{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T10:31:24Z","timestamp":1791109884454,"version":"4.1.0"},"reference-count":62,"publisher":"American Society for Microbiology","issue":"12","license":[{"start":{"date-parts":[[2011,12,1]],"date-time":"2011-12-01T00:00:00Z","timestamp":1322697600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Eukaryot Cell"],"published-print":{"date-parts":[[2011,12]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Echinocandin drugs such as caspofungin (CASP), micafungin, and anidulafungin inhibit fungal cell wall biogenesis by blocking Fks1-mediated \u03b2-glucan deposition into the cell surface. Candins have become suitable drugs to treat life-threatening diseases caused by several fungal species, including\n            <jats:named-content content-type=\"genus-species\">Candida albicans<\/jats:named-content>\n            , that are pathogenic for humans\n            <jats:italic>.<\/jats:italic>\n            Here, we present the discovery of a novel CASP-induced flocculation phenotype of\n            <jats:named-content content-type=\"genus-species\">C. albicans<\/jats:named-content>\n            , which formed large cell aggregates in the presence of CASP. High concentrations of sugars such as mannose or glucose inhibit CASP-induced flocculation and improve survival of\n            <jats:named-content content-type=\"genus-species\">C. albicans<\/jats:named-content>\n            cells exposed to CASP. Notably, exposure of\n            <jats:named-content content-type=\"genus-species\">C. albicans<\/jats:named-content>\n            cells to CASP triggers Efg1-dependent expression of the adhesin\n            <jats:italic>ALS1<\/jats:italic>\n            and induces invasive growth on agar plates. Indeed, cells lacking either Efg1 or Als1 show strongly diminished CASP-induced flocculation, and the absence of Efg1 leads to marked CASP hypersensitivity. On the other hand, CASP-induced invasive growth is enhanced in cells lacking Efg1. Hence, CASP stress drives an Efg1-dependent response, indicating that this multifunctional transcriptional regulator, which is otherwise involved in filamentation, white-to-opaque switching, and virulence, also modulates cell wall remodeling upon CASP challenge. Taken together, our data suggest that CASP-induced cell wall damage activates Efg1 in parallel with the known cell integrity stress signaling pathway to coordinate cell wall remodeling.\n          <\/jats:p>","DOI":"10.1128\/ec.05187-11","type":"journal-article","created":{"date-parts":[[2011,10,29]],"date-time":"2011-10-29T03:13:57Z","timestamp":1319858037000},"page":"1694-1704","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":43,"title":["Efg1 Controls Caspofungin-Induced Cell Aggregation of Candida albicans through the Adhesin Als1"],"prefix":"10.1128","volume":"10","author":[{"given":"Christa","family":"Gregori","sequence":"first","affiliation":[{"name":"Medical University of Vienna, Max F. 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