Fimbria-mediated adherence of Candida albicans to glycosphingolipid receptors on human buccal epithelial cells

Abstract

Candida albicans is an opportunist fungal pathogen that has the ability to adhere to host cell surface receptors via a number of adhesins. Yu et al.

Adherence ability of Candida africana: a comparative study with Candida albicans and Candida dubliniensis

“…Unattached cells were removed from the strips by washing with 5 ml phosphate-buffered saline (PBS) solution. Subsequently, the strips were submerged in 4 ml of yeast nitrogen base (YNB) containing 50 mmol l )1 glucose and incubated over a series of time intervals (2,4,6,8,24 and 48 h) at 37°C. As negative controls, six strips were handled in an identical fashion, except that no Candida suspensions were added.…”

“…5 In fact, C. albicans has been demonstrated to bind to several cell types such as buccal epithelial cells, vascular endothelial cells, human corneocytes and vaginal epithelial cells. 6 Biofilms represent the most prevalent type of microbial growth in nature with significant implications in pathogenicity.…”

Blood Groups in Infection and Host Susceptibility

“…Candida can recognize stratherin, hydroxyapatite, and RGDcontaining proteins such as fibronectin and fibrinogen (213). Candida species also possess lectin-like adhesins, with binding to LacCer, asialo-GM1, Le a , and H-active glycans (213)(214)(215)(216)(217)(218)(219). The type of adhesin expressed varies by strain and is influenced by growth conditions (218)(219)(220).…”

Use of synthetic peptides to confirm that the Pseudomonas aeruginosa PAK pilus adhesin and the Candida albicans fimbrial adhesin possess a homologous receptor‐binding domain

“…The receptor-binding domain (termed 'adhesintope') of the P. aeruginosa PAK pilin adhesin has been shown to reside in the carboxyterminal disulphide-looped region (PAK128-144) of the PAK pilin (Irvin et al, 1989;Lee et al, 1994;. C. albicans and other fungi have also been previously shown to bind to glycosphingolipids in vitro (Jimenez-Lucho et al, 1990) and we have established that C. albicans utilizes fimbriae to bind to asialo-GM 1 -like receptors on the surface of humans BECs (Yu et al, 1994b). We have also demonstrated that P. aeruginosa pili and synthetic C-terminal pilin peptides containing the pilus adhesin bind to asialo-GM 1 Sheth et al, 1994).…”

“…It has been demonstrated that one of the mechanisms by which C. albicans adheres to hBECs is mediated by the interaction of C. albicans fimbrial adhesins and glycosphingolipid (asialo-GM 1 ) on the surface of hBECs in vitro and that the ligand-binding domain on the asialo-GM 1 -like receptors is presumably located in a disaccharide (bGalNAc(1-4)bGal), i.e. the carbohydrate portion of asialo-GM 1 , since both asialo-GM 1 and synthetic b GalNAc(1-4)bGal can inhibit the binding of C. albicans fimbrial binding to asialo-GM 1 and hBECs (Yu et al, 1994b). As a putative receptor, asialo-GM 1 and its minimal disaccharide sequence (bGalNAc(1-4)bGal) can also significantly block C. albicans whole-cells binding to hBECs (Fig.…”