{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T13:52:02Z","timestamp":1792072322877,"version":"4.4.0"},"update-to":[{"DOI":"10.1371\/journal.ppat.1009881","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2021,10,20]],"date-time":"2021-10-20T00:00:00Z","timestamp":1634688000000}}],"reference-count":93,"publisher":"Public Library of Science (PLoS)","issue":"10","license":[{"start":{"date-parts":[[2021,10,8]],"date-time":"2021-10-08T00:00:00Z","timestamp":1633651200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000009","name":"Foundation for the National Institutes of Health","doi-asserted-by":"publisher","award":["F32-AI154570"],"award-info":[{"award-number":["F32-AI154570"]}],"id":[{"id":"10.13039\/100000009","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000009","name":"foundation for the national institutes of health","doi-asserted-by":"publisher","award":["R01-AI132627"],"award-info":[{"award-number":["R01-AI132627"]}],"id":[{"id":"10.13039\/100000009","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000009","name":"foundation for the national institutes of health","doi-asserted-by":"publisher","award":["R01-AI137070"],"award-info":[{"award-number":["R01-AI137070"]}],"id":[{"id":"10.13039\/100000009","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000009","name":"foundation for the national institutes of health","doi-asserted-by":"publisher","award":["R21-AI144060"],"award-info":[{"award-number":["R21-AI144060"]}],"id":[{"id":"10.13039\/100000009","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000861","name":"burroughs wellcome fund","doi-asserted-by":"publisher","award":["PATH"],"award-info":[{"award-number":["PATH"]}],"id":[{"id":"10.13039\/100000861","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000968","name":"american heart association","doi-asserted-by":"publisher","award":["AH830263"],"award-info":[{"award-number":["AH830263"]}],"id":[{"id":"10.13039\/100000968","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.plospathogens.org"],"crossmark-restriction":false},"short-container-title":["PLoS Pathog"],"abstract":"<jats:p>\n                    Pathogenic bacteria rely on protein phosphorylation to adapt quickly to stress, including that imposed by the host during infection. Penicillin-binding protein and serine\/threonine-associated (PASTA) kinases are signal transduction systems that sense cell wall integrity and modulate multiple facets of bacterial physiology in response to cell envelope stress. The PASTA kinase in the cytosolic pathogen\n                    <jats:italic>Listeria monocytogenes<\/jats:italic>\n                    , PrkA, is required for cell wall stress responses, cytosolic survival, and virulence, yet its substrates and downstream signaling pathways remain incompletely defined. We combined orthogonal phosphoproteomic and genetic analyses in the presence of a \u03b2-lactam antibiotic to define PrkA phosphotargets and pathways modulated by PrkA. These analyses synergistically highlighted ReoM, which was recently identified as a PrkA target that influences peptidoglycan (PG) synthesis, as an important phosphosubstrate during cell wall stress. We find that deletion of\n                    <jats:italic>reoM<\/jats:italic>\n                    restores cell wall stress sensitivities and cytosolic survival defects of a \u0394\n                    <jats:italic>prkA<\/jats:italic>\n                    mutant to nearly wild-type levels. While a \u0394\n                    <jats:italic>prkA<\/jats:italic>\n                    mutant is defective for PG synthesis during cell wall stress, a double \u0394\n                    <jats:italic>reoM<\/jats:italic>\n                    \u0394\n                    <jats:italic>prkA<\/jats:italic>\n                    mutant synthesizes PG at rates similar to wild type. In a mouse model of systemic listeriosis, deletion of\n                    <jats:italic>reoM<\/jats:italic>\n                    in a \u0394\n                    <jats:italic>prkA<\/jats:italic>\n                    background almost fully restored virulence to wild-type levels. However, loss of\n                    <jats:italic>reoM<\/jats:italic>\n                    alone also resulted in attenuated virulence, suggesting ReoM is critical at some points during pathogenesis. Finally, we demonstrate that the PASTA kinase\/ReoM cell wall stress response pathway is conserved in a related pathogen, methicillin-resistant\n                    <jats:italic>Staphylococcus aureus<\/jats:italic>\n                    . Taken together, our phosphoproteomic analysis provides a comprehensive overview of the PASTA kinase targets of an important model pathogen and suggests that a critical role of PrkA\n                    <jats:italic>in vivo<\/jats:italic>\n                    is modulating PG synthesis through regulation of ReoM to facilitate cytosolic survival and virulence.\n                  <\/jats:p>","DOI":"10.1371\/journal.ppat.1009881","type":"journal-article","created":{"date-parts":[[2021,10,9]],"date-time":"2021-10-09T19:57:03Z","timestamp":1633809423000},"page":"e1009881","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":37,"title":["PASTA kinase-dependent control of peptidoglycan synthesis via ReoM is required for cell wall stress responses, cytosolic survival, and virulence in Listeria monocytogenes"],"prefix":"10.1371","volume":"17","author":[{"given":"Jessica L.","family":"Kelliher","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0286-6345","authenticated-orcid":true,"given":"Caroline M.","family":"Grunenwald","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rhiannon R.","family":"Abrahams","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4662-4890","authenticated-orcid":true,"given":"McKenzie E.","family":"Daanen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9289-5910","authenticated-orcid":true,"given":"Cassandra I.","family":"Lew","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5012-5993","authenticated-orcid":true,"given":"Warren E.","family":"Rose","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9367-794X","authenticated-orcid":true,"given":"John-Demian","family":"Sauer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2021,10,8]]},"reference":[{"key":"ppat.1009881.ref001","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.211106398","article-title":"Microinjection and growth of bacteria in the cytosol of mammalian host cells","volume":"98","author":"M Goetz","year":"2001","journal-title":"Proceedings of the National Academy of Sciences"},{"key":"ppat.1009881.ref002","first-page":"103","article-title":"A Legionella pneumophila-translocated substrate that is required for growth within macrophages and protection from host cell death","author":"RK Laguna","year":"2006","journal-title":"Proceedings of the National Academy of Sciences"},{"key":"ppat.1009881.ref003","doi-asserted-by":"crossref","DOI":"10.1046\/j.1462-5822.2001.00087.x","article-title":"SifA permits survival and replication of Salmonella typhimurium in murine macrophages","volume":"3","author":"JH Brumell","year":"2001","journal-title":"Cellular Microbiology"},{"key":"ppat.1009881.ref004","doi-asserted-by":"crossref","DOI":"10.1099\/00221287-148-9-2705","article-title":"Growth and killing of a Salmonella enterica serovar Typhimurium sifA mutant strain in the cytosol of different host cell lines","volume":"148","author":"CR Beuz\u00f3n","year":"2002","journal-title":"Microbiology"},{"key":"ppat.1009881.ref005","article-title":"Preventing bacterial DNA release and absent in melanoma 2 inflammasome activation by a Legionella effector functioning in membrane trafficking","volume":"109","author":"J Ge","year":"2012","journal-title":"Proceedings of the National Academy of Sciences"},{"key":"ppat.1009881.ref006","doi-asserted-by":"crossref","first-page":"412","DOI":"10.1016\/j.chom.2010.04.004","article-title":"Listeria monocytogenes triggers AIM2-mediated pyroptosis upon infrequent bacteriolysis in the macrophage cytosol","volume":"7","author":"JD Sauer","year":"2010","journal-title":"Cell Host Microbe"},{"key":"ppat.1009881.ref007","doi-asserted-by":"crossref","first-page":"1586","DOI":"10.1111\/j.1462-5822.2011.01643.x","article-title":"Elevated AIM2-mediated pyroptosis triggered by hypercytotoxic Francisella mutant strains is attributed to increased intracellular bacteriolysis","volume":"13","author":"K Peng","year":"2011","journal-title":"Cell Microbiol"},{"key":"ppat.1009881.ref008","doi-asserted-by":"crossref","DOI":"10.1016\/j.chom.2016.06.003","article-title":"Group B Streptococcus Degrades Cyclic-di-AMP to Modulate STING-Dependent Type I Interferon Production","volume":"20","author":"WA Andrade","year":"2016","journal-title":"Cell Host & Microbe"},{"key":"ppat.1009881.ref009","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2016.05.030","article-title":"Type I Interferon Induction by Neisseria gonorrhoeae: Dual Requirement of Cyclic GMP-AMP Synthase and Toll-like Receptor 4.","volume":"15","author":"WA Andrade","year":"2016","journal-title":"Cell Reports."},{"key":"ppat.1009881.ref010","doi-asserted-by":"crossref","DOI":"10.4049\/jimmunol.1302718","article-title":"The DNA Sensor, Cyclic GMP\u2013AMP Synthase, Is Essential for Induction of IFN-\u03b2 during Chlamydia trachomatis Infection","volume":"193","author":"Y Zhang","year":"2014","journal-title":"The Journal of Immunology"},{"key":"ppat.1009881.ref011","doi-asserted-by":"crossref","DOI":"10.1016\/j.chom.2015.05.005","article-title":"Cyclic GMP-AMP Synthase Is an Innate Immune DNA Sensor for Mycobacterium tuberculosis.","volume":"17","author":"AC Collins","year":"2015","journal-title":"Cell Host & Microbe"},{"key":"ppat.1009881.ref012","doi-asserted-by":"crossref","DOI":"10.1016\/j.chom.2015.05.003","article-title":"Mycobacterium tuberculosis Differentially Activates cGAS- and Inflammasome-Dependent Intracellular Immune Responses through ESX-1.","volume":"17","author":"R Wassermann","year":"2015","journal-title":"Cell Host & Microbe."},{"key":"ppat.1009881.ref013","doi-asserted-by":"crossref","DOI":"10.1016\/j.chom.2015.05.004","article-title":"The Cytosolic Sensor cGAS Detects Mycobacterium tuberculosis DNA to Induce Type I Interferons and Activate Autophagy","volume":"17","author":"RO Watson","year":"2015","journal-title":"Cell Host & Microbe"},{"key":"ppat.1009881.ref014","doi-asserted-by":"crossref","DOI":"10.1016\/j.immuni.2014.12.010","article-title":"NOD1 and NOD2: Signaling, Host Defense, and Inflammatory Disease.","volume":"41","author":"R Caruso","year":"2014","journal-title":"Immunity"},{"key":"ppat.1009881.ref015","doi-asserted-by":"crossref","DOI":"10.2217\/fmb-2016-0221","article-title":"How the study of Listeria monocytogenes has led to new concepts in biology","volume":"12","author":"N Rolhion","year":"2017","journal-title":"Future Microbiology"},{"key":"ppat.1009881.ref016","author":"K Jordan","year":"2018","journal-title":"Listeria monocytogenes in Foods"},{"key":"ppat.1009881.ref017","article-title":"Foodborne Illness Acquired in the United States\u2014Major Pathogens","volume":"17","author":"E Scallan","year":"2011","journal-title":"Emerging Infectious Diseases"},{"key":"ppat.1009881.ref018","doi-asserted-by":"crossref","DOI":"10.1111\/j.1469-0691.2005.01146.x","article-title":"Understanding how Listeria monocytogenes targets and crosses host barriers","volume":"11","author":"M. Lecuit","year":"2005","journal-title":"Clinical Microbiology and Infection"},{"key":"ppat.1009881.ref019","doi-asserted-by":"crossref","DOI":"10.1016\/j.micinf.2007.05.005","article-title":"Listeriolysin O: a phagosome-specific lysin","volume":"9","author":"P Schnupf","year":"2007","journal-title":"Microbes and Infection"},{"key":"ppat.1009881.ref020","doi-asserted-by":"crossref","DOI":"10.1111\/cmi.12854","article-title":"Actin-based motility allows Listeria monocytogenes to avoid autophagy in the macrophage cytosol","volume":"20","author":"MI Cheng","year":"2018","journal-title":"Cellular Microbiology"},{"key":"ppat.1009881.ref021","first-page":"109","article-title":"Actin filaments and the growth, movement, and spread of the intracellular bacterial parasite, Listeria monocytogenes","author":"LG Tilney","year":"1989","journal-title":"Journal of Cell Biology"},{"key":"ppat.1009881.ref022","doi-asserted-by":"crossref","first-page":"e1006001","DOI":"10.1371\/journal.ppat.1006001","article-title":"The Listeria monocytogenes PASTA Kinase PrkA and Its Substrate YvcK Are Required for Cell Wall Homeostasis, Metabolism, and Virulence.","volume":"12","author":"DA Pensinger","year":"2016","journal-title":"PLoS Pathog."},{"key":"ppat.1009881.ref023","article-title":"The Extracytoplasmic Domain of the Mycobacterium tuberculosis Ser\/Thr Kinase PknB Binds Specific Muropeptides and Is Required for PknB Localization.","volume":"7","author":"M Mir","year":"2011","journal-title":"PLoS Pathogens"},{"key":"ppat.1009881.ref024","doi-asserted-by":"crossref","DOI":"10.1002\/cbic.201700385","article-title":"A Comprehensive Study of the Interaction between Peptidoglycan Fragments and the Extracellular Domain of Mycobacterium tuberculosis Ser\/Thr Kinase PknB","volume":"18","author":"Q Wang","year":"2017","journal-title":"ChemBioChem"},{"key":"ppat.1009881.ref025","article-title":"A Eukaryotic-like Ser\/Thr Kinase Signals Bacteria to Exit Dormancy in Response to Peptidoglycan Fragments","volume":"135","author":"IM Shah","year":"2008","journal-title":"Cell"},{"key":"ppat.1009881.ref026","doi-asserted-by":"crossref","DOI":"10.1016\/j.febslet.2010.12.016","article-title":"Recognition of peptidoglycan and \u03b2-lactam antibiotics by the extracellular domain of the Ser\/Thr protein kinase StkP from Streptococcus pneumoniae","volume":"585","author":"B Maestro","year":"2011","journal-title":"FEBS Letters"},{"key":"ppat.1009881.ref027","doi-asserted-by":"crossref","DOI":"10.1093\/femsre\/fuv041","article-title":"Role of eukaryotic-like serine\/threonine kinases in bacterial cell division and morphogenesis","volume":"40","author":"S Manuse","year":"2016","journal-title":"FEMS Microbiology Reviews"},{"key":"ppat.1009881.ref028","doi-asserted-by":"crossref","first-page":"4486","DOI":"10.1128\/AAC.02396-14","article-title":"Selective pharmacologic inhibition of a PASTA kinase increases Listeria monocytogenes susceptibility to beta-lactam antibiotics","volume":"58","author":"DA Pensinger","year":"2014","journal-title":"Antimicrob Agents Chemother"},{"key":"ppat.1009881.ref029","doi-asserted-by":"crossref","first-page":"17037","DOI":"10.1074\/jbc.M117.808600","article-title":"A screen for kinase inhibitors identifies antimicrobial imidazopyridine aminofurazans as specific inhibitors of the Listeria monocytogenes PASTA kinase PrkA","volume":"292","author":"AJ Schaenzer","year":"2017","journal-title":"J Biol Chem"},{"key":"ppat.1009881.ref030","first-page":"191","article-title":"Characterization of a Serine\/Threonine Kinase Involved in Virulence of Staphylococcus aureus","author":"M D\u00e9barbouill\u00e9","year":"2009","journal-title":"Journal of Bacteriology"},{"key":"ppat.1009881.ref031","doi-asserted-by":"crossref","DOI":"10.1128\/IAI.00296-10","article-title":"Role of PknB Kinase in Antibiotic Resistance and Virulence in Community-Acquired Methicillin-Resistant Staphylococcus aureus Strain USA300","volume":"78","author":"S Tamber","year":"2010","journal-title":"Infection and Immunity"},{"key":"ppat.1009881.ref032","doi-asserted-by":"crossref","first-page":"1508","DOI":"10.1021\/acsinfecdis.8b00136","article-title":"GW779439X and Its Pyrazolopyridazine Derivatives Inhibit the Serine\/Threonine Kinase Stk1 and Act As Antibiotic Adjuvants against beta-Lactam-Resistant Staphylococcus aureus.","volume":"4","author":"AJ Schaenzer","year":"2018","journal-title":"ACS Infect Dis."},{"key":"ppat.1009881.ref033","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-017-05314-z","article-title":"A novel STK1-targeted small-molecule as an \u201cantibiotic resistance breaker\u201d against multidrug-resistant Staphylococcus aureus.","volume":"7","author":"S Kant","year":"2017","journal-title":"Scientific Reports"},{"key":"ppat.1009881.ref034","doi-asserted-by":"crossref","first-page":"e00199","DOI":"10.1128\/mBio.00199-11","article-title":"Reciprocal regulation of cephalosporin resistance in Enterococcus faecalis.","volume":"2","author":"CJ Kristich","year":"2011","journal-title":"MBio"},{"key":"ppat.1009881.ref035","doi-asserted-by":"crossref","DOI":"10.1128\/IAI.72.4.2434-2437.2004","article-title":"Protein Serine\/Threonine Kinase StkP Positively Controls Virulence and Competence in Streptococcus pneumoniae","volume":"72","author":"J Echenique","year":"2004","journal-title":"Infection and Immunity"},{"key":"ppat.1009881.ref036","doi-asserted-by":"crossref","DOI":"10.1186\/1471-2180-9-121","article-title":"The highly conserved serine threonine kinase StkP of Streptococcus pneumoniae contributes to penicillin susceptibility independently from genes encoding penicillin-binding proteins","volume":"9","author":"R Dias","year":"2009","journal-title":"BMC Microbiology"},{"key":"ppat.1009881.ref037","doi-asserted-by":"crossref","DOI":"10.1128\/JB.01221-09","article-title":"Regulatory Interactions of a Virulence-Associated Serine\/Threonine Phosphatase-Kinase Pair in Bacillus anthracis","volume":"192","author":"SM Shakir","year":"2010","journal-title":"Journal of Bacteriology"},{"key":"ppat.1009881.ref038","doi-asserted-by":"crossref","DOI":"10.1074\/jbc.M114.563536","article-title":"Protein Kinase B (PknB) of Mycobacterium tuberculosis Is Essential for Growth of the Pathogen in Vitro as well as for Survival within the Host.","volume":"289","author":"Y Chawla","year":"2014","journal-title":"Journal of Biological Chemistry"},{"key":"ppat.1009881.ref039","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1016\/j.tim.2017.06.010","article-title":"Do Shoot the Messenger: PASTA Kinases as Virulence Determinants and Antibiotic Targets","volume":"26","author":"DA Pensinger","year":"2018","journal-title":"Trends Microbiol"},{"key":"ppat.1009881.ref040","doi-asserted-by":"crossref","DOI":"10.1074\/mcp.M113.035949","article-title":"Quantitative Phosphoproteome Analysis of Bacillus subtilis Reveals Novel Substrates of the Kinase PrkC and Phosphatase PrpC.","volume":"13","author":"V Ravikumar","year":"2014","journal-title":"Molecular & Cellular Proteomics"},{"key":"ppat.1009881.ref041","doi-asserted-by":"crossref","DOI":"10.1016\/j.chembiol.2010.06.012","article-title":"A Metabolomic View of Staphylococcus aureus and Its Ser\/Thr Kinase and Phosphatase Deletion Mutants: Involvement in Cell Wall Biosynthesis.","volume":"17","author":"M Liebeke","year":"2010","journal-title":"Chemistry & Biology"},{"key":"ppat.1009881.ref042","doi-asserted-by":"crossref","DOI":"10.1074\/mcp.RA120.002232","article-title":"In-Depth Characterization of the Staphylococcus aureus Phosphoproteome Reveals New Targets of Stk1","volume":"20","author":"N Prust","year":"2021","journal-title":"Molecular & Cellular Proteomics"},{"key":"ppat.1009881.ref043","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1008452","article-title":"Protein kinases PknA and PknB independently and coordinately regulate essential Mycobacterium tuberculosis physiologies and antimicrobial susceptibility","volume":"16","author":"J Zeng","year":"2020","journal-title":"PLOS Pathogens"},{"key":"ppat.1009881.ref044","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-019-09223-9","article-title":"LipidII interaction with specific residues of Mycobacterium tuberculosis PknB extracytoplasmic domain governs its optimal activation","volume":"10","author":"P Kaur","year":"2019","journal-title":"Nature Communications"},{"key":"ppat.1009881.ref045","doi-asserted-by":"crossref","DOI":"10.1111\/j.1742-4658.2005.04560.x","article-title":"Characterization of a eukaryotic type serine\/threonine protein kinase and protein phosphatase of Streptococcus pneumoniae and identification of kinase substrates.","volume":"272","author":"L Nov\u00e1kov\u00e1","year":"2005","journal-title":"FEBS Journal"},{"key":"ppat.1009881.ref046","doi-asserted-by":"crossref","DOI":"10.1128\/IAI.05360-11","article-title":"Serine\/Threonine Protein Kinase Stk Is Required for Virulence, Stress Response, and Penicillin Tolerance in Streptococcus pyogenes","volume":"79","author":"J Bugrysheva","year":"2011","journal-title":"Infection and Immunity"},{"key":"ppat.1009881.ref047","doi-asserted-by":"crossref","DOI":"10.1021\/bi401177n","article-title":"Two Unique Phosphorylation-Driven Signaling Pathways Crosstalk in Staphylococcus aureus to Modulate the Cell-Wall Charge: Stk1\/Stp1 Meets GraSR.","volume":"52","author":"M Fridman","year":"2013","journal-title":"Biochemistry"},{"key":"ppat.1009881.ref048","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijmm.2016.12.001","article-title":"The cell wall precursor lipid II acts as a molecular signal for the Ser\/Thr kinase PknB of Staphylococcus aureus","volume":"307","author":"P Hardt","year":"2017","journal-title":"International Journal of Medical Microbiology"},{"key":"ppat.1009881.ref049","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.14590","article-title":"A cytoplasmic peptidoglycan amidase homologue controls mycobacterial cell wall synthesis","volume":"5","author":"CC Boutte","year":"2016","journal-title":"eLife"},{"key":"ppat.1009881.ref050","doi-asserted-by":"crossref","DOI":"10.1016\/j.jmb.2008.12.031","article-title":"PknB-Mediated Phosphorylation of a Novel Substrate, N-Acetylglucosamine-1-Phosphate Uridyltransferase, Modulates Its Acetyltransferase Activity","volume":"386","author":"A Parikh","year":"2009","journal-title":"Journal of Molecular Biology"},{"key":"ppat.1009881.ref051","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pgen.1007689","article-title":"A metabolic checkpoint protein GlmR is important for diverting carbon into peptidoglycan biosynthesis in Bacillus subtilis","volume":"14","author":"V Patel","year":"2018","journal-title":"PLOS Genetics"},{"key":"ppat.1009881.ref052","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.56048","article-title":"PrkA controls peptidoglycan biosynthesis through the essential phosphorylation of ReoM.","volume":"9","author":"S Wamp","year":"2020","journal-title":"eLife"},{"key":"ppat.1009881.ref053","doi-asserted-by":"crossref","first-page":"6179","DOI":"10.1128\/AAC.01472-13","article-title":"IreB, a Ser\/Thr kinase substrate, influences antimicrobial resistance in Enterococcus faecalis","volume":"57","author":"CL Hall","year":"2013","journal-title":"Antimicrob Agents Chemother"},{"key":"ppat.1009881.ref054","doi-asserted-by":"crossref","DOI":"10.1021\/pr500929u","article-title":"Quantitative Proteome Analyses Identify PrfA-Responsive Proteins and Phosphoproteins in Listeria monocytogenes","volume":"13","author":"SK Misra","year":"2014","journal-title":"Journal of Proteome Research"},{"key":"ppat.1009881.ref055","doi-asserted-by":"crossref","DOI":"10.1002\/pmic.201100259","article-title":"Analysis of the serine\/threonine\/tyrosine phosphoproteome of the pathogenic bacterium Listeria monocytogenes reveals phosphorylated proteins related to virulence","volume":"11","author":"SK Misra","year":"2011","journal-title":"PROTEOMICS"},{"key":"ppat.1009881.ref056","doi-asserted-by":"crossref","DOI":"10.1016\/j.jprot.2011.03.005","article-title":"Serine\/threonine protein kinase PrkA of the human pathogen Listeria monocytogenes: Biochemical characterization and identification of interacting partners through proteomic approaches","volume":"74","author":"A Lima","year":"2011","journal-title":"Journal of Proteomics"},{"key":"ppat.1009881.ref057","doi-asserted-by":"crossref","DOI":"10.1159\/000308512","article-title":"In vitro Phosphorylation of Key Metabolic Enzymes from Bacillus subtilis PrkC Phosphorylates Enzymes from Different Branches of Basic Metabolism","volume":"18","author":"N Pietack","year":"2010","journal-title":"Journal of Molecular Microbiology and Biotechnology"},{"key":"ppat.1009881.ref058","doi-asserted-by":"crossref","DOI":"10.1111\/mmi.13015","article-title":"Phosphorylation of the cell division protein GpsB regulates PrkC kinase activity through a negative feedback loop in Bacillus subtilis","volume":"97","author":"F Pompeo","year":"2015","journal-title":"Molecular Microbiology"},{"key":"ppat.1009881.ref059","article-title":"Isolation of Listeria monocytogenes mutants with high-level in vitro expression of host cytosol-induced gene products","volume":"48","author":"LM Shetron-Rama","year":"2003","journal-title":"Molecular Microbiology"},{"key":"ppat.1009881.ref060","doi-asserted-by":"crossref","DOI":"10.1046\/j.1365-2958.2000.01773.x","article-title":"The ClpP serine protease is essential for the intracellular parasitism and virulence of Listeria monocytogenes","volume":"35","author":"O Gaillot","year":"2002","journal-title":"Molecular Microbiology"},{"key":"ppat.1009881.ref061","doi-asserted-by":"crossref","DOI":"10.1046\/j.1365-2958.1996.641432.x","article-title":"Identification of a ClpC ATPase required for stress tolerance and in vivo survival of Listeria monocytogenes","volume":"21","author":"C Rouquette","year":"1996","journal-title":"Molecular Microbiology"},{"key":"ppat.1009881.ref062","doi-asserted-by":"crossref","DOI":"10.1128\/JB.00393-16","article-title":"Suppressor Mutations Linking gpsB with the First Committed Step of Peptidoglycan Biosynthesis in Listeria monocytogenes","volume":"199","author":"J Rismondo","year":"2017","journal-title":"Journal of Bacteriology"},{"key":"ppat.1009881.ref063","doi-asserted-by":"crossref","DOI":"10.1021\/cb3004995","article-title":"d -Amino Acid Chemical Reporters Reveal Peptidoglycan Dynamics of an Intracellular Pathogen.","volume":"8","author":"MS Siegrist","year":"2013","journal-title":"ACS Chemical Biology"},{"key":"ppat.1009881.ref064","doi-asserted-by":"crossref","DOI":"10.1038\/nature12892","article-title":"A new metabolic cell-wall labelling method reveals peptidoglycan in Chlamydia trachomatis","volume":"506","author":"GW Liechti","year":"2014","journal-title":"Nature"},{"key":"ppat.1009881.ref065","article-title":"Structure and Dimerization of IreB, a Negative Regulator of Cephalosporin Resistance in Enterococcus faecalis","volume":"429","author":"CL Hall","year":"2017","journal-title":"Journal of Molecular Biology"},{"key":"ppat.1009881.ref066","article-title":"Mutations of the Listeria monocytogenes Peptidoglycan N -Deacetylase and O -Acetylase Result in Enhanced Lysozyme Sensitivity, Bacteriolysis, and Hyperinduction of Innate Immune Pathways","volume":"79","author":"CS Rae","year":"2011","journal-title":"Infection and Immunity"},{"key":"ppat.1009881.ref067","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.1219125110","article-title":"Structural and functional insights into caseinolytic proteases reveal an unprecedented regulation principle of their catalytic triad","volume":"110","author":"E Zeiler","year":"2013","journal-title":"Proceedings of the National Academy of Sciences"},{"key":"ppat.1009881.ref068","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1004996","article-title":"Peptidoglycan Branched Stem Peptides Contribute to Streptococcus pneumoniae Virulence by Inhibiting Pneumolysin Release.","volume":"11","author":"NG Greene","year":"2015","journal-title":"PLOS Pathogens"},{"key":"ppat.1009881.ref069","doi-asserted-by":"crossref","DOI":"10.1046\/j.1365-2958.2002.03178.x","article-title":"Characterization of a membrane-linked Ser\/Thr protein kinase in Bacillus subtilis, implicated in developmental processes","volume":"46","author":"E Madec","year":"2002","journal-title":"Molecular Microbiology"},{"key":"ppat.1009881.ref070","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.0608742104","article-title":"A eukaryotic-type Ser\/Thr kinase in Enterococcus faecalis mediates antimicrobial resistance and intestinal persistence","volume":"104","author":"CJ Kristich","year":"2007","journal-title":"Proceedings of the National Academy of Sciences"},{"key":"ppat.1009881.ref071","doi-asserted-by":"crossref","DOI":"10.1128\/mBio.02333-17","article-title":"Multisystem Analysis of Mycobacterium tuberculosis Reveals Kinase-Dependent Remodeling of the Pathogen-Environment Interface.","volume":"9","author":"X Carette","year":"2018","journal-title":"mBio"},{"key":"ppat.1009881.ref072","doi-asserted-by":"crossref","DOI":"10.1128\/AEM.65.5.2112-2115.1999","article-title":"Mutational Analysis of the Role of HPr in Listeria monocytogenes","volume":"65","author":"DP Christensen","year":"1999","journal-title":"Applied and Environmental Microbiology"},{"key":"ppat.1009881.ref073","doi-asserted-by":"crossref","DOI":"10.1111\/j.1365-2958.1993.tb01211.x","article-title":"Dual roles of plcA in Listeria monocytogenes pathogenesis","volume":"8","author":"A Camilli","year":"1993","journal-title":"Molecular Microbiology"},{"key":"ppat.1009881.ref074","doi-asserted-by":"crossref","DOI":"10.1016\/0300-9084(92)90143-3","article-title":"Use of a new integrational vector to investigate compartment-specific expression of the Bacillus subtilis spollM gene","volume":"74","author":"K Smith","year":"1992","journal-title":"Biochimie"},{"key":"ppat.1009881.ref075","article-title":"Tools for Functional Postgenomic Analysis of Listeria monocytogenes","volume":"74","author":"IR Monk","year":"2008","journal-title":"Applied and Environmental Microbiology"},{"key":"ppat.1009881.ref076","doi-asserted-by":"crossref","DOI":"10.1128\/JB.184.15.4177-4186.2002","article-title":"Construction, Characterization, and Use of Two Listeria monocytogenes Site-Specific Phage Integration Vectors","volume":"184","author":"P Lauer","year":"2002","journal-title":"Journal of Bacteriology"},{"key":"ppat.1009881.ref077","doi-asserted-by":"crossref","first-page":"2218","DOI":"10.1128\/AEM.00136-13","article-title":"Genetic tools to enhance the study of gene function and regulation in Staphylococcus aureus","volume":"79","author":"JL Bose","year":"2013","journal-title":"Appl Environ Microbiol"},{"key":"ppat.1009881.ref078","doi-asserted-by":"crossref","DOI":"10.1046\/j.1365-2958.2000.01643.x","article-title":"Generalized transduction of serotype 1\/2 and serotype 4b strains of Listeria monocytogenes","volume":"35","author":"DA Hodgson","year":"2000","journal-title":"Molecular Microbiology"},{"key":"ppat.1009881.ref079","first-page":"e00537","article-title":"A genetic resource for rapid and comprehensive phenotype screening of nonessential Staphylococcus aureus genes.","volume":"4","author":"PD Fey","year":"2013","journal-title":"MBio"},{"key":"ppat.1009881.ref080","doi-asserted-by":"crossref","DOI":"10.1016\/j.chembiol.2016.09.012","article-title":"A Small-Molecule Inhibitor of Iron-Sulfur Cluster Assembly Uncovers a Link between Virulence Regulation and Metabolism in Staphylococcus aureus","volume":"23","author":"JE Choby","year":"2016","journal-title":"Cell Chemical Biology"},{"key":"ppat.1009881.ref081","article-title":"Mutation of the transcriptional regulator YtoI rescues Listeria monocytogenes mutants deficient in the essential shared metabolite 1,4-dihydroxy-2-naphthoate (DHNA).","author":"GY Chen","year":"2019","journal-title":"Infect Immun"},{"key":"ppat.1009881.ref082","doi-asserted-by":"crossref","DOI":"10.1038\/nmeth.1923","article-title":"Fast gapped-read alignment with Bowtie 2","volume":"9","author":"B Langmead","year":"2012","journal-title":"Nature Methods"},{"key":"ppat.1009881.ref083","article-title":"The Sequence Alignment\/Map format and SAMtools","volume":"25","author":"H Li","year":"2009","journal-title":"Bioinformatics"},{"key":"ppat.1009881.ref084","article-title":"A statistical framework for SNP calling, mutation discovery, association mapping and population genetical parameter estimation from sequencing data","volume":"27","author":"H. Li","year":"2011","journal-title":"Bioinformatics"},{"key":"ppat.1009881.ref085","volume-title":"Methods for Dilution Antimicrobial Susceptibility Tests for Bacteria That Grow Aerobically; Approved Standard.","author":"M. Weinstein","year":"2012","edition":"9"},{"key":"ppat.1009881.ref086","doi-asserted-by":"crossref","first-page":"12419","DOI":"10.1073\/pnas.1019041108","article-title":"Listeria monocytogenes engineered to activate the Nlrc4 inflammasome are severely attenuated and are poor inducers of protective immunity","volume":"108","author":"JD Sauer","year":"2011","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ppat.1009881.ref087","doi-asserted-by":"crossref","DOI":"10.1016\/0022-1759(88)90310-9","article-title":"A quick and simple method for the quantitation of lactate dehydrogenase release in measurements of cellular cytotoxicity and tumor necrosis factor (TNF) activity.","volume":"115","author":"T Decker","year":"1988","journal-title":"Journal of Immunological Methods"},{"key":"ppat.1009881.ref088","doi-asserted-by":"crossref","first-page":"688","DOI":"10.1128\/IAI.00999-10","article-title":"The N-ethyl-N-nitrosourea-induced Goldenticket mouse mutant reveals an essential function of Sting in the in vivo interferon response to Listeria monocytogenes and cyclic dinucleotides","volume":"79","author":"JD Sauer","year":"2011","journal-title":"Infect Immun"},{"key":"ppat.1009881.ref089","doi-asserted-by":"crossref","DOI":"10.1128\/iai.62.12.5608-5613.1994","article-title":"Characterization of Listeria monocytogenes pathogenesis in a strain expressing perfringolysin O in place of listeriolysin O","volume":"62","author":"S Jones","year":"1994","journal-title":"Infection and Immunity"},{"key":"ppat.1009881.ref090","doi-asserted-by":"crossref","DOI":"10.1084\/jem.167.4.1459","article-title":"Role of hemolysin for the intracellular growth of Listeria monocytogenes","volume":"167","author":"DA Portnoy","year":"1988","journal-title":"Journal of Experimental Medicine"},{"key":"ppat.1009881.ref091","article-title":"Isolation of Listeria monocytogenes small-plaque mutants defective for intracellular growth and cell-to-cell spread","volume":"58","author":"AN Sun","year":"1990","journal-title":"Infection and Immunity"},{"key":"ppat.1009881.ref092","article-title":"Listeria monocytogenes MenI encodes a DHNA-CoA thioesterase necessary for menaquinone biosynthesis, cytosolic survival, and virulence","author":"HB Smith","year":"2021","journal-title":"Infection and Immunity"},{"key":"ppat.1009881.ref093","doi-asserted-by":"crossref","DOI":"10.1128\/mBio.00969-14","article-title":"Comparison of Widely Used Listeria monocytogenes Strains EGD, 10403S, and EGD-e Highlights Genomic Differences Underlying Variations in Pathogenicity.","volume":"5","author":"C B\u00e9cavin","year":"2014","journal-title":"mBio"}],"updated-by":[{"DOI":"10.1371\/journal.ppat.1009881","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2021,10,20]],"date-time":"2021-10-20T00:00:00Z","timestamp":1634688000000}}],"container-title":["PLOS Pathogens"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.ppat.1009881","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,10,20]],"date-time":"2021-10-20T23:59:40Z","timestamp":1634774380000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.ppat.1009881"}},"subtitle":[],"editor":[{"given":"Christopher M.","family":"Sassetti","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2021,10,8]]},"references-count":93,"journal-issue":{"issue":"10","published-online":{"date-parts":[[2021,10,8]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.ppat.1009881","relation":{"has-preprint":[{"id-type":"doi","id":"10.1101\/2021.08.20.457112","asserted-by":"object"}]},"ISSN":["1553-7374"],"issn-type":[{"value":"1553-7374","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,10,8]]}}}