Secretion of cryparin, a fungal hydrophobin.

Abstract:

: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.

journal_name

Appl Environ Microbiol

authors

McCabe PM,Van Alfen NK

doi

10.1128/AEM.65.12.5431-5435.1999

keywords:

subject

Has Abstract

pub_date

1999-12-01 00:00:00

pages

5431-5

issue

12

eissn

0099-2240

issn

1098-5336

journal_volume

65

pub_type

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