{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T13:44:45Z","timestamp":1790257485595,"version":"4.1.0"},"reference-count":44,"publisher":"American Society for Microbiology","issue":"1","license":[{"start":{"date-parts":[[2011,1,1]],"date-time":"2011-01-01T00:00:00Z","timestamp":1293840000000},"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":[[2011,1]]},"abstract":"<jats:title>ABSTRACT<\/jats:title><jats:p><jats:named-content content-type=\"genus-species\">Histoplasma capsulatum<\/jats:named-content>strains can be classified into two chemotypes based on cell wall composition. The cell wall of chemotype II yeast contains a layer of \u03b1-(1,3)-glucan that masks immunostimulatory \u03b2-(1,3)-glucans from detection by the Dectin-1 receptor on host phagocytes. This \u03b1-(1,3)-glucan cell wall component is essential for chemotype II<jats:named-content content-type=\"genus-species\">Histoplasma<\/jats:named-content>virulence. In contrast, chemotype I yeast cells lack \u03b1-(1,3)-glucan<jats:italic>in vitro<\/jats:italic>, yet they remain fully virulent<jats:italic>in vivo<\/jats:italic>. Analysis of the chemotype I \u03b1-glucan synthase (<jats:italic>AGS1<\/jats:italic>) locus revealed a 2.7-kb insertion in the promoter region that diminishes<jats:italic>AGS1<\/jats:italic>expression. Nonetheless,<jats:italic>AGS1<\/jats:italic>mRNA can be detected during respiratory infection with chemotype I yeast, suggesting that \u03b1-(1,3)-glucan could be produced during<jats:italic>in vivo<\/jats:italic>growth despite its absence<jats:italic>in vitro<\/jats:italic>. To directly test whether<jats:italic>AGS1<\/jats:italic>contributes to chemotype I strain virulence, we prevented<jats:italic>AGS1<\/jats:italic>function by RNA interference and by insertional mutation. Loss of<jats:italic>AGS1<\/jats:italic>function in chemotype I does not impair the cytotoxicity of<jats:italic>ags1<\/jats:italic>(\u2212) mutant yeast to cultured macrophages, nor does it affect the intracellular growth of yeast. In a murine model of histoplasmosis, the<jats:italic>ags1<\/jats:italic>(\u2212) chemotype I mutant strains show no defect in lung infection or in extrapulmonary dissemination. Together, these studies demonstrate that<jats:italic>AGS1<\/jats:italic>expression is dispensable for chemotype I yeast virulence, in contrast to the case for chemotype II yeast. Despite the absence of cell wall \u03b1-(1,3)-glucan, chemotype I yeast can avoid detection by Dectin-1 in a growth stage-dependent manner. This suggests the production of a unique<jats:named-content content-type=\"genus-species\">Histoplasma<\/jats:named-content>chemotype I factor that, at least partially, circumvents the \u03b1-(1,3)-glucan requirement for yeast virulence.<\/jats:p>","DOI":"10.1128\/ec.00214-10","type":"journal-article","created":{"date-parts":[[2010,10,30]],"date-time":"2010-10-30T03:07:54Z","timestamp":1288408074000},"page":"87-97","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":71,"title":["The Yeast-Phase Virulence Requirement for \u03b1-Glucan Synthase Differs among Histoplasma capsulatum Chemotypes"],"prefix":"10.1128","volume":"10","author":[{"given":"Jessica A.","family":"Edwards","sequence":"first","affiliation":[{"name":"Departments of Microbiology and Internal Medicine, The Center for Microbial Interface Biology, Ohio State University, 484 W. 12th Avenue, Columbus, Ohio 43210"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elizabeth A.","family":"Alore","sequence":"additional","affiliation":[{"name":"Departments of Microbiology and Internal Medicine, The Center for Microbial Interface Biology, Ohio State University, 484 W. 12th Avenue, Columbus, Ohio 43210"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chad A.","family":"Rappleye","sequence":"additional","affiliation":[{"name":"Departments of Microbiology and Internal Medicine, The Center for Microbial Interface Biology, Ohio State University, 484 W. 12th Avenue, Columbus, Ohio 43210"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1621\/nrs.01012"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/S1130-1406(08)70019-6"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1038\/35092620"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1462-5822.2005.00505.x"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1462-5822.2004.00454.x"},{"key":"e_1_3_3_7_2","doi-asserted-by":"crossref","first-page":"2588","DOI":"10.4049\/jimmunol.134.4.2588","article-title":"A beta-glucan inhibitable receptor on human monocytes: its identity with the phagocytic receptor for particulate activators of the alternative complement pathway","volume":"134","author":"Czop J. 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