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Infection and Immunity, October 1999, p. 5200-5205, Vol. 67, No. 10
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Recognition of Fibronectin by Penicillium marneffei Conidia via a Sialic Acid-Dependent Process and Its Relationship to the Interaction Between Conidia and Laminin

A. J. Hamilton,1,2,* L. Jeavons,1,2 S. Youngchim,2 and N. Vanittanakom2

Dunhill Dermatology Laboratory, St. John's Institute of Dermatology, Guys, Kings' and St. Thomas' Medical Schools, London, United Kingdom,1 and Microbiology Department, Faculty of Medicine, Chiang Mai University, Chiang Mai, Thailand2

Received 22 April 1999/Returned for modification 10 June 1999/Accepted 6 July 1999

Adhesion of Penicillium marneffei conidia to the extracellular matrix protein laminin via a sialic acid-dependent process has previously been demonstrated. This study describes the interaction of P. marneffei conidia with fibronectin and examines the relationship of this process to the recognition of laminin via conidia. Immunofluorescence microscopy demonstrated that fibronectin bound to the surface of conidia and to phialides, but not to hyphae, in a pattern similar to that reported for laminin. Conidia were able to bind to fibronectin immobilized on microtiter plates in a concentration-dependent manner. However, binding to fibronectin (at any given concentration of protein and conidia) was less than that to laminin under equivalent conditions. Soluble fibronectin and antifibronectin antibody inhibited adherence of conidia to fibronectin in the plate adherence assay; soluble laminin also caused pronounced inhibition. Various monosaccharides and several peptides had no effect on adherence to fibronectin. However, N-acetylneuraminic acid abolished adherence to fibronectin, indicating that the interaction was mediated through a sialic acid-dependent process; the latter parallels observations of laminin binding by conidia. Fibronectin binding (and binding of laminin) was considerably reduced by prolonged preincubation of conidia with chymotrypsin, suggesting the protein nature of the binding site. Conidia from older cultures were more adherent to both immobilized fibronectin and laminin than conidia from younger cultures. Ligand affinity binding demonstrated the presence of a 20-kDa protein with the ability to bind both fibronectin and laminin. There would therefore appear to be a common receptor for the binding of fibronectin and laminin on the surface of P. marneffei, and the interaction described here maybe important in mediating attachment of the fungus to host tissue.

* Corresponding author. Mailing address: Dunhill Dermatology Laboratory, 5th Floor, Thomas Guy House, Guys Hospital, London SE1 9RT, United Kingdom. Phone: 0171 955 4663. Fax: 0171 407 6689. E-mail: a.hamilton{at}umds.ac.uk.

Infection and Immunity, October 1999, p. 5200-5205, Vol. 67, No. 10
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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