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Oak stress\u2010induced protein 1 (OSIP1) is a fungal\u2010specific protein with unknown function. By using\n                    <jats:italic>Podospora anserina<\/jats:italic>\n                    and\n                    <jats:italic>Phanerochaete chrysosporium<\/jats:italic>\n                    as models, we combined both\n                    <jats:italic>in vivo<\/jats:italic>\n                    functional approaches and biophysical characterization of OSIP1 recombinant protein. The\n                    <jats:italic>P. anserina OSIP1<\/jats:italic>\n                    <jats:sup>\u0394<\/jats:sup>\n                    mutant showed an increased sensitivity to the antifungal caspofungin compared to the wild type. This correlated with the production of a weakened extracellular exopolysaccharide\/protein matrix (ECM). Since the recombinant OSIP1 from\n                    <jats:italic>P. chrysosporium<\/jats:italic>\n                    self\u2010assembled as fibers and was capable of gelation, it is likely that OSIP1 is linked to ECM formation that acts as a physical barrier preventing drug toxicity. Moreover, compared to the wild type, the\n                    <jats:italic>OSIP1<\/jats:italic>\n                    <jats:sup>\u0394<\/jats:sup>\n                    mutant was more sensitive to oak extractives including chaotropic phenols and benzenes. It exhibited a strongly modified secretome pattern and an increased production of proteins associated to the cell\u2010wall integrity signalling pathway, when grown on oak sawdust. This demonstrates that OSIP1 has also an important role in fungal resistance to extractive\u2010induced stress.\n                  <\/jats:p>","DOI":"10.1111\/1462-2920.15381","type":"journal-article","created":{"date-parts":[[2021,1,4]],"date-time":"2021-01-04T01:45:24Z","timestamp":1609724724000},"page":"1594-1607","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["<scp>OSIP1<\/scp>\n                    is a self\u2010assembling\n                    <scp>DUF3129<\/scp>\n                    protein required to protect fungal cells from toxins and stressors"],"prefix":"10.1111","volume":"23","author":[{"given":"Nicolas","family":"Valette","sequence":"first","affiliation":[{"name":"Universit\u00e9 de Lorraine INRAE, Interactions Arbres\/Micro\u2010organismes (IAM), UMR 1136  Nancy 54000 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Cit\u00e9, Laboratoire Interdisciplinaire des Energies de Demain (LIED)  Paris 75205 France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Philippe","family":"Silar","sequence":"additional","affiliation":[{"name":"Universit\u00e9 Paris Diderot Sorbonne Paris Cit\u00e9, Laboratoire Interdisciplinaire des Energies de Demain (LIED)  Paris 75205 France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christophe","family":"Guyeux","sequence":"additional","affiliation":[{"name":"Computer Science Department, FEMTO\u2010ST Institute, UMR 6174 CNRS Universit\u00e9 de Bourgogne Franche\u2010Comt\u00e9, 16 route de Gray  Besan\u00e7on 25030 France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jean\u2010Claude","family":"Charr","sequence":"additional","affiliation":[{"name":"Computer Science Department, FEMTO\u2010ST Institute, UMR 6174 CNRS Universit\u00e9 de Bourgogne Franche\u2010Comt\u00e9, 16 route de Gray  Besan\u00e7on 25030 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