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Infection and Immunity, June 2000, p. 3172-3179, Vol. 68, No. 6
Department of Microbiology and Immunology,
Faculty of Medicine, University of Montreal and Sainte-Justine
Hospital, Montreal, Quebec H3T 1C5, Canada
Received 30 November 1999/Returned for modification 5 January
2000/Accepted 9 March 2000
In order to approximate and adhere to mucosal epithelial cells,
Candida must traverse the overlying mucus layer.
Interactions of Candida species with mucin and human buccal
epithelial cells (BECs) were thus investigated in vitro. Binding
of the Candida species to purified small intestinal mucin
showed a close correlation with their hierarchy of virulence.
Significant differences (P < 0.05) were found among
three categories of Candida species adhering highly
(C. dubliniensis, C. tropicalis, and C. albicans), moderately (C. parapsilosis and C. lusitaniae) or weakly (C. krusei and C. glabrata) to mucin. Adherence of C. albicans to BECs
was quantitatively inhibited by graded concentrations of mucin.
However, inhibition of adherence was reversed by pretreatment of mucin
with pronase or C. albicans secretory aspartyl proteinase
Sap2p but not with sodium periodate. Saturable concentration- and
time-dependent binding of mucin to C. albicans was
abrogated by pronase or Sap2p treatment of mucin but was unaffected by
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Characterization of Binding of Candida albicans to
Small Intestinal Mucin and Its Role in Adherence to Mucosal
Epithelial Cells
-mercaptoethanol, sodium periodate, neuraminidase, lectins, or
potentially inhibitory sugars. Probing of membrane blots of the mucin
with C. albicans revealed binding of the yeast to the
66-kDa cleavage product of the 118-kDa C-terminal glycopeptide of
mucin. Although no evidence was found for the participation of C. albicans cell surface mannoproteins in specific receptor-ligand
binding to mucin, inhibition of binding by p-nitrophenol (1 mM) and tetramethylurea (0.36 M) revealed that hydrophobic interactions
are involved in adherence of C. albicans to mucin. These
results suggest that C. albicans may both
adhere to and enzymatically degrade mucins by the action of Saps, and
that both properties may act to modulate Candida populations in the oral cavity and gastrointestinal tract.
*
Corresponding author. Mailing address: Department of
Microbiology and Immunology, Sainte-Justine Hospital and University of Montreal, 3175 Chemin Côte Sainte-Catherine, Montreal, Quebec H3T
1C5, Canada. Phone: (514) 345-4643. Fax: (514) 345-4860. E-mail: louisr{at}globale.net.
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