{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,23]],"date-time":"2026-08-23T14:51:47Z","timestamp":1787496707797,"version":"build-2736575974"},"reference-count":150,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2022,6,27]],"date-time":"2022-06-27T00:00:00Z","timestamp":1656288000000},"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. Immunol."],"abstract":"<jats:p>Posttranslational modifications (PTMs) allow to control molecular and cellular functions in response to specific signals and changes in the microenvironment of cells. They regulate structure, localization, stability, and function of proteins in a spatial and temporal manner. Among them, specific thiol modifications of cysteine (Cys) residues facilitate rapid signal transduction. In fact, Cys is unique because it contains the highly reactive thiol group that can undergo different reversible and irreversible modifications. Upon inflammation and changes in the cellular microenvironment, many extracellular soluble and membrane proteins undergo thiol modifications, particularly dithiol\u2013disulfide exchange, S-glutathionylation, and S-nitrosylation. Among others, these thiol switches are essential for inflammatory signaling, regulation of gene expression, cytokine release, immunoglobulin function and isoform variation, and antigen presentation. Interestingly, also the redox state of bacterial and viral proteins depends on host cell-mediated redox reactions that are critical for invasion and infection. Here, we highlight mechanistic thiol switches in inflammatory pathways and infections including cholera, diphtheria, hepatitis, human immunodeficiency virus (HIV), influenza, and coronavirus disease 2019 (COVID-19).<\/jats:p>","DOI":"10.3389\/fimmu.2022.932525","type":"journal-article","created":{"date-parts":[[2022,6,27]],"date-time":"2022-06-27T02:11:05Z","timestamp":1656295865000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":8,"title":["Thiol Modifications in the Extracellular Space\u2014Key Proteins in Inflammation and Viral Infection"],"prefix":"10.3389","volume":"13","author":[{"given":"Kathrin A.","family":"Br\u00fccksken","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paola","family":"Loreto Palacio","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eva-Maria","family":"Hanschmann","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2022,6,27]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1038\/srep00090","article-title":"Proteome-Wide Post-Translational Modification Statistics: Frequency Analysis and Curation of the Swiss-Prot Database","volume":"1","author":"Khoury","year":"2011","journal-title":"Sci Rep"},{"key":"B2","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1093\/database\/baab012","article-title":"Post-Translational Modifications in Proteins: Resources, Tools and Prediction Methods","volume":"2021","author":"Ramazi","year":"2021","journal-title":"Database"},{"key":"B3","doi-asserted-by":"publisher","DOI":"10.2144\/000112201","article-title":"Analysis of Posttranslational Modifications of Proteins by Tandem Mass Spectrometry","volume":"40","author":"Larsen","year":"2006","journal-title":"Biotechniques"},{"key":"B4","doi-asserted-by":"publisher","DOI":"10.1007\/978-3-030-15950-4_10","article-title":"The Methods Employed in Mass Spectrometric Analysis of Posttranslational Modifications (PTMs) and Protein-Protein Interactions (PPIs)","volume":"1140","author":"Yakubu","year":"2019","journal-title":"Adv Exp Med Biol"},{"key":"B5","doi-asserted-by":"publisher","first-page":"0","DOI":"10.1016\/j.mcpro.2021.100129","article-title":"Decoding Post-Translational Modification Crosstalk With Proteomics","volume":"20","author":"Leutert","year":"2021","journal-title":"Mol Cell Proteomics"},{"key":"B6","doi-asserted-by":"publisher","first-page":"193","DOI":"10.3109\/1354750X.2011.557440","article-title":"Post-Translational Modifications of the Extracellular Matrix are Key Events in Cancer Progression: Opportunities for Biochemical Marker Development","volume":"16","author":"Leeming","year":"2011","journal-title":"Biomarkers"},{"key":"B7","doi-asserted-by":"publisher","first-page":"8","DOI":"10.1016\/j.semcdb.2015.02.012","article-title":"Oxidative and Other Posttranslational Modifications in Extracellular Vesicle Biology","volume":"40","author":"Szab\u00f3-Taylor","year":"2015","journal-title":"Semin Cell Dev Biol"},{"key":"B8","doi-asserted-by":"publisher","first-page":"45","DOI":"10.1007\/978-3-030-67171-6_3","article-title":"The Role of Post-Translational Modifications in Targeting Protein Cargo to Extracellular Vesicles","volume":"97","author":"Atukorala","year":"2021","journal-title":"Subcellular Biochem"},{"key":"B9","doi-asserted-by":"publisher","DOI":"10.1007\/978-3-319-06068-2_13","article-title":"Redox Proteomics: From Bench to Bedside","volume":"806","author":"Ckless","year":"2014","journal-title":"Adv Exp Med Biol"},{"key":"B10","doi-asserted-by":"publisher","DOI":"10.1089\/ars.2012.4599","article-title":"Thioredoxins, Glutaredoxins, and Peroxiredoxins\u2014Molecular Mechanisms and Health Significance: From Cofactors to Antioxidants to Redox Signaling","volume":"19","author":"Hanschmann","year":"2013","journal-title":"Antioxid Redox Signal"},{"key":"B11","doi-asserted-by":"publisher","DOI":"10.1016\/j.redox.2016.12.035","article-title":"Hydrogen Peroxide as a Central Redox Signaling Molecule in Physiological Oxidative Stress: Oxidative Eustress","volume":"11","author":"Sies","year":"2017","journal-title":"Redox Biol"},{"key":"B12","doi-asserted-by":"publisher","DOI":"10.1515\/hsz-2020-0266","article-title":"Thiol Switches in Membrane Proteins - 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