{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,20]],"date-time":"2026-09-20T01:14:52Z","timestamp":1789866892157,"version":"4.0.1"},"reference-count":54,"publisher":"SAGE Publications","issue":"12","license":[{"start":{"date-parts":[[2018,12,1]],"date-time":"2018-12-01T00:00:00Z","timestamp":1543622400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.sagepub.com\/page\/policies\/text-and-data-mining-license"}],"content-domain":{"domain":["journals.sagepub.com"],"crossmark-restriction":true},"short-container-title":["OMICS: A Journal of Integrative Biology"],"published-print":{"date-parts":[[2018,12,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    The cell surface proteome of the foodborne pathogen\n                    <jats:italic toggle=\"yes\">Listeria monocytogenes<\/jats:italic>\n                    , the etiological agent of listeriosis, is critical for understanding the physiological processes associated with stress resistance and persistence in the environment. In this context, the most widespread mode of growth for bacterial cells in natural and industrial environments is in biofilms. Cell surface proteins are, however, challenging to characterize because of their low abundance and poor solubility. Moreover, cell surface protein extracts are usually contaminated with cytoplasmic proteins that constitute the main signal in proteomic analysis. This study aimed to compare the efficiency of three methods to extract and explore surface proteins of\n                    <jats:italic toggle=\"yes\">L. monocytogenes<\/jats:italic>\n                    growing in a biofilm: trypsin shaving, biotinylation, and cell fractionation. Peptide separation and identification were performed by shotgun proteomics using high-performance liquid chromatography combined with tandem mass spectrometry (LC-MS\/MS). The biotinylation method was the most effective in extracting surface proteins, with the lowest rate of contamination by cytoplasmic proteins. Although presenting a higher contamination rate in cytoplasmic proteins, the other two techniques allowed the identification of additional surface proteins. Seven proteins were commonly retrieved by the three methods. The extracted proteins belong to several functional classes, involved in virulence, transport, or metabolic pathways. Finally, the three extraction methods seemed complementary and their combined use improved the exploration of the bacterial surface proteome. These new findings collectively inform future discovery and translational proteomics for clinical, environmental health, and industrial applications.\n                  <\/jats:p>","DOI":"10.1089\/omi.2018.0144","type":"journal-article","created":{"date-parts":[[2018,11,20]],"date-time":"2018-11-20T14:26:51Z","timestamp":1542724011000},"page":"779-787","update-policy":"https:\/\/doi.org\/10.1177\/sage-journals-update-policy","source":"Crossref","is-referenced-by-count":18,"title":["Comparison of three methods for cell surface proteome extraction of\n                    <i>Listeria monocytogenes<\/i>\n                    biofilms"],"prefix":"10.1177","volume":"22","author":[{"given":"Julia","family":"Esbelin","sequence":"first","affiliation":[{"name":"Universit\u00e9 Clermont Auvergne, INRA, UMR Microbiologie Environnement Digestif Sant\u00e9 (MEDiS), Saint-Gen\u00e8s Champanelle, France."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tiago","family":"Santos","sequence":"additional","affiliation":[{"name":"Universit\u00e9 Clermont Auvergne, INRA, UMR Microbiologie Environnement Digestif Sant\u00e9 (MEDiS), Saint-Gen\u00e8s Champanelle, France."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"C\u00e9line","family":"Ribi\u00e8re","sequence":"additional","affiliation":[{"name":"Universit\u00e9 Clermont Auvergne, INRA, UMR Microbiologie Environnement Digestif Sant\u00e9 (MEDiS), Saint-Gen\u00e8s Champanelle, France."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Micka\u00ebl","family":"Desvaux","sequence":"additional","affiliation":[{"name":"Universit\u00e9 Clermont Auvergne, INRA, UMR Microbiologie Environnement Digestif Sant\u00e9 (MEDiS), Saint-Gen\u00e8s Champanelle, France."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Didier","family":"Viala","sequence":"additional","affiliation":[{"name":"INRA, Plate-Forme d'Exploration du M\u00e9tabolisme composante prot\u00e9omique (PFEMcp), Saint-Gen\u00e8s Champanelle, France."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christophe","family":"Chambon","sequence":"additional","affiliation":[{"name":"INRA, Plate-Forme d'Exploration du M\u00e9tabolisme composante prot\u00e9omique (PFEMcp), Saint-Gen\u00e8s Champanelle, France."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michel","family":"H\u00e9braud","sequence":"additional","affiliation":[{"name":"Universit\u00e9 Clermont Auvergne, INRA, UMR Microbiologie Environnement Digestif Sant\u00e9 (MEDiS), Saint-Gen\u00e8s Champanelle, France."},{"name":"INRA, Plate-Forme d'Exploration du M\u00e9tabolisme composante prot\u00e9omique (PFEMcp), Saint-Gen\u00e8s Champanelle, France."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"179","published-online":{"date-parts":[[2018,12,20]]},"reference":[{"key":"e_1_3_3_2_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1469-0691.2009.03109.x"},{"key":"e_1_3_3_3_1","doi-asserted-by":"publisher","DOI":"10.1080\/1040841X.2016.1208146"},{"key":"e_1_3_3_4_1","doi-asserted-by":"publisher","DOI":"10.1128\/JB.00976-06"},{"key":"e_1_3_3_5_1","doi-asserted-by":"publisher","DOI":"10.1128\/MMBR.00039-06"},{"key":"e_1_3_3_6_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.2008.06211.x"},{"key":"e_1_3_3_7_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0966-842X(02)02342-9"},{"key":"e_1_3_3_8_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.mib.2006.04.008"},{"key":"e_1_3_3_9_1","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.73.8.4853-4863.2005"},{"key":"e_1_3_3_10_1","doi-asserted-by":"publisher","DOI":"10.3389\/fmicb.2018.00100"},{"key":"e_1_3_3_11_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1574-6968.2006.00122.x"},{"key":"e_1_3_3_12_1","first-page":"359","article-title":"Analysis of Cell Envelope Proteins","author":"Desvaux M","year":"2008","unstructured":"Desvaux M, , and H\u00e9braud M. (2008). Analysis of Cell Envelope Proteins. Handbook of Listeria. Florida: Taylor and Francis Group, 359\u2013393.","journal-title":"Handbook of Listeria"},{"key":"e_1_3_3_13_1","first-page":"313","article-title":"Bacterial secreted proteins: secretory mechanisms and role in pathogenesis","author":"Desvaux M","year":"2009","unstructured":"Desvaux M, , and H\u00e9braud M. (2009). Bacterial secreted proteins: secretory mechanisms and role in pathogenesis. In: Handbook of Listeria. Wooldridge K, ed. Norwich, United Kingdom: Caister Academic Press, 313\u2013345.","journal-title":"Handbook of Listeria"},{"key":"e_1_3_3_14_1","doi-asserted-by":"publisher","DOI":"10.1002\/pmic.201000062"},{"key":"e_1_3_3_15_1","doi-asserted-by":"publisher","DOI":"10.1002\/pmic.201100134"},{"key":"e_1_3_3_16_1","doi-asserted-by":"publisher","DOI":"10.1002\/pmic.201000823"},{"key":"e_1_3_3_17_1","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.micro.57.030502.090934"},{"key":"e_1_3_3_18_1","doi-asserted-by":"publisher","DOI":"10.3389\/fmicb.2015.00841"},{"key":"e_1_3_3_19_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.meatsci.2013.05.023"},{"key":"e_1_3_3_20_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.1063447"},{"key":"e_1_3_3_21_1","doi-asserted-by":"publisher","DOI":"10.1002\/pmic.200402075"},{"key":"e_1_3_3_22_1","doi-asserted-by":"publisher","DOI":"10.1002\/pmic.200700550"},{"key":"e_1_3_3_23_1","doi-asserted-by":"publisher","DOI":"10.1186\/1471-2180-10-121"},{"key":"e_1_3_3_24_1","doi-asserted-by":"publisher","DOI":"10.1007\/978-1-4939-0703-8_10"},{"key":"e_1_3_3_25_1","doi-asserted-by":"publisher","DOI":"10.1021\/pr901143a"},{"key":"e_1_3_3_26_1","doi-asserted-by":"publisher","DOI":"10.1021\/pr1009838"},{"key":"e_1_3_3_27_1","doi-asserted-by":"publisher","DOI":"10.1002\/pmic.200400928"},{"key":"e_1_3_3_28_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2133653100"},{"key":"e_1_3_3_29_1","doi-asserted-by":"publisher","DOI":"10.1074\/mcp.M113.029066"},{"key":"e_1_3_3_30_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.jprot.2018.03.026"},{"key":"e_1_3_3_31_1","first-page":"7","article-title":"Surfaceome and exoproteome of a clinical sequence type 398 methicillin resistant Staphylococcus aureus strain","volume":"3","author":"Monteiro R","year":"2015","unstructured":"Monteiro R, , H\u00e9braud M, , Chafsey I, et al. (2015). Surfaceome and exoproteome of a clinical sequence type 398 methicillin resistant Staphylococcus aureus strain. Bioch Bioph Rep, 3, 7\u201313.","journal-title":"Bioch Bioph Rep"},{"key":"e_1_3_3_32_1","doi-asserted-by":"publisher","DOI":"10.1128\/MMBR.63.1.174-229.1999"},{"key":"e_1_3_3_33_1","doi-asserted-by":"publisher","DOI":"10.1002\/pmic.201000808"},{"key":"e_1_3_3_34_1","doi-asserted-by":"publisher","DOI":"10.1002\/pmic.200900564"},{"key":"e_1_3_3_35_1","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2958.1998.01016.x"},{"key":"e_1_3_3_36_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.jprot.2012.04.037"},{"key":"e_1_3_3_37_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.jprot.2013.03.035"},{"key":"e_1_3_3_38_1","first-page":"29","article-title":"Analysis of the peptidoglycan hydrolases of Listeria monocytogenes: Multiple enzymes with multiple functions","author":"Popowska M","year":"2004","unstructured":"Popowska M. (2004). Analysis of the peptidoglycan hydrolases of Listeria monocytogenes: Multiple enzymes with multiple functions. Pol J Microbiol 53, Suppl, 29\u201334.","journal-title":"Pol J Microbiol 53"},{"key":"e_1_3_3_39_1","first-page":"237","article-title":"Murein-hydrolyzing activity of flagellin FlaA of Listeria monocytogenes","volume":"53","author":"Popowska M","year":"2004","unstructured":"Popowska M, , and Markiewicz Z. (2004). Murein-hydrolyzing activity of flagellin FlaA of Listeria monocytogenes. Pol J Microbiol, 53, 237\u2013241.","journal-title":"Pol J Microbiol"},{"key":"e_1_3_3_40_1","doi-asserted-by":"publisher","DOI":"10.1021\/pr400768v"},{"key":"e_1_3_3_41_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.jprot.2015.01.007"},{"key":"e_1_3_3_42_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1462-2920.2010.02378.x"},{"key":"e_1_3_3_43_1","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0042982"},{"key":"e_1_3_3_44_1","doi-asserted-by":"publisher","DOI":"10.1038\/nbt1179"},{"key":"e_1_3_3_45_1","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0111880"},{"key":"e_1_3_3_46_1","doi-asserted-by":"publisher","DOI":"10.1128\/JB.01132-06"},{"key":"e_1_3_3_47_1","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.mi.37.100183.002441"},{"key":"e_1_3_3_48_1","doi-asserted-by":"publisher","DOI":"10.1089\/omi.2010.0113"},{"key":"e_1_3_3_49_1","doi-asserted-by":"publisher","DOI":"10.1128\/mr.57.2.320-346.1993"},{"key":"e_1_3_3_50_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.mimet.2015.01.004"},{"key":"e_1_3_3_51_1","doi-asserted-by":"publisher","DOI":"10.3390\/pathogens5020040"},{"key":"e_1_3_3_52_1","doi-asserted-by":"publisher","DOI":"10.1128\/MMBR.64.3.515-547.2000"},{"key":"e_1_3_3_53_1","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0011634"},{"key":"e_1_3_3_54_1","doi-asserted-by":"publisher","DOI":"10.1128\/JB.01768-14"},{"key":"e_1_3_3_55_1","doi-asserted-by":"publisher","DOI":"10.1084\/jem.20111843"}],"container-title":["OMICS: A Journal of Integrative Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.sagepub.com\/doi\/full-xml\/10.1089\/omi.2018.0144","content-type":"application\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/journals.sagepub.com\/doi\/pdf\/10.1089\/omi.2018.0144","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/journals.sagepub.com\/doi\/pdf\/10.1089\/omi.2018.0144","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,5,1]],"date-time":"2026-05-01T23:02:23Z","timestamp":1777676543000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.sagepub.com\/doi\/10.1089\/omi.2018.0144"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,12,1]]},"references-count":54,"journal-issue":{"issue":"12","published-print":{"date-parts":[[2018,12,1]]}},"alternative-id":["10.1089\/omi.2018.0144"],"URL":"https:\/\/doi.org\/10.1089\/omi.2018.0144","relation":{},"ISSN":["1536-2310","1557-8100"],"issn-type":[{"value":"1536-2310","type":"print"},{"value":"1557-8100","type":"electronic"}],"subject":[],"published":{"date-parts":[[2018,12,1]]}}}