Physiological compensation in antisense transformants: Specific induction of an "ersatz" glucan endo-1,3-β-glucosidase in plants infected with necrotizing viruses

Abstract

Plant class I glucan endo-1,3-β-glucosidases (β-1,3-glucanase; 1,3-β-D-glucan glucanohydrolase, EC 3.2.1.39) have been implicated in development and defense against pathogen attack. Nevertheless, β-1,3-glucanase deficiencies generated by antisense transformation of Nicotiana sylvestris and tobacco have little biological effect. We report here that another β-1,3-glucanase activity is induced in these deficient mutants after infection with necrotizing viruses. Induction of class I β-1,3-glucanase was markedly inhibited in leaves of N. sylvestris and tobacco antisense transformants infected with tobacco necrosis virus and tobacco mosaic virus, respectively. A serologically distinct β-1,3-glucanase activity was present in the infected antisense transformants but was absent in both healthy and infected control plants and in antisense transformants treated with the stress hormone ethylene. Immunoblot analyses, localization studies, and measurements of antibody specificity indicate that this compensatory β-1,3-glucanase activity is an intracellular enzyme different from known tobacco β-1,3-glucanases. Therefore, plants can compensate for a deficiency in enzyme activity by producing a functionally equivalent replacement - i.e., "ersatz" - protein or proteins. The fact that compensation for β-1,3-glucanase activity occurs in response to infection argues strongly for an important role of these enzymes in pathogenesis.