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Volume 271,
Number 11,
Issue of March 15, 1996 pp. 6298-6305
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
Developmental
Expression of a Tandemly Repeated, Proline- and Glutamine-rich Amino
Acid Motif on Hyphal Surfaces of Candida albicans
(Received for publication, August 25, 1995; and in revised form, January 5, 1996)
Janet F.
Staab,
Christopher
A.
Ferrer,
Paula
Sundstrom
cDNA sequences encoding a cell wall protein have been isolated
from the opportunistic pathogen, Candida albicans, an organism
that can cause serious disease in immunocompromised patients such as
those with AIDS. The cDNA encodes a peptide that is largely composed of
an acidic, repeated motif 10 amino acids in length that is rich in
proline and glutamine residues. The cDNA gene product was found to be
present on hyphal surfaces by immunofluorescence assays using
monospecific antisera raised to the recombinant protein produced in Pichia pastoris. The hyphae-specific surface location was also
seen on organisms colonizing the gastrointestinal mucosa of mice,
indicating that the antigen is produced and developmentally regulated
during growth in host tissues. The cDNA clone hybridized to an abundant
messenger RNA 2.3 kilobases in size that was present in hyphal but not
yeast forms. These studies demonstrate that the bud-hypha transition is
accompanied by the de novo synthesis of proteins that are
targeted to hyphal surfaces. The primary sequence of the unique amino
acid motif shares features with surface proteins of other lower
eukaryotic microorganisms and with host acidic salivary proline-rich
proteins.

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G. Newport and N. Agabian
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J. Biol. Chem.,
November 14, 1997;
272(46):
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[Abstract]
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Copyright © 1996 by the American Society for Biochemistry and Molecular Biology.
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