Glycosylphosphatidylinositol-anchored Ecm33p influences conidial cell wall biosynthesis in Aspergillus fumigatus

Appl Environ Microbiol. 2006 May;72(5):3259-67. doi: 10.1128/AEM.72.5.3259-3267.2006.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aspergillus fumigatus / genetics
  • Aspergillus fumigatus / metabolism
  • Aspergillus fumigatus / physiology*
  • Cell Wall / metabolism*
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism*
  • Gene Expression Regulation, Fungal
  • Glycosylphosphatidylinositols / metabolism*
  • Humans
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Mutation
  • Neutrophils / immunology
  • Spores, Fungal / metabolism*

Substances

  • Fungal Proteins
  • Glycosylphosphatidylinositols
  • Membrane Proteins