Evidence for αvβ3 and αvβ5 Integrin‐like Vitronectin (VN) Receptors inCandida albicansand Their Involvement in Yeast Cell Adhesion to VN | Zendy

Elisabetta Spreghini | Zendy; Angela Gismondi | Zendy; Mario Piccoli | Zendy; Giorgio Santoni | Zendy

Open Access

Evidence for αvβ3 and αvβ5 Integrin‐like Vitronectin (VN) Receptors inCandida albicansand Their Involvement in Yeast Cell Adhesion to VN

Author(s) -

Elisabetta Spreghini,

Angela Gismondi,

Mario Piccoli,

Giorgio Santoni

Publication year - 1999

Publication title -

the journal of infectious diseases

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.69

H-Index - 252

eISSN - 1537-6613

pISSN - 0022-1899

DOI - 10.1086/314822

Subject(s) - vitronectin , candida albicans , integrin , receptor , biology , corpus albicans , antibody , yeast , microbiology and biotechnology , immunofluorescence , cell adhesion , adhesion , candida glabrata , cell , chemistry , biochemistry , immunology , organic chemistry

The expression of integrin vitronectin (VN) receptors on Candida albicans yeasts and their involvement in the adhesion to VN were investigated. By immunofluorescence and cytofluorimetric analysis, several antibodies directed against human alphav, beta3, beta5, alphavbeta3, or alphavbeta5 integrin positively stained C. albicans yeasts. Biochemical analysis on yeast lysates with anti-human alphav, beta3, or beta5 antibody revealed molecular species of 130, 110, 100, and 84 kDa. The 130-kDa band was identified as alphav, whereas the doublet of 110/100 kDa and the 84-kDa band likely correspond to the beta3 and beta5 subunits, respectively. Some 48%-54% of Candida yeasts specifically adhered to VN, and this binding was strongly inhibited by anti-human alphav, beta3, alphavbeta3, and alphavbeta5 antibodies and by RGD- but not RGE-containing peptides. In addition, VN inhibited C. albicans adherence to a human endothelial cell line. Thus, C. albicans in the yeast phase expresses VN receptors antigenically related to the vertebrate alphavbeta3 and alphavbeta5 integrins, which mediate its adhesion to VN.

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