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Coordinate Accumulation of Antifungal Proteins and Hexoses Constitutes a Developmentally Controlled Defense Response during Fruit Ripening in Grape1

Ron A. Salzman, Irina Tikhonova, Bruce P. Bordelon, Paul M. Hasegawa, and Ray A. Bressan*

Center for Plant Environmental Stress Physiology, Purdue University, 1165 Horticulture Building, West Lafayette, Indiana 47907-1165

During ripening of grape (Vitis labruscana L. cv Concord) berries, abundance of several proteins increased, coordinately with hexoses, to the extent that these became the predominant proteins in the ovary. These proteins have been identified by N-terminal amino acid-sequence analysis and/or function to be a thaumatin-like protein (grape osmotin), a lipid-transfer protein, and a basic and an acidic chitinase. The basic chitinase and grape osmotin exhibited activities against the principal grape fungal pathogens Guignardia bidwellii and Botrytis cinerea based on in vitro growth assays. The growth-inhibiting activity of the antifungal proteins was substantial at levels comparable to those that accumulate in the ripening fruit, and these activities were enhanced by as much as 70% in the presence of 1 M glucose, a physiological hexose concentration in berries. The simultaneous accumulation of the antifungal proteins and sugars during berry ripening was correlated with the characteristic development of pathogen resistance that occurs in fruits during ripening. Taken together, accumulation of these proteins, in combination with sugars, appears to constitute a novel, developmentally regulated defense mechanism against phytopathogens in the maturing fruit.

1   This research was partially supported by a grant from the Purdue Agricultural Research Program. This is publication no. 15,479 of the Purdue University Agricultural Experiment Station.
*   Corresponding author; e-mail bressan{at}hort.purdue.edu; fax 1-765-494-0391.

Plant Physiol. (1998) 117: 465-472
Copyright Clearance Center:   0032-0889/98/117/0465/08
© 1998 American Society of Plant Physiologists




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