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Glycosylphosphatidylinositol-anchored ecm33p influences conidial (2005).
| Content Provider | CiteSeerX |
|---|---|
| Abstract | ECM33 encodes a glycosylphosphatidylinositol-anchored protein whose orthologs in yeast are essential for sporulation. Aspergillus fumigatus Ecm33p is unique and has an apparent mass of 55 kDa. Disruption of A. fumigatus ECM33 results in a mutant with several morphogenetic aberrations, including the following: (i) a defect in conidial separation, (ii) an increase in the diameter of the conidia of the mutant associated with an increase in the concentration of the cell wall chitin, (iii) conidia that were sensitive to the absence of aeration during long-term storage, and (iv) conidia that were more resistant to killing by phagocytes, whereas the mycelium was more easily killed by neutrophils. The fungal cell wall is composed of interlinked polysaccha-rides. Enzymes involved in the biosynthesis of linear glucan and chitin, the main cell wall polysaccharides encountered in the fungal kingdom, have been identified (5). In contrast, en-zymes responsible for providing cell wall stability through their activities in the branching and cross-linking of these linear polysaccharides in a three-dimensional rigid skeleton have not been discovered. During a search for such enzymes, the first |
| File Format | |
| Publisher Date | 2005-01-01 |
| Access Restriction | Open |
| Subject Keyword | Glycosylphosphatidylinositol-anchored Ecm33p Influence Conidial Fungal Cell Wall Three-dimensional Rigid Skeleton Main Cell Wall Polysaccharide Fumigatus Ecm33p Glycosylphosphatidylinositol-anchored Protein Apparent Mass Linear Polysaccharide Interlinked Polysaccha-rides Fungal Kingdom Cell Wall Chitin Long-term Storage Cell Wall Stability Fumigatus Ecm33 Result Conidial Separation Several Morphogenetic Aberration |
| Content Type | Text |
