{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,28]],"date-time":"2026-10-28T14:48:42Z","timestamp":1793198922520,"version":"4.5.0"},"reference-count":94,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2021,12,24]],"date-time":"2021-12-24T00:00:00Z","timestamp":1640304000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Microbiol."],"abstract":"<jats:p><jats:italic>Listeria monocytogenes<\/jats:italic> continues to be a food safety challenge owing to its stress tolerance and virulence traits. Several listeriosis outbreaks have been linked to the consumption of contaminated ready-to-eat food products. Numerous interventions, including nisin application, are presently employed to mitigate against <jats:italic>L. monocytogenes<\/jats:italic> risk in food products. In response, <jats:italic>L. monocytogenes<\/jats:italic> deploys several defense mechanisms, reducing nisin efficacy, that are not yet fully understood. Cold shock proteins (Csps) are small, highly conserved nucleic acid-binding proteins involved in several gene regulatory processes to mediate various stress responses in bacteria. <jats:italic>L. monocytogenes<\/jats:italic> possesses three <jats:italic>csp<\/jats:italic> gene paralogs; <jats:italic>cspA<\/jats:italic>, <jats:italic>cspB<\/jats:italic>, and <jats:italic>cspD<\/jats:italic>. Using a panel of single, double, and triple <jats:italic>csp<\/jats:italic> gene deletion mutants, the role of Csps in <jats:italic>L. monocytogenes<\/jats:italic> nisin tolerance was examined, demonstrating their importance in nisin stress responses of this bacterium. Without <jats:italic>csp<\/jats:italic> genes, a <jats:italic>L. monocytogenes<\/jats:italic> \u0394<jats:italic>cspABD<\/jats:italic> mutant displayed severely compromised growth under nisin stress. Characterizing single (\u0394<jats:italic>cspA<\/jats:italic>, \u0394<jats:italic>cspB<\/jats:italic>, and \u0394<jats:italic>cspD<\/jats:italic>) and double (\u0394<jats:italic>cspBD<\/jats:italic>, \u0394<jats:italic>cspAD<\/jats:italic>, and \u0394<jats:italic>cspAB<\/jats:italic>) <jats:italic>csp<\/jats:italic> gene deletion mutants revealed a hierarchy (<jats:italic>cspD<\/jats:italic> &amp;gt; <jats:italic>cspB<\/jats:italic> &amp;gt; <jats:italic>cspA<\/jats:italic>) of importance in <jats:italic>csp<\/jats:italic> gene contributions toward the <jats:italic>L. monocytogenes<\/jats:italic> nisin tolerance phenotype. Individual eliminations of either <jats:italic>cspA<\/jats:italic> or <jats:italic>cspB<\/jats:italic> improved the nisin stress tolerance phenotype, suggesting that their expression has a curbing effect on the expression of nisin resistance functions through CspD. Gene expression analysis revealed that Csp deficiency altered the expression of DltA, MprF, and penicillin-binding protein-encoding genes. Furthermore, the \u0394<jats:italic>cspABD<\/jats:italic> mutation induced an overall more electronegative cell surface, enhancing sensitivity to nisin and other cationic antimicrobials as well as the quaternary ammonium compound disinfectant benzalkonium chloride. These observations demonstrate that the molecular functions of Csps regulate systems important for enabling the constitution and maintenance of an optimal composed cell envelope that protects against cell-envelope-targeting stressors, including nisin. Overall, our data show an important contribution of Csps for <jats:italic>L. monocytogenes<\/jats:italic> stress protection in food environments where antimicrobial peptides are used. Such knowledge can be harnessed in the development of better <jats:italic>L. monocytogenes<\/jats:italic> control strategies. Furthermore, the potential that Csps have in inducing cross-protection must be considered when combining hurdle techniques or using them in a series.<\/jats:p>","DOI":"10.3389\/fmicb.2021.811939","type":"journal-article","created":{"date-parts":[[2021,12,24]],"date-time":"2021-12-24T09:33:12Z","timestamp":1640338392000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":18,"title":["Cold Shock Proteins Promote Nisin Tolerance in Listeria monocytogenes Through Modulation of Cell Envelope Modification Responses"],"prefix":"10.3389","volume":"12","author":[{"given":"Francis","family":"Muchaamba","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joseph","family":"Wambui","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Roger","family":"Stephan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Taurai","family":"Tasara","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2021,12,24]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1046\/j.1365-2958.2002.02723.x","article-title":"Formation of D-alanyl-lipoteichoic acid is required for adhesion and virulence of Listeria monocytogenes.","volume":"43","author":"Abachin","year":"2002","journal-title":"Mol. Microbiol."},{"key":"B2","doi-asserted-by":"publisher","first-page":"1962","DOI":"10.1128\/aem.60.6.1962-1968.1994","article-title":"Mode of action of nisin Z against Listeria monocytogenes ScottA grown at high and low temperatures.","volume":"60","author":"Abee","year":"1994","journal-title":"Appl. Environ. Microbiol."},{"key":"B3","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1016\/j.lwt.2018.10.014","article-title":"Influence of cold stress on the survival of Listeria monocytogenes Bug600 and ScottA in lethal alkali, acid and oxidative stress.","volume":"100","author":"Abeysundara","year":"2019","journal-title":"Lebensm. Wiss. Technol."},{"key":"B4","doi-asserted-by":"publisher","first-page":"590","DOI":"10.1089\/mdr.2017.0147","article-title":"Vancomycin-Resistant enterococci: a review of antimicrobial resistance mechanisms and perspectives of human and animal health.","volume":"24","author":"Ahmed","year":"2018","journal-title":"Microb. Drug Resist."},{"key":"B5","doi-asserted-by":"publisher","first-page":"2939","DOI":"10.1007\/s00253-016-7343-9","article-title":"Bacteriocins of lactic acid bacteria: extending the family.","volume":"100","author":"Alvarez-Sieiro","year":"2016","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"B6","doi-asserted-by":"publisher","first-page":"e2004303","DOI":"10.1371\/journal.pbio.2004303","article-title":"Communication across the bacterial cell envelope depends on the size of the periplasm.","volume":"15","author":"Asmar","year":"2017","journal-title":"PLoS Biol."},{"key":"B7","doi-asserted-by":"publisher","first-page":"1429","DOI":"10.1046\/j.1365-2958.1999.01284.x","article-title":"Characterization of Escherichia coli cspE, whose product negatively regulates transcription of cspA, the gene for the major cold shock protein.","volume":"31","author":"Bae","year":"1999","journal-title":"Mol. Microbiol."},{"key":"B8","doi-asserted-by":"publisher","first-page":"7784","DOI":"10.1073\/pnas.97.14.7784","article-title":"Escherichia coli CspA-family RNA chaperones are transcription antiterminators.","volume":"97","author":"Bae","year":"2000","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B9","doi-asserted-by":"publisher","first-page":"817","DOI":"10.1080\/10408398.2012.729231","article-title":"Bacteriocins: recent trends and potential applications.","volume":"56","author":"Bali","year":"2016","journal-title":"Crit. Rev. Food Sci. Nutr."},{"key":"B10","doi-asserted-by":"publisher","first-page":"191","DOI":"10.1146\/annurev-food-030713-092350","article-title":"Stress adaptation in foodborne pathogens.","volume":"6","author":"Begley","year":"2015","journal-title":"Annu. Rev. Food Sci. Technol."},{"key":"B11","doi-asserted-by":"publisher","first-page":"6541","DOI":"10.1128\/AEM.00203-10","article-title":"Glutamate decarboxylase-mediated nisin resistance in Listeria monocytogenes.","volume":"76","author":"Begley","year":"2010","journal-title":"Appl. Environ. Microbiol."},{"key":"B12","doi-asserted-by":"publisher","first-page":"2231","DOI":"10.1128\/AEM.72.3.2231-2234.2006","article-title":"Tolerance of Listeria monocytogenes to cell envelope-acting antimicrobial agents is dependent on SigB.","volume":"72","author":"Begley","year":"2006","journal-title":"Appl. Environ. Microbiol."},{"key":"B13","doi-asserted-by":"publisher","first-page":"2602","DOI":"10.1128\/AEM.07658-11","article-title":"Listeria monocytogenes shows temperature-dependent and -independent responses to salt stress, including responses that induce cross-protection against other stresses.","volume":"78","author":"Bergholz","year":"2012","journal-title":"Appl. Environ. Microbiol."},{"key":"B14","doi-asserted-by":"publisher","first-page":"5682","DOI":"10.1128\/AEM.01797-13","article-title":"Nisin resistance of Listeria monocytogenes is increased by exposure to salt stress and is mediated via LiaR.","volume":"79","author":"Bergholz","year":"2013","journal-title":"Appl. Environ. Microbiol."},{"key":"B15","doi-asserted-by":"publisher","first-page":"2255","DOI":"10.1128\/aem.58.7.2255-2259.1992","article-title":"Depletion of proton motive force by nisin in Listeria monocytogenes cells.","volume":"58","author":"Bruno","year":"1992","journal-title":"Appl. Environ. Microbiol."},{"key":"B16","doi-asserted-by":"publisher","first-page":"2700","DOI":"10.3389\/fmicb.2018.02700","article-title":"Resistance of Listeria monocytogenes to stress conditions encountered in food and food processing environments.","volume":"9","author":"Bucur","year":"2018","journal-title":"Front. Microbiol."},{"key":"B17","doi-asserted-by":"publisher","first-page":"37","DOI":"10.1016\/j.ijfoodmicro.2015.12.014","article-title":"The response of foodborne pathogens to osmotic and desiccation stresses in the food chain.","volume":"221","author":"Burgess","year":"2016","journal-title":"Int. J. Food Microbiol."},{"key":"B18","doi-asserted-by":"publisher","first-page":"1345","DOI":"10.1093\/nar\/gkx1284","article-title":"The regulon of the RNA chaperone CspA and its auto-regulation in Staphylococcus aureus.","volume":"46","author":"Caballero","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"B19","doi-asserted-by":"publisher","first-page":"e1004919","DOI":"10.1371\/journal.ppat.1004919","article-title":"L- Rhamnosylation of Listeria monocytogenes wall Teichoic acids promotes resistance to antimicrobial peptides by delaying interaction with the membrane.","volume":"11","author":"Carvalho","year":"2015","journal-title":"PLoS Pathog."},{"key":"B20","doi-asserted-by":"crossref","first-page":"324","DOI":"10.15585\/mmwr.mm6711a3","article-title":"Centre for disease control and prevention. Preliminary incidence and trends of infections with pathogens transmitted commonly through food. Foodborne Diseases Active Surveillance Network, 10 U.S. Sites, 2006-2017.","volume":"67","year":"2018","journal-title":"MMWR Morb. Mortal. Wkly. Rep."},{"key":"B21","doi-asserted-by":"publisher","first-page":"108793","DOI":"10.1016\/j.ijfoodmicro.2020.108793","article-title":"Pre-growth conditions and strain diversity affect nisin treatment efficacy against Listeria monocytogenes on cold-smoked salmon.","volume":"333","author":"Chen","year":"2020","journal-title":"Int. J. Food Microbiol."},{"key":"B22","doi-asserted-by":"publisher","first-page":"4416","DOI":"10.1128\/AAC.00503-10","article-title":"The ABC transporter AnrAB contributes to the innate resistance of Listeria monocytogenes to nisin, bacitracin, and various beta-lactam antibiotics.","volume":"54","author":"Collins","year":"","journal-title":"Antimicrob. Agents Chemother."},{"key":"B23","doi-asserted-by":"crossref","first-page":"4658","DOI":"10.1128\/AAC.00290-10","article-title":"TelA contributes to the innate resistance of Listeria monocytogenes to nisin and other cell wall- acting antibiotics.","volume":"54","author":"Collins","year":"","journal-title":"Antimicrob. Agents Chemother."},{"key":"B24","doi-asserted-by":"publisher","first-page":"2784","DOI":"10.1128\/AAC.46.9.2784-2790.2002","article-title":"The LisRK signal transduction system determines the sensitivity of Listeria monocytogenes to nisin and cephalosporins.","volume":"46","author":"Cotter","year":"2002","journal-title":"Antimicrob. Agents Chemother."},{"key":"B25","doi-asserted-by":"publisher","first-page":"95","DOI":"10.1038\/nrmicro2937","article-title":"Bacteriocins \u2013 a viable alternative to antibiotics?","volume":"11","author":"Cotter","year":"2013","journal-title":"Nat. Rev. Microbiol."},{"key":"B26","doi-asserted-by":"publisher","first-page":"12","DOI":"10.1038\/s41396-018-0241-7","article-title":"Stressor interaction networks suggest antibiotic resistance co-opted from stress responses to temperature.","volume":"13","author":"Cruz-Loya","year":"2019","journal-title":"ISME J."},{"key":"B27","doi-asserted-by":"publisher","first-page":"171","DOI":"10.1128\/MMBR.00051-14","article-title":"Lantibiotic resistance.","volume":"79","author":"Draper","year":"2015","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"B28","doi-asserted-by":"publisher","first-page":"453","DOI":"10.3389\/fcimb.2017.00453","article-title":"Cold-Shock Domain Family Proteins (Csps) are involved in regulation of virulence, cellular aggregation, and flagella-based motility in Listeria monocytogenes.","volume":"7","author":"Eshwar","year":"2017","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"B29","doi-asserted-by":"publisher","first-page":"5077","DOI":"10.2903\/j.efsa.2017.5077","article-title":"The European Union summary report on trends and sources of zoonoses, zoonotic agents and food-borne outbreaks in 2016.","volume":"15","year":"2017","journal-title":"EFSA J."},{"key":"B30","doi-asserted-by":"publisher","first-page":"31651","DOI":"10.1074\/jbc.M102855200","article-title":"Escherichia coli poly(A)- binding proteins that interact with components of degradosomes or impede RNA decay mediated by polynucleotide phosphorylase and RNase E.","volume":"276","author":"Feng","year":"2001","journal-title":"J. Biol. Chem."},{"key":"B31","doi-asserted-by":"publisher","first-page":"373","DOI":"10.1099\/mic.0.044776-0","article-title":"The cell envelope stress response mediated by the LiaFSRLm three-component system of Listeria monocytogenes is controlled via the phosphatase activity of the bifunctional histidine kinase LiaSLm.","volume":"157","author":"Fritsch","year":"2011","journal-title":"Microbiology"},{"key":"B32","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.ijfoodmicro.2006.07.008","article-title":"Listeria: a foodborne pathogen that knows how to survive.","volume":"113","author":"Gandhi","year":"2007","journal-title":"Int. J. Food Microbiol."},{"key":"B33","doi-asserted-by":"publisher","first-page":"1262","DOI":"10.1080\/10408398.2013.763765","article-title":"Nisin as a food preservative: part 1: physicochemical properties, antimicrobial activity, and main uses.","volume":"56","author":"Gharsallaoui","year":"2016","journal-title":"Crit. Rev. Food Sci. Nutr."},{"key":"B34","doi-asserted-by":"publisher","first-page":"849","DOI":"10.1126\/science.1063447","article-title":"Comparative genomics of Listeria species.","volume":"294","author":"Glaser","year":"2001","journal-title":"Science"},{"key":"B35","author":"G\u00f6ker","year":"2016","journal-title":"Analysing Growth Curves and Other User-Defined Data in Opm. 1\u201318."},{"key":"B36","author":"G\u00f6ker","year":"2016","journal-title":"opm: An R Package for Analysing Phenotype Microarray and Growth Curve Data. Phenotype Microarray Data: 1-68."},{"key":"B37","doi-asserted-by":"crossref","first-page":"741","DOI":"10.1046\/j.1365-2958.1997.5121878.x","article-title":"A family of cold shock proteins in Bacillus subtilis is essential for cellular growth and for efficient protein synthesis at optimal and low temperatures.","volume":"25","author":"Graumann","year":"1997","journal-title":"Mol. Microbiol."},{"key":"B38","doi-asserted-by":"publisher","first-page":"756","DOI":"10.1128\/AEM.68.2.756-764.2002","article-title":"Frequency of bacteriocin resistance development and associated fitness costs in Listeria monocytogenes.","volume":"68","author":"Gravesen","year":"2002","journal-title":"Appl. Environ. Microbiol."},{"key":"B39","doi-asserted-by":"publisher","first-page":"1669","DOI":"10.1128\/AEM.70.3.1669-1679.2004","article-title":"pbp2229-mediated nisin resistance mechanism in Listeria monocytogenes confers cross-protection to class IIa bacteriocins and affects virulence gene expression.","volume":"70","author":"Gravesen","year":"2004","journal-title":"Appl. Environ. Microbiol."},{"key":"B40","doi-asserted-by":"publisher","first-page":"127","DOI":"10.1089\/10766290152045002","article-title":"Spontaneous nisin-resistant Listeria monocytogenes mutants with increased expression of a putative penicillin-binding protein and their sensitivity to various antibiotics.","volume":"7","author":"Gravesen","year":"2001","journal-title":"Microb. Drug Resist."},{"key":"B41","doi-asserted-by":"publisher","first-page":"e00901","DOI":"10.1128\/IAI.00901-17","article-title":"The VirAB ABC transporter is required for VirR regulation of Listeria monocytogenes virulence and resistance to nisin.","volume":"86","author":"Grubaugh","year":"2018","journal-title":"Infect. Immun."},{"key":"B42","doi-asserted-by":"publisher","first-page":"635","DOI":"10.3389\/fmicb.2020.00635","article-title":"Nevertheless, she resisted \u2013 role of the environment on Listeria monocytogenes sensitivity to nisin treatment in a laboratory cheese model.","volume":"11","author":"Henderson","year":"2020","journal-title":"Front. Microbiol."},{"key":"B43","doi-asserted-by":"publisher","first-page":"601","DOI":"10.1038\/s41579-018-0049-5","article-title":"RNA-binding proteins in bacteria.","volume":"16","author":"Holmqvist","year":"2018","journal-title":"Nat. Rev. Microbiol."},{"key":"B44","doi-asserted-by":"publisher","first-page":"749","DOI":"10.1038\/nrm3884","article-title":"The structure, function and evolution of proteins that bind DNA and RNA.","volume":"15","author":"Hudson","year":"2014","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"B45","doi-asserted-by":"publisher","first-page":"2041","DOI":"10.3168\/jds.2019-17498","article-title":"Invited review: advances in nisin use for preservation of dairy products.","volume":"103","author":"Ibarra-S\u00e1nchez","year":"2020","journal-title":"J. Dairy Sci."},{"key":"B46","doi-asserted-by":"publisher","first-page":"e01470","DOI":"10.1128\/AEM.01470-19","article-title":"The VirAB-VirSR-AnrAB multicomponent system is involved in resistance of Listeria monocytogenes EGD-e to cephalosporins, bacitracin, nisin, benzalkonium chloride, and ethidium bromide.","volume":"85","author":"Jiang","year":"2019","journal-title":"Appl. Environ. Microbiol."},{"key":"B47","doi-asserted-by":"publisher","first-page":"107","DOI":"10.1111\/j.1574-6976.2007.00091.x","article-title":"Cell envelope stress response in Gram-positive bacteria.","volume":"32","author":"Jordan","year":"2008","journal-title":"FEMS Microbiol. Rev."},{"key":"B48","doi-asserted-by":"publisher","first-page":"3421","DOI":"10.1128\/AAC.47.11.3421-3429.2003","article-title":"CesRK, a two-component signal transduction system in Listeria monocytogenes, responds to the presence of cell wall-acting antibiotics and affects \u03b2-lactam resistance.","volume":"47","author":"Kallipolitis","year":"2003","journal-title":"Antimicrob. Agents Chemother."},{"key":"B49","doi-asserted-by":"publisher","first-page":"4553","DOI":"10.1128\/AEM.00648-15","article-title":"VirR-mediated resistance of Listeria monocytogenes against food antimicrobials and cross- protection induced by exposure to organic acid salts.","volume":"81","author":"Kang","year":"2015","journal-title":"Appl. Environ. Microbiol."},{"key":"B50","doi-asserted-by":"publisher","first-page":"63","DOI":"10.1590\/S1517-83822013005000025","article-title":"Antibacterial efficacy of nisin, pediocin 34 and enterocin FH99 against Listeria monocytogenes and cross resistance of its bacteriocin resistant variants to common food preservatives.","volume":"44","author":"Kaur","year":"2013","journal-title":"Braz. J. Microbiol."},{"key":"B51","doi-asserted-by":"publisher","first-page":"11","DOI":"10.1007\/s12602-011-9085-4","article-title":"Mechanism of nisin, pediocin 34, and enterocin FH99 resistance in Listeria monocytogenes.","volume":"4","author":"Kaur","year":"2012","journal-title":"Probiotics Antimicrob. Proteins"},{"key":"B52","doi-asserted-by":"publisher","first-page":"ME01","DOI":"10.7860\/JCDR\/2014\/8777.4356","article-title":"Ampicillin: rise fall and resurgence.","volume":"8","author":"Kaushik","year":"2014","journal-title":"J. Clin. Diagn. Res."},{"key":"B53","doi-asserted-by":"publisher","first-page":"1151","DOI":"10.3389\/fmicb.2016.01151","article-title":"Cold shock proteins: a minireview with special emphasis on Csp-family of enteropathogenic Yersinia.","volume":"7","author":"Keto-Timonen","year":"2016","journal-title":"Front. Microbiol."},{"key":"B54","doi-asserted-by":"publisher","first-page":"108662","DOI":"10.1016\/j.ijfoodmicro.2020.108662","article-title":"Cold-shock proteins affect desiccation tolerance, biofilm formation and motility in Listeria monocytogenes.","volume":"329","author":"Kragh","year":"2020","journal-title":"Int. J. Food Microbiol."},{"key":"B55","doi-asserted-by":"publisher","first-page":"1538","DOI":"10.3389\/fmicb.2019.01538","article-title":"New insights on the role of the pLMST6 plasmid in Listeria monocytogenes biocide tolerance and virulence.","volume":"10","author":"Kropac","year":"2019","journal-title":"Front. Microbiol."},{"key":"B56","doi-asserted-by":"publisher","first-page":"4177","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":"Lauer","year":"2002","journal-title":"J. Bacteriol."},{"key":"B57","doi-asserted-by":"publisher","first-page":"495","DOI":"10.1007\/s10295-013-1243-0","article-title":"Gene expression profiling of a nisin-sensitive Listeria monocytogenes scott A ctsR deletion mutant.","volume":"40","author":"Liu","year":"2013","journal-title":"J. Ind. Microbiol. Biotechnol."},{"key":"B58","doi-asserted-by":"publisher","first-page":"775","DOI":"10.1089\/fpd.2009.0458","article-title":"Reduced host cell invasiveness and oxidative stress tolerance in double and triple csp gene family deletion mutants of Listeria monocytogenes.","volume":"7","author":"Loepfe","year":"2010","journal-title":"Foodborne Pathog. Dis."},{"key":"B59","doi-asserted-by":"publisher","first-page":"771","DOI":"10.1111\/j.1365-2958.2006.05267.x","article-title":"LmrCD is a major multidrug resistance transporter in Lactococcus lactis.","volume":"61","author":"Lubelski","year":"2006","journal-title":"Mol. Microbiol."},{"key":"B60","doi-asserted-by":"publisher","first-page":"262","DOI":"10.1111\/jam.13479","article-title":"Genetic and environmental factors influence Listeria monocytogenes nisin resistance.","volume":"123","author":"Malekmohammadi","year":"2017","journal-title":"J. Appl. Microbiol."},{"key":"B61","doi-asserted-by":"publisher","first-page":"1367","DOI":"10.1111\/j.1365-2958.2005.04776.x","article-title":"VirR, a response regulator critical for Listeria monocytogenes virulence.","volume":"57","author":"Mandin","year":"2005","journal-title":"Mol. Microbiol."},{"key":"B62","doi-asserted-by":"publisher","first-page":"108952","DOI":"10.1016\/j.ijfoodmicro.2020.108952","article-title":"Antimicrobial effect of nisin in processed cheese \u2013 Quantification of residual nisin by LC-MS\/MS and development of new growth and growth boundary model for Listeria monocytogenes.","volume":"338","author":"Martinez-Rios","year":"2021","journal-title":"Int. J. Food Microbiol."},{"key":"B63","doi-asserted-by":"publisher","first-page":"2888","DOI":"10.1128\/AAC.48.8.2888-2896.2004","article-title":"Antibiotic-inducible promoter regulated by the cell envelope stress-sensing two- component system LiaRS of Bacillus subtilis.","volume":"48","author":"Mascher","year":"2004","journal-title":"Antimicrob. Agents Chemother."},{"key":"B64","doi-asserted-by":"publisher","first-page":"6824","DOI":"10.1073\/pnas.1620772114","article-title":"RNA target profiles direct the discovery of virulence functions for the cold-shock proteins CspC and CspE.","volume":"114","author":"Michaux","year":"2017","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B65","doi-asserted-by":"publisher","first-page":"6900","DOI":"10.1128\/JB.01673-12","article-title":"CspR, a cold shock RNA-binding protein involved in the long-term survival and the virulence of Enterococcus faecalis.","volume":"194","author":"Michaux","year":"2012","journal-title":"J. Bacteriol."},{"key":"B66","doi-asserted-by":"publisher","first-page":"1061","DOI":"10.3390\/microorganisms9051061","article-title":"Listeria monocytogenes cold shock proteins: small proteins with a huge impact.","volume":"9","author":"Muchaamba","year":"2021","journal-title":"Microorganisms"},{"key":"B67","doi-asserted-by":"publisher","first-page":"1865","DOI":"10.3389\/fmicb.2016.01865","article-title":"The role of stress and stress adaptations in determining the fate of the bacterial pathogen listeria monocytogenes in the food chain.","volume":"7","author":"NicAog\u00e1in","year":"2016","journal-title":"Front. Microbiol."},{"key":"B68","doi-asserted-by":"publisher","first-page":"963","DOI":"10.1099\/mic.0.055467-0","article-title":"Genome-wide transcriptional profiling of the cell envelope stress response and the role of LisRK and CesRK in Listeria monocytogenes.","volume":"158","author":"Nielsen","year":"2012","journal-title":"Microbiology"},{"key":"B69","doi-asserted-by":"publisher","first-page":"1057","DOI":"10.1089\/fpd.2009.0292","article-title":"sigma(B) and sigma(L) contribute to Listeria monocytogenes 10403S response to the antimicrobial peptides SdpC and nisin.","volume":"6","author":"Palmer","year":"2009","journal-title":"Foodborne Pathog. Dis."},{"key":"B70","doi-asserted-by":"publisher","first-page":"101","DOI":"10.1002\/jobm.201100288","article-title":"Osmotic stress adaptations in rhizobacteria.","volume":"53","author":"Paul","year":"2013","journal-title":"J. Basic Microbiol."},{"key":"B71","doi-asserted-by":"publisher","first-page":"788","DOI":"10.4161\/rna.7.6.13482","article-title":"RNA remodeling and gene regulation by cold shock proteins.","volume":"7","author":"Phadtare","year":"2010","journal-title":"RNA Biol."},{"key":"B72","doi-asserted-by":"publisher","first-page":"827","DOI":"10.1002\/9781119004813.ch80","article-title":"Gene regulation by cold shock proteins via transcription antitermination","author":"Phadtare","year":"2016","journal-title":"Stress and Environmental Regulation of Gene Expression and Adaptation in Bacteria"},{"key":"B73","doi-asserted-by":"publisher","first-page":"7239","DOI":"10.1074\/jbc.M111496200","article-title":"The nucleic acid melting activity of Escherichia coli CspE is critical for transcription antitermination and cold acclimation of cells.","volume":"277","author":"Phadtare","year":"2002","journal-title":"J. Biol. Chem."},{"key":"B74","doi-asserted-by":"publisher","first-page":"109170","DOI":"10.1016\/j.ijfoodmicro.2021.109170","article-title":"Proteomic analysis reveals differential responses of Listeria monocytogenes to free and nanoencapsulated nisin.","volume":"346","author":"Pinilla","year":"2021","journal-title":"Int. J. Food Microbiol."},{"key":"B75","doi-asserted-by":"publisher","first-page":"154","DOI":"10.1186\/1471-2180-14-154","article-title":"Identification and characterization of an operon, msaABCR, that controls virulence and biofilm development in Staphylococcus aureus.","volume":"14","author":"Sahukhal","year":"2014","journal-title":"BMC Microbiol."},{"key":"B76","doi-asserted-by":"publisher","first-page":"5584","DOI":"10.1128\/AEM.01812-13","article-title":"PrfA-like transcription factor gene lmo0753 contributes to L-rhamnose utilization in Listeria monocytogenes strains associated with human food-borne infections.","volume":"79","author":"Salazar","year":"2013","journal-title":"Appl. Environ. Microbiol."},{"key":"B77","doi-asserted-by":"publisher","first-page":"179","DOI":"10.1016\/J.IFSET.2018.06.008","article-title":"Nisin and other antimicrobial peptides: production, mechanisms of action, and application in active food packaging.","volume":"48","author":"Santos","year":"2018","journal-title":"Innov. Food Sci. Emerg. Technol."},{"key":"B78","doi-asserted-by":"publisher","first-page":"1023","DOI":"10.1089\/fpd.2013.1562","article-title":"Cold shock proteins contribute to the regulation of listeriolysin O production in Listeria monocytogenes.","volume":"10","author":"Sch\u00e4rer","year":"2013","journal-title":"Foodborne Pathog. Dis."},{"key":"B79","doi-asserted-by":"crossref","first-page":"1621","DOI":"10.1128\/AEM.02154-08","article-title":"Role of cold shock proteins in growth of Listeria monocytogenes under cold and osmotic stress conditions.","volume":"75","author":"Schmid","year":"2009","journal-title":"Appl. Environ. Microbiol."},{"key":"B80","doi-asserted-by":"publisher","first-page":"a000414","DOI":"10.1101\/cshperspect.a000414","article-title":"The bacterial cell envelope.","volume":"2","author":"Silhavy","year":"2010","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"B81","doi-asserted-by":"publisher","first-page":"103906","DOI":"10.1016\/j.jprot.2020.103906","article-title":"Nisin influence on the expression of Listeria monocytogenes surface proteins.","volume":"226","author":"Stincone","year":"2020","journal-title":"J. Proteomics"},{"key":"B82","doi-asserted-by":"publisher","first-page":"265","DOI":"10.1111\/j.1574-6968.2007.00633.x","article-title":"Evaluation of housekeeping genes in Listeria monocytogenes as potential internal control references for normalizing mRNA expression levels in stress adaptation models using real-time PCR.","volume":"269","author":"Tasara","year":"2007","journal-title":"FEMS Microbiol. Lett."},{"key":"B83","doi-asserted-by":"publisher","first-page":"1325","DOI":"10.1111\/j.1365-2958.2006.05452.x","article-title":"The MprF protein is required for lysinylation of phospholipids in listerial membranes and confers resistance to cationic antimicrobial peptides (CAMPs) on Listeria monocytogenes.","volume":"62","author":"Thedieck","year":"2006","journal-title":"Mol. Microbiol."},{"key":"B84","doi-asserted-by":"publisher","first-page":"9300","DOI":"10.1021\/bi8006737","article-title":"Multidrug transport by the ABC transporter Sav1866 from Staphylococcus aureus.","volume":"47","author":"Velamakanni","year":"2008","journal-title":"Biochemistry"},{"key":"B85","doi-asserted-by":"publisher","first-page":"549531","DOI":"10.3389\/fmicb.2020.549531","article-title":"The analysis of field strains isolated from food, animal and clinical sources uncovers natural mutations in Listeria monocytogenes nisin resistance genes.","volume":"11","author":"Wambui","year":"2020","journal-title":"Front. Microbiol."},{"key":"B86","doi-asserted-by":"publisher","first-page":"417","DOI":"10.1007\/s11427-015-4981-6","article-title":"RNA-seq reveals the critical role of CspA in regulating Brucella melitensis metabolism and virulence.","volume":"59","author":"Wang","year":"2016","journal-title":"Sci. China Life Sci."},{"key":"B87","doi-asserted-by":"publisher","first-page":"27","DOI":"10.1111\/1574-6968.12430","article-title":"Cold shock protein A plays an important role in the stress adaptation and virulence of Brucella melitensis.","volume":"354","author":"Wang","year":"2014","journal-title":"FEMS Microbiol. Lett."},{"key":"B88","doi-asserted-by":"publisher","first-page":"7","DOI":"10.1093\/jac\/14.suppl_d.7","article-title":"Mode of action and in-vitro activity of vancomycin.","volume":"14","author":"Watanakunakorn","year":"1984","journal-title":"J. Antimicrob. Chemother."},{"key":"B89","doi-asserted-by":"publisher","first-page":"1772","DOI":"10.1074\/jbc.M006770200","article-title":"Specific binding of nisin to the peptidoglycan precursor lipid II combines pore formation and inhibition of cell wall biosynthesis for potent antibiotic activity.","volume":"276","author":"Wiedemann","year":"2001","journal-title":"J. Biol. Chem."},{"key":"B90","doi-asserted-by":"publisher","first-page":"710085","DOI":"10.3389\/fmicb.2021.710085","article-title":"Adaptive response of Listeria monocytogenes to the stress factors in the food processing environment.","volume":"12","author":"Wiktorczyk-Kapischke","year":"2021","journal-title":"Front. Microbiol."},{"key":"B91","doi-asserted-by":"publisher","first-page":"6326","DOI":"10.1128\/jb.174.20.6326-6335.1992","article-title":"Characterization of cspB, a Bacillus subtilis inducible cold shock gene affecting cell viability at low temperatures.","volume":"174","author":"Willimsky","year":"1992","journal-title":"J. Bacteriol."},{"key":"B92","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1080\/10408398.2021.1913570","article-title":"Recent advances in understanding the effect of acid-adaptation on the cross-protection to food-related stress of common foodborne pathogens.","volume":"27","author":"Wu","year":"2021","journal-title":"Crit. Rev. Food Sci. Nutr."},{"key":"B93","doi-asserted-by":"publisher","first-page":"25","DOI":"10.1016\/j.jgar.2018.06.003","article-title":"Transcriptomic study on persistence and survival of Listeria monocytogenes following lethal treatment with nisin.","volume":"15","author":"Wu","year":"2018","journal-title":"J. Glob. Antimicrob. Resist."},{"key":"B94","doi-asserted-by":"publisher","first-page":"413","DOI":"10.1007\/s13213-013-0679-9","article-title":"Mechanisms of nisin resistance in Gram-positive bacteria.","volume":"64","author":"Zhou","year":"2014","journal-title":"Ann. Microbiol."}],"container-title":["Frontiers in Microbiology"],"original-title":[],"link":[{"URL":"https:\/\/www.frontiersin.org\/articles\/10.3389\/fmicb.2021.811939\/full","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,12,24]],"date-time":"2021-12-24T09:33:21Z","timestamp":1640338401000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.frontiersin.org\/articles\/10.3389\/fmicb.2021.811939\/full"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,12,24]]},"references-count":94,"alternative-id":["10.3389\/fmicb.2021.811939"],"URL":"https:\/\/doi.org\/10.3389\/fmicb.2021.811939","relation":{},"ISSN":["1664-302X"],"issn-type":[{"value":"1664-302X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,12,24]]},"article-number":"811939"}}