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Aspergillus nidulans UDP-galactopyranose mutase, encoded by ugmA plays key roles in colony growth, hyphal morphogensis, and conidiation
Growing resistance to current anti-fungal drugs is spurring investigation of new targets, including those in fungal wall metabolism. Galactofuranose (Gal f) is found in the cell walls of many fungi including Aspergillus fumigatus, which is currently the most prevalent opportunistic fungal pathogen i...
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Published in: | Fungal genetics and biology 2008-12, Vol.45 (12), p.1533-1542 |
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Main Authors: | , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Growing resistance to current anti-fungal drugs is spurring investigation of new targets, including those in fungal wall metabolism. Galactofuranose (Gal
f) is found in the cell walls of many fungi including
Aspergillus fumigatus, which is currently the most prevalent opportunistic fungal pathogen in developed countries, and
A. nidulans, a closely-related, tractable model system. UDP-galactopyranose mutase (UGM) converts UDP-galactopyranose into UDP-Gal
f prior to incorporation into the fungal wall. We deleted the single-copy UGM sequence (AN3112.4, which we call
ugmA) from an
A. nidulans nkuAΔ strain, creating
ugmAΔ. Haploid
ugmAΔ strains were able to complete their asexual life cycle, showing that
ugmA is not essential. However,
ugmAΔ strains had compact colonial growth, which was associated with substantially delayed and abnormal conidiation. Compared to a wildtype morphology strain,
ugmAΔ strains had aberrant hyphal morphology, producing wide, uneven, highly-branched hyphae, with thick, relatively electron-dense walls as visualized by transmission electron microscopy. These effects were partially remediated by growth on high osmolarity medium, or on medium containing 10
μg/mL Calcofluor, consistent with Gal
f being important in cell wall structure and/or function. |
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ISSN: | 1087-1845 1096-0937 |
DOI: | 10.1016/j.fgb.2008.09.008 |