Self versus non-self: fungal cell wall degradation in Trichoderma.

Lysis of the prey's cell wall is one of the key steps during mycoparasitism. Genome analysis of two mycoparasitic Trichoderma species, T. atroviride and T. virens, revealed an expanded arsenal of genes encoding enzymes potentially involved in cell wall hydrolysis. Glycoside hydrolase family 18, which contains all fungal chitinases, is the largest family of carbohydrate-active enzymes in mycoparasitic Trichoderma species. However, in addition to their aggressive functions during mycoparasitism, the roles of chitinases and other cell wall degrading enzymes also include remodelling and recycling of the fungus's own cell wall. In this review we discuss current knowledge about fungal cell wall degrading enzymes in Trichoderma and how the fungus distinguishes between self- and non-self fungal cell wall degradation. In the past few years, the chitinolytic enzyme machinery of Trichoderma has been used as a model system to address this question. Gene expression profiles of most investigated chitinases indicate an overlap of functions of the respective enzymes and an involvement in both self- and non-self fungal cell wall degradation. Similar sets of enzymes appear to be involved in mycoparasitism, exogenous chitin decomposition and recycling of the fungus's own cell wall. Thus, we hypothesize that the regulation of self and non-self fungal cell wall degradation is not due to a speciation of individual chitinases. Rather, we hypothesize that it is regulated by substrate accessibility due to cell wall protection in healthy hyphae vs deprotection during mycoparasitic attack, hyphal ageing and autolysis.