{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,14]],"date-time":"2026-09-14T23:41:43Z","timestamp":1789429303317,"version":"build-2803163510"},"reference-count":32,"publisher":"American Society for Microbiology","issue":"3","license":[{"start":{"date-parts":[[2013,3,1]],"date-time":"2013-03-01T00:00:00Z","timestamp":1362096000000},"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":[[2013,3]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            In order to colonize the host and cause disease,\n            <jats:named-content content-type=\"genus-species\">Candida albicans<\/jats:named-content>\n            must avoid being killed by host defense peptides. Previously, we determined that the regulatory protein Ssd1 governs antimicrobial peptide resistance in\n            <jats:named-content content-type=\"genus-species\">C. albicans<\/jats:named-content>\n            . Here, we sought to identify additional genes whose products govern susceptibility to antimicrobial peptides. We discovered that a\n            <jats:italic>bcr1<\/jats:italic>\n            \u0394\/\u0394 mutant, like the\n            <jats:italic>ssd1<\/jats:italic>\n            \u0394\/\u0394 mutant, had increased susceptibility to the antimicrobial peptides, protamine, RP-1, and human \u03b2 defensin-2. Homozygous deletion of\n            <jats:italic>BCR1<\/jats:italic>\n            in the\n            <jats:italic>ssd1<\/jats:italic>\n            \u0394\/\u0394 mutant did not result in a further increase in antimicrobial peptide susceptibility. Exposure of the\n            <jats:italic>bcr1<\/jats:italic>\n            \u0394\/\u0394 and\n            <jats:italic>ssd1<\/jats:italic>\n            \u0394\/\u0394 mutants to RP-1 induced greater loss of mitochondrial membrane potential and increased plasma membrane permeability than with the control strains. Therefore, Bcr1 and Ssd1 govern antimicrobial peptide susceptibility and likely function in the same pathway. Furthermore,\n            <jats:italic>BCR1<\/jats:italic>\n            mRNA expression was downregulated in the\n            <jats:italic>ssd1<\/jats:italic>\n            \u0394\/\u0394 mutant, and the forced expression of\n            <jats:italic>BCR1<\/jats:italic>\n            in the\n            <jats:italic>ssd1<\/jats:italic>\n            \u0394\/\u0394 mutant partially restored antimicrobial peptide resistance. These results suggest that Bcr1 functions downstream of Ssd1. Interestingly, overexpression of 11 known Bcr1 target genes in the\n            <jats:italic>bcr1<\/jats:italic>\n            \u0394\/\u0394 mutant failed to restore antimicrobial peptide resistance, suggesting that other Bcr1 target genes are likely responsible for antimicrobial peptide resistance. Collectively, these results demonstrate that Bcr1 functions downstream of Ssd1 to govern antimicrobial peptide resistance by maintaining mitochondrial energetics and reducing membrane permeabilization.\n          <\/jats:p>","DOI":"10.1128\/ec.00285-12","type":"journal-article","created":{"date-parts":[[2013,1,12]],"date-time":"2013-01-12T05:53:41Z","timestamp":1357970021000},"page":"411-419","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":19,"title":["Bcr1 Functions Downstream of Ssd1 To Mediate Antimicrobial Peptide Resistance in Candida albicans"],"prefix":"10.1128","volume":"12","author":[{"given":"Sook-In","family":"Jung","sequence":"first","affiliation":[{"name":"Division of Infectious Diseases, Chonnom National University Medical School, Gwangju, South Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jonathan S.","family":"Finkel","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Norma V.","family":"Solis","sequence":"additional","affiliation":[{"name":"Division of Infectious Diseases, Harbor-UCLA Medical Center, Los Angeles Biomedical Research Institute at Harbor-UCLA Medical Center, Torrance, California, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Siyang","family":"Chaili","sequence":"additional","affiliation":[{"name":"Division of Infectious Diseases, Harbor-UCLA Medical Center, Los Angeles Biomedical Research Institute at Harbor-UCLA Medical Center, Torrance, California, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aaron P.","family":"Mitchell","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael R.","family":"Yeaman","sequence":"additional","affiliation":[{"name":"Division of Infectious Diseases, Harbor-UCLA Medical Center, Los Angeles Biomedical Research Institute at Harbor-UCLA Medical Center, Torrance, California, USA"},{"name":"Division of Molecular Medicine, Harbor-UCLA Medical Center, Los Angeles Biomedical Research Institute at Harbor-UCLA Medical Center, Torrance, California, USA"},{"name":"David Geffen School of Medicine at UCLA, Los Angeles, California, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Scott G.","family":"Filler","sequence":"additional","affiliation":[{"name":"Division of Infectious Diseases, Harbor-UCLA Medical Center, Los Angeles Biomedical Research Institute at Harbor-UCLA Medical Center, Torrance, California, USA"},{"name":"David Geffen School of Medicine at UCLA, Los Angeles, California, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev-pharmtox-010611-134535"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0005039"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1002501"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1128\/EC.00039-07"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.1128\/EC.00133-10"},{"key":"e_1_3_3_7_2","doi-asserted-by":"publisher","DOI":"10.1128\/EC.00402-07"},{"key":"e_1_3_3_8_2","doi-asserted-by":"publisher","DOI":"10.3109\/13693780903410386"},{"key":"e_1_3_3_9_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1462-5822.2004.00476.x"},{"key":"e_1_3_3_10_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.181.6.1868-1874.1999"},{"key":"e_1_3_3_11_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.73.2.1239-1242.2005"},{"key":"e_1_3_3_12_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1462-5822.2008.01198.x"},{"key":"e_1_3_3_13_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0401567101"},{"key":"e_1_3_3_14_2","volume-title":"Reference method for broth dilution antifungal susceptibility testing of yeasts","author":"Clinical and Laboratory Standards Institute","year":"2008","unstructured":"Clinical and Laboratory Standards Institute. 2008. 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