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Pathogenicity and Medical Microbiology |
Secció Departamental de Bioquímica i Biologia Molecular, Facultat de Farmacia, Universitat de Valencia, Avda Vicent A. Estellés, s/n, 46100-Burjassot (València), Spain1
Departamento de Bioquímica, Facultad de Estomatología, Benemérita Universidad autónoma de Puebla, Mexico2
Author for correspondence: Joaquín Timoneda. Tel: +34 6 3983189. Fax: +34 6 3864917. e-mail: Joaquin.Timoneda{at}uv.es
Adherence of the opportunistic pathogen Candida albicans to basement membrane (BM) proteins is considered a crucial step in the development of candidiasis. In this study the interactions of C. albicans yeast cells with the three main domains of type IV collagen, a major BM glycoprotein, were analysed. C. albicans adhered to the three immobilized domains by different mechanisms. Adhesion to the N-terminal cross-linking domain (7S) required the presence of divalent cations, whereas interaction with the central collagenous domain (CC) was cation-independent. Recognition of the C-terminal non-collagenous domain (NC1) was partially cation-dependent. Binding inhibition assays with the corresponding domains in soluble form showed that these interactions were specific. Both Ca2+ and Mg2+ promoted adhesion to the 7S domain and the interaction was completely abolished by EDTA. Treatment of the 7S domain, or its subunits, with N-glycosidase F reduced yeast binding by approximately 70%. Moreover, several sugars known to be part of the N-linked oligosaccharide chains of collagen IV inhibited adhesion to immobilized 7S; N-acetylglucosamine, L-fucose and methylmannoside caused a similar inhibition whereas N-acetyllactosamine was a more effective inhibitor. In contrast, glucose, galactose, lactose or heparan sulfate did not affect yeast binding. Combinations of the inhibitory sugars at suboptimal inhibition concentrations did not reduce C. albicans adhesion more than the individual sugars, pointing to a single lectin as responsible for the interaction. These results taken together show that C. albicans utilizes several adhesins for interacting with type IV collagen, and that at least one of them is a lectin which recognizes the 7S(IV) oligosaccharide residues as its receptor.
Keywords: yeast, basement membrane, adhesion, oligosaccharide binding
Abbreviations: BM, basement membrane; CC, central collagenous domain of type IV collagen; ConA, concanavalin A; ECM, extracellular matrix; LBM, anterior lens capsule basement membrane; NC1, C-terminal non-collagenous domain of type IV collagen; 7S, N-terminal 7S domain of type IV collagen
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