Sensitivity of Neurospora crassa to a Marine-Derived Aspergillus tubingensis Anhydride Exhibiting Antifungal Activity That Is Mediated by the MAS1 Protein
The fungus Aspergillus tubingensis (strain OY907) was isolated from the Mediterranean marine sponge Ircinia variabilis. Extracellular extracts produced by this strain were found to inhibit the growth of several fungi. Among the secreted extract components, a novel anhydride metabolite, tubingenoic...
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MDPI AG
2014-09-01
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| Series: | Marine Drugs |
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| Online Access: | http://www.mdpi.com/1660-3397/12/9/4713 |
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| author | Liat Koch Anat Lodin Inbal Herold Micha Ilan Shmuel Carmeli Oded Yarden |
| author_facet | Liat Koch Anat Lodin Inbal Herold Micha Ilan Shmuel Carmeli Oded Yarden |
| author_sort | Liat Koch |
| collection | DOAJ |
| description | The fungus Aspergillus tubingensis (strain OY907) was isolated from the Mediterranean marine sponge Ircinia variabilis. Extracellular extracts produced by this strain were found to inhibit the growth of several fungi. Among the secreted extract components, a novel anhydride metabolite, tubingenoic anhydride A (1) as well as the known 2-carboxymethyl-3-hexylmaleic acid anhydride, asperic acid, and campyrone A and C were purified and their structure elucidated. Compound 1 and 2-carboxymethyl-3-hexylmaleic acid anhydride inhibited Neurospora crassa growth (MIC = 330 and 207 μM, respectively) and affected hyphal morphology. We produced a N. crassa mutant exhibiting tolerance to 1 and found that a yet-uncharacterized gene, designated mas-1, whose product is a cytosolic protein, confers sensitivity to this compound. The ∆mas-1 strain showed increased tolerance to sublethal concentrations of the chitin synthase inhibitor polyoxin D, when compared to the wild type. In addition, the expression of chitin synthase genes was highly elevated in the ∆mas-1 strain, suggesting the gene product is involved in cell wall biosynthesis and the novel anhydride interferes with its function. |
| first_indexed | 2024-12-10T07:12:15Z |
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| issn | 1660-3397 |
| language | English |
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| publishDate | 2014-09-01 |
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| series | Marine Drugs |
| spelling | doaj.art-76f5a2dde40b4ba4913f2d1a5046134d2022-12-22T01:58:02ZengMDPI AGMarine Drugs1660-33972014-09-011294713473110.3390/md12094713md12094713Sensitivity of Neurospora crassa to a Marine-Derived Aspergillus tubingensis Anhydride Exhibiting Antifungal Activity That Is Mediated by the MAS1 ProteinLiat Koch0Anat Lodin1Inbal Herold2Micha Ilan3Shmuel Carmeli4Oded Yarden5Department of Plant Pathology and Microbiology, The R.H. Smith Faculty of Agriculture, Food and Environment, The Hebrew University of Jerusalem, Rehovot 76100, IsraelSchool of Chemistry, Raymond and Beverly Sackler Faculty of Exact Sciences, Tel Aviv 69978, IsraelDepartment of Plant Pathology and Microbiology, The R.H. Smith Faculty of Agriculture, Food and Environment, The Hebrew University of Jerusalem, Rehovot 76100, IsraelDepartment of Zoology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, IsraelSchool of Chemistry, Raymond and Beverly Sackler Faculty of Exact Sciences, Tel Aviv 69978, IsraelDepartment of Plant Pathology and Microbiology, The R.H. Smith Faculty of Agriculture, Food and Environment, The Hebrew University of Jerusalem, Rehovot 76100, IsraelThe fungus Aspergillus tubingensis (strain OY907) was isolated from the Mediterranean marine sponge Ircinia variabilis. Extracellular extracts produced by this strain were found to inhibit the growth of several fungi. Among the secreted extract components, a novel anhydride metabolite, tubingenoic anhydride A (1) as well as the known 2-carboxymethyl-3-hexylmaleic acid anhydride, asperic acid, and campyrone A and C were purified and their structure elucidated. Compound 1 and 2-carboxymethyl-3-hexylmaleic acid anhydride inhibited Neurospora crassa growth (MIC = 330 and 207 μM, respectively) and affected hyphal morphology. We produced a N. crassa mutant exhibiting tolerance to 1 and found that a yet-uncharacterized gene, designated mas-1, whose product is a cytosolic protein, confers sensitivity to this compound. The ∆mas-1 strain showed increased tolerance to sublethal concentrations of the chitin synthase inhibitor polyoxin D, when compared to the wild type. In addition, the expression of chitin synthase genes was highly elevated in the ∆mas-1 strain, suggesting the gene product is involved in cell wall biosynthesis and the novel anhydride interferes with its function.http://www.mdpi.com/1660-3397/12/9/4713natural productsantifungalAspergillus tubingensisNeurospora crassacell wallchitin synthase |
| spellingShingle | Liat Koch Anat Lodin Inbal Herold Micha Ilan Shmuel Carmeli Oded Yarden Sensitivity of Neurospora crassa to a Marine-Derived Aspergillus tubingensis Anhydride Exhibiting Antifungal Activity That Is Mediated by the MAS1 Protein Marine Drugs natural products antifungal Aspergillus tubingensis Neurospora crassa cell wall chitin synthase |
| title | Sensitivity of Neurospora crassa to a Marine-Derived Aspergillus tubingensis Anhydride Exhibiting Antifungal Activity That Is Mediated by the MAS1 Protein |
| title_full | Sensitivity of Neurospora crassa to a Marine-Derived Aspergillus tubingensis Anhydride Exhibiting Antifungal Activity That Is Mediated by the MAS1 Protein |
| title_fullStr | Sensitivity of Neurospora crassa to a Marine-Derived Aspergillus tubingensis Anhydride Exhibiting Antifungal Activity That Is Mediated by the MAS1 Protein |
| title_full_unstemmed | Sensitivity of Neurospora crassa to a Marine-Derived Aspergillus tubingensis Anhydride Exhibiting Antifungal Activity That Is Mediated by the MAS1 Protein |
| title_short | Sensitivity of Neurospora crassa to a Marine-Derived Aspergillus tubingensis Anhydride Exhibiting Antifungal Activity That Is Mediated by the MAS1 Protein |
| title_sort | sensitivity of neurospora crassa to a marine derived aspergillus tubingensis anhydride exhibiting antifungal activity that is mediated by the mas1 protein |
| topic | natural products antifungal Aspergillus tubingensis Neurospora crassa cell wall chitin synthase |
| url | http://www.mdpi.com/1660-3397/12/9/4713 |
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