{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T14:20:51Z","timestamp":1790518851798,"version":"4.1.0"},"reference-count":56,"publisher":"American Society for Microbiology","issue":"12","license":[{"start":{"date-parts":[[2012,12,1]],"date-time":"2012-12-01T00:00:00Z","timestamp":1354320000000},"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":["Antimicrob Agents Chemother"],"published-print":{"date-parts":[[2012,12]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Aspergillus fumigatus<\/jats:named-content>\n            has two chitin synthases (\n            <jats:italic>CSMA<\/jats:italic>\n            and\n            <jats:italic>CSMB<\/jats:italic>\n            ) with a myosin motor-like domain (MMD) arranged in a head-to-head configuration. To understand the function of these chitin synthases, single and double\n            <jats:italic>csm<\/jats:italic>\n            mutant strains were constructed and analyzed. Although there was a slight reduction in mycelial growth of the mutants, the total chitin synthase activity and the cell wall chitin content were similar in the mycelium of all of the mutants and the parental strain. In the conidia, chitin content in the \u0394\n            <jats:italic>csmA<\/jats:italic>\n            strain cell wall was less than half the amount found in the parental strain. In contrast, the \u0394\n            <jats:italic>csmB<\/jats:italic>\n            mutant strain and, unexpectedly, the \u0394\n            <jats:italic>csmA<\/jats:italic>\n            \/\u0394\n            <jats:italic>csmB<\/jats:italic>\n            mutant strain did not show any modification of chitin content in their conidial cell walls. In contrast to the hydrophobic conidia of the parental strain, conidia of all of the\n            <jats:italic>csm<\/jats:italic>\n            mutants were hydrophilic due to the presence of an amorphous material covering the hydrophobic surface-rodlet layer. The deletion of\n            <jats:italic>CSM<\/jats:italic>\n            genes also resulted in an increased susceptibility of resting and germinating conidia to echinocandins. These results show that the deletion of the\n            <jats:italic>CSMA<\/jats:italic>\n            and\n            <jats:italic>CSMB<\/jats:italic>\n            genes induced a significant disorganization of the cell wall structure, even though they contribute only weakly to the overall cell wall chitin synthesis.\n          <\/jats:p>","DOI":"10.1128\/aac.00752-12","type":"journal-article","created":{"date-parts":[[2012,9,11]],"date-time":"2012-09-11T06:10:15Z","timestamp":1347343815000},"page":"6121-6131","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":61,"title":["Chitin Synthases with a Myosin Motor-Like Domain Control the Resistance of Aspergillus fumigatus to Echinocandins"],"prefix":"10.1128","volume":"56","author":[{"given":"Cristina","family":"Jim\u00e9nez-Ortigosa","sequence":"first","affiliation":[{"name":"Departamento de Microbiolog\u00eda y Gen\u00e9tica, Universidad de Salamanca, Salamanca, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vishukumar","family":"Aimanianda","sequence":"additional","affiliation":[{"name":"Unit\u00e9 des Aspergillus, Institut Pasteur, Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laetitia","family":"Muszkieta","sequence":"additional","affiliation":[{"name":"Unit\u00e9 des Aspergillus, Institut Pasteur, Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Isabelle","family":"Mouyna","sequence":"additional","affiliation":[{"name":"Unit\u00e9 des Aspergillus, Institut Pasteur, Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David","family":"Alsteens","sequence":"additional","affiliation":[{"name":"Institute of Condensed Matter and Nanosciences, Universit\u00e9 Catholique de Louvain, Louvain-la-Neuve, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"St\u00e9phane","family":"Pire","sequence":"additional","affiliation":[{"name":"Institute of Condensed Matter and Nanosciences, Universit\u00e9 Catholique de Louvain, Louvain-la-Neuve, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Remi","family":"Beau","sequence":"additional","affiliation":[{"name":"Unit\u00e9 des Aspergillus, Institut Pasteur, Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sven","family":"Krappmann","sequence":"additional","affiliation":[{"name":"Microbiology Institute\u2013Clinical Microbiology, Immunology and Hygiene, University Hospital of Erlangen and Friedrich-Alexander-University, Erlangen-N\u00fcrnberg, Erlangen, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anne","family":"Beauvais","sequence":"additional","affiliation":[{"name":"Unit\u00e9 des Aspergillus, Institut Pasteur, Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yves F.","family":"Dufr\u00eane","sequence":"additional","affiliation":[{"name":"Institute of Condensed Matter and Nanosciences, Universit\u00e9 Catholique de Louvain, Louvain-la-Neuve, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"C\u00e9sar","family":"Roncero","sequence":"additional","affiliation":[{"name":"Departamento de Microbiolog\u00eda y Gen\u00e9tica, Universidad de Salamanca, Salamanca, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jean-Paul","family":"Latg\u00e9","sequence":"additional","affiliation":[{"name":"Unit\u00e9 des Aspergillus, Institut Pasteur, Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1038\/nature08264"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1006\/fgbi.1997.0959"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1128\/EC.4.11.1902-1912.2005"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1099\/00221287-139-12-3071"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.00485-06"},{"key":"e_1_3_3_7_2","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1099\/00221287-138-1-97","article-title":"Chitinase and chitin synthase 1: counterbalancing activities in cell separation of Saccharomyces cerevisiae","volume":"138","author":"Cabib E","year":"1992","unstructured":"CabibE SilvermanSJ ShawJA. 1992. 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