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Applied and Environmental Microbiology, December 1999, p. 5431-5435, Vol. 65, No. 12
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Secretion of Cryparin, a Fungal Hydrophobin

Patricia M. McCabedagger and Neal K. Van Alfen*

Department of Plant Pathology and Microbiology, Texas A&M University, College Station, Texas 77843

Received 26 July 1999/Accepted 23 September 1999

Cryparin is a cell-surface-associated hydrophobin of the filamentous ascomycete Cryphonectria parasitica. This protein contains a signal peptide that directs it to the vesicle-mediated secretory pathway. We detected a glycosylated form of cryparin in a secretory vesicle fraction, but secreted forms of this protein are not glycosylated. This glycosylation occurred in the proprotein region, which is cleaved during maturation by a Kex2-like serine protease, leaving a mature form of cryparin that could be isolated from both the cell wall and culture medium. Pulse-chase labeling experiments showed that cryparin was secreted through the cell wall, without being bound, into the culture medium. The secreted protein then binds to the cell walls of C. parasitica, where it remains. Binding of cryparin to the cell wall occurred in submerged culture, presumably because of the lectin-like properties unique to this hydrophobin. Thus, the binding of this hydrophobin to the cell wall is different from that of other hydrophobins which are reported to require a hydrophobic-hydrophilic interface for assembly.

* Corresponding author. Mailing address: Department of Plant Pathology, University of California, Davis, CA 95616. Phone: (530) 754-5500. Fax: (530) 752-5674. E-mail: nkvanalfen{at}ucdavis.edu.

dagger Present address: Department of Plant Pathology, University of California, Davis, CA 95616.

Applied and Environmental Microbiology, December 1999, p. 5431-5435, Vol. 65, No. 12
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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