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

Unité des Aspergillus, Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris Cedex 15, France¹
National and Kapodistrian University of Athens, 15784 Athens, Greece²
Novozymes A/S, Krogshoejvej 36, 2880 Bagsvaerd, Denmark³

Author for correspondence: Muriel Bernard. Tel: +33 1 45 68 82 25. Fax: +33 1 40 61 34 19. e-mail: mbernard{at}pasteur.fr

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/ß-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-ß-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.

Keywords: GPI protein, 1,3-ß-glucan

Abbreviations: AfPhoAp, acid phosphatase of A. fumigatus; GPI, glycosylphosphatidylinositol; P_i, inorganic phosphate; PNGase, peptide-N-glycosidase

The GenBank accession number for the A. fumigatus PHOA sequence reported in this paper is AF462065.

^a Present address: Biodex, Saint Amand les Eaux, France.

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