DIFFERENTIATION AND CELL-WALL DEGRADING ENZYMES IN THE OBLIGATELY BIOTROPHIC RUST FUNGUS UROMYCES-VICIAE-FABAE

Rust fungi differentiate a series of complex infection structures to infect their host plants. Artificial membranes providing a signal for the induction of infection structure differentiation have been used to study events taking place during early stages of host-pathogen interaction. During the prepenetration phase, serine esterases, one of which shows cutinase activity, appear to be important for adhesion of uredospores of Uromyces viciae-fabae to the plant cuticle. When the fungus grows through the stomatal opening, chitin deacetylase activity increases drastically. The role of this enzyme in masking and preventing degradation of fungal structures by plant chitinases is discussed. Different isoforms of protease, cellulase, and pectin methylesterases (PME) are formed when the fungus enters the intercellular space, and synthesis of polygalacturonate lyase (PL) coincides with formation of haustorial mother cells. Based on the physicochemical and catalytic properties of these cell wall degrading enzymes a model is presented that explains highly localized breaching of plant cell walls by obligate biotrophs. cDNAs corresponding to genes activated during late stages of infection structure differentiation of Uromyces viciae-fabae have been isolated by differential hybridization. The transcripts of the genes designated rif16 and rif21 occur when haustorial mother cells are formed, and the corresponding gene products may thus be important for successful infection.