Τίτλος:
Characterization of a cell-wall acid phosphatase (PhoAp) in Aspergillus
fumigatus
Γλώσσες Τεκμηρίου:
Αγγλικά
Περίληψη:
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.
Συγγραφείς:
Bernard, M
Mouyna, I
Dubreucq, G
Debeaupuis, JP and
Fontaine, T
Vorgias, C
Fuglsang, C
Latge, JP
Περιοδικό:
MICROBIOLOGY-SGM
Εκδότης:
SOC GENERAL MICROBIOLOGY
Λέξεις-κλειδιά:
GPI protein; 1,3-beta-glucan
DOI:
10.1099/00221287-148-9-2819
