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5β1 integrin
1Chair of General Pathology, University of Camerino, Camerino, Italy
2Department of Experimental Medicine, University of Rome La Sapienza, Rome, Italy
3Moffitt Cancer Center, University of South Florida, Tampa, FL, USA
Author for correspondence: Giorgio Santoni. Tel: + 39 737 2538. Fax: +39 737 2538.
ABSTRACT
Cell adhesion molecules, by regulating host-micro-organism interaction, play major role in the pathogenesis of infectious diseases. The present study was undertaken to investigate the expression of the fibronectin (FN) receptor prototype,
5β1 integrin, on Candida albicans and its involvement in the adhesion to FN. By immunofluorescence and fluorescence activated cell sorter (FACS) analysis, several monoclonal antibodies (mAbs) directed against human
5 or β1 integrin subunits, or two different antisera to FN receptor positively stained C. albicans yeast and germ tube phases, this immunoreactivity increasing upon germ tube transition. Twenty-five to thirty per cent of [3H]glucose-labelled Candida yeasts specifically adhered to FN and this adhesion was increased upon germ tube transition. C. albicans yeast and gerr tube forms bound to an RGD-containing 120 kDa tryptic fragment of FN and adhesion to FN was markedly inhibited by GRGDSP, but not GRGESP peptides. Moreover, binding of both C. albicans phases to FN was strongly inhibited by anti-
5 SAM-1 mAb, or both anti-fibronectin receptor (FNr) antisera. Overall these results indicate that C. albicans yeast and germ tube phases express a receptor antigenically related to
5β1 integrin which mediates their adhesion to FN. The
5β1 integrin-like receptor expression on C. albicans could be relevant for fungus-host interaction and in the dissemination process of Candida infection.
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