\n                    in\n                    <jats:italic>S. aureus<\/jats:italic>\n                    . Here, we investigated the role of MsrA\/B in oxidative and cell envelope stress. Our results show that although hydrogen peroxide and paraquat induce\n                    <jats:italic>msrA\/B<\/jats:italic>\n                    expression, the \u0394\n                    <jats:italic>msrA\/B<\/jats:italic>\n                    strain was not susceptible to either oxidant, whereas the \u0394\n                    <jats:italic>clpX<\/jats:italic>\n                    strain was sensitive to both. We also found that loss of\n                    <jats:italic>msrA\/B<\/jats:italic>\n                    conferred penicillin\u2010specific sensitivity, but, unlike \u0394\n                    <jats:italic>clpX<\/jats:italic>\n                    , increased sensitivity was not seen with other cell wall or cell membrane targeting antibiotics. Inactivation of the catalytic cysteine of either Msr domain of MsrA\/B failed to complement, suggesting that the reducing activity of MsrA\/B is required for penicillin resistance. These findings indicate that while MsrA\/B contributes to penicillin resistance, other proteins in the ClpXP modulon must also play a role in oxidative and cell envelope stress.\n                  <\/jats:p>","DOI":"10.1002\/mbo3.70377","type":"journal-article","created":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T05:31:40Z","timestamp":1786944700000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Role of ClpX and MsrA\/B in the Oxidative and Cell Wall Stress Response in\n                    <i>Bacillus anthracis<\/i>\n                    Sterne"],"prefix":"10.1002","volume":"15","author":[{"given":"Aeron B.","family":"Pennington","sequence":"first","affiliation":[{"name":"Department of Biology Texas Christian University Fort Worth Texas USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Salina","family":"Hona","sequence":"additional","affiliation":[{"name":"Department of Biology Texas Christian University Fort Worth Texas USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Josey I.","family":"Austin","sequence":"additional","affiliation":[{"name":"Department of Biology Texas Christian University Fort Worth Texas USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kelsey C.","family":"Waite","sequence":"additional","affiliation":[{"name":"Department of Biology Texas Christian University Fort Worth Texas USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0809-9469","authenticated-orcid":false,"given":"Mikaela D.","family":"Stewart","sequence":"additional","affiliation":[{"name":"Department of Biology Texas Christian University Fort Worth Texas USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8863-1522","authenticated-orcid":false,"given":"Shauna M.","family":"McGillivray","sequence":"additional","affiliation":[{"name":"Department of 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