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PBP2A can catalyze\n            <jats:sc>dd<\/jats:sc>\n            -transpeptidation of peptidoglycan (PG) because of its low affinity for \u03b2-lactam antibiotics and can functionally cooperate with the PBP2 transglycosylase in the biosynthesis of PG. Here, we focus upon the role of the membrane-bound PrsA foldase protein as a regulator of \u03b2-lactam resistance expression. Deletion of\n            <jats:italic>prsA<\/jats:italic>\n            altered oxacillin resistance in three different SCC\n            <jats:italic>mec<\/jats:italic>\n            backgrounds and, more importantly, caused a decrease in PBP2A membrane amounts without affecting\n            <jats:italic>mecA<\/jats:italic>\n            mRNA levels. The N- and C-terminal domains of PrsA were found to be critical features for PBP2A protein membrane levels and oxacillin resistance. We propose that PrsA has a role in posttranscriptional maturation of PBP2A, possibly in the export and\/or folding of newly synthesized PBP2A. This additional level of control in the expression of the\n            <jats:italic>mecA<\/jats:italic>\n            -dependent MRSA phenotype constitutes an opportunity to expand the strategies to design anti-infective agents.\n          <\/jats:p>","DOI":"10.1128\/aac.02333-15","type":"journal-article","created":{"date-parts":[[2015,12,29]],"date-time":"2015-12-29T03:23:15Z","timestamp":1451359395000},"page":"1656-1666","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":61,"title":["The Staphylococcus aureus Chaperone PrsA Is a New Auxiliary Factor of Oxacillin Resistance Affecting Penicillin-Binding Protein 2A"],"prefix":"10.1128","volume":"60","author":[{"given":"Ambre","family":"Jousselin","sequence":"first","affiliation":[{"name":"Infectious Diseases Service, University Hospital and Medical School of Geneva, Geneva, Switzerland"},{"name":"Laboratory of Bacterial Cell Biology, Instituto de Tecnologia Qu\u00edmica e Biol\u00f3gica Ant\u00f3nio Xavier, Universidade Nova de Lisboa, Oeiras, Portugal"}]},{"given":"Caroline","family":"Manzano","sequence":"additional","affiliation":[{"name":"Infectious Diseases Service, University Hospital and Medical School of Geneva, Geneva, Switzerland"}]},{"given":"Alexandra","family":"Biette","sequence":"additional","affiliation":[{"name":"Infectious Diseases Service, University Hospital and Medical School of Geneva, Geneva, Switzerland"}]},{"given":"Patricia","family":"Reed","sequence":"additional","affiliation":[{"name":"Laboratory of Bacterial Cell Biology, Instituto de Tecnologia Qu\u00edmica e Biol\u00f3gica Ant\u00f3nio Xavier, Universidade Nova de Lisboa, Oeiras, Portugal"}]},{"given":"Mariana G.","family":"Pinho","sequence":"additional","affiliation":[{"name":"Laboratory of Bacterial Cell Biology, Instituto de Tecnologia Qu\u00edmica e Biol\u00f3gica Ant\u00f3nio Xavier, Universidade Nova de Lisboa, Oeiras, Portugal"}]},{"given":"Adriana E.","family":"Rosato","sequence":"additional","affiliation":[{"name":"Houston Methodist Research Institute, Houston, Texas, USA"}]},{"given":"William L.","family":"Kelley","sequence":"additional","affiliation":[{"name":"Infectious Diseases Service, University Hospital and Medical School of Geneva, Geneva, Switzerland"}]},{"given":"Adriana","family":"Renzoni","sequence":"additional","affiliation":[{"name":"Infectious Diseases Service, University Hospital and Medical School of Geneva, Geneva, Switzerland"}]}],"member":"235","reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0140-6736(09)61999-1"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1038\/ng.3219"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pmed.1001104"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1001\/jama.2014.9743"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.1038\/nrmicro2200"},{"key":"e_1_3_3_7_2","doi-asserted-by":"publisher","DOI":"10.1172\/JCI68834"},{"key":"e_1_3_3_8_2","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1002505"},{"key":"e_1_3_3_9_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.chembiol.2012.11.013"},{"key":"e_1_3_3_10_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.00220-13"},{"key":"e_1_3_3_11_2","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0021577"},{"key":"e_1_3_3_12_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.02802-14"},{"key":"e_1_3_3_13_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.06264-11"},{"key":"e_1_3_3_14_2","first-page":"2333","article-title":"Mutants of Bacillus subtilis defective in protein export","volume":"134","author":"Kontinen VP","year":"1988","unstructured":"Kontinen VP, Sarvas M. 1988. 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