title: Characterization of binding of Candida albicans to small intestinal mucin and its role in adherence to mucosal epithelial cells.
abstract: 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 beta-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.
authors.affiliation: Department of Microbiology and Immunology, Faculty of Medicine, University of Montreal and Sainte-Justine Hospital, Montreal, Quebec H3T 1C5, Canada. louisr@globale.net
authors.forename: L
authors.initials: L
authors.lastname: de Repentigny
authors.forename: F
authors.initials: F
authors.lastname: Aumont
authors.forename: K
authors.initials: K
authors.lastname: Bernard
authors.forename: P
authors.initials: P
authors.lastname: Belhumeur
mesh_terms: D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000494:pharmacology; D002176:Candida albicans / Q000472:pathogenicity*; D002448:Cell Adhesion; D004847:Epithelial Cells / Q000382:microbiology*; D005656:Fungal Proteins; D007413:Intestinal Mucosa / Q000737:chemistry; D007421:Intestine, Small / Q000737:chemistry*; D008297:Male; D009061:Mouth Mucosa / Q000166:cytology / Q000382:microbiology*; D009077:Mucins / Q000187:drug effects; D011402:Pronase / Q000494:pharmacology; D011817:Rabbits
chemical_list: D005656:Fungal Proteins; D009077:Mucins; D016282:Aspartic Acid Endopeptidases; C090753:SAP2 protein, Candida; D011402:Pronase