Characterization of a cell-wall acid phosphatase (PhoAp) in Aspergillus fumigatus - Institut Pasteur Access content directly
Journal Articles Microbiology Year : 2002

Characterization of a cell-wall acid phosphatase (PhoAp) in Aspergillus fumigatus

Muriel Bernard
  • Function : Correspondent author
  • PersonId : 1028597

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Isabelle Mouyna
Guy Dubreucq
  • Function : Author
Jean-Paul Debeaupuis
  • Function : Author
Thierry Fontaine
Claus C. Fuglsang
  • Function : Author
Jean-Paul Latgé
  • Function : Author
  • PersonId : 859664

Abstract

In the filamentous fungus Aspergillus fumigatus, the vast majority of the cell-wall-associated proteins are secreted proteins that are in transit in the cell wall. These proteins can be solubilized by detergents and reducing agents. Incubation of a SDS/beta-mercaptoethanol-treated cell-wall extract with various recombinant enzymes that hydrolyse cell-wall polysaccharides resulted in the release of a unique protein in minute amounts only after incubation of the cell wall in the presence of 1,3-beta-glucanase. Sequence analysis and biochemical studies showed that this glycoprotein, with an apparent molecular mass of 80 kDa, was an acid phosphatase (PhoAp) that was active on both phosphate monoesters and phosphate diesters. PhoAp is a glycosylphosphatidylinositol-anchored protein that was recovered in the culture filtrate and cell-wall fraction of A. fumigatus after cleavage of its anchor. It is also a phosphate-repressible acid phosphatase. The absence of PhoAp from a phosphate-rich medium was not associated with a reduction in fungal growth, indicating that this cell-wall-associated protein does not play a role in the morphogenesis of A. fumigatus.

Dates and versions

pasteur-01710765 , version 1 (16-02-2018)

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Muriel Bernard, Isabelle Mouyna, Guy Dubreucq, Jean-Paul Debeaupuis, Thierry Fontaine, et al.. Characterization of a cell-wall acid phosphatase (PhoAp) in Aspergillus fumigatus. Microbiology, 2002, 148 (9), pp.2819 - 2829. ⟨10.1099/00221287-148-9-2819⟩. ⟨pasteur-01710765⟩

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