摘要

alpha-Glucan affects fungal cell-cell interactions and is important for the virulence of pathogenic fungi. Interfering with production of alpha-glucan could help to prevent fungal infection. In our previous study, we reported that an amylase-like protein, AmyD, could repress alpha-glucan accumulation in Aspergillus nidulans. However, the underlying molecular mechanism was not clear. Here, we examined the localization of AmyD and found it was a membrane-associated protein. We studied AmyD function in alpha-glucan degradation, as well as with other predicted amylase-like proteins and three annotated alpha-glucanases. AmyC and AmyE share a substantial sequence identity with AmyD, however, neither affects alpha-glucan synthesis. In contrast, AgnB and MutA (but not AgnE) are functional alpha-glucanases that also repress alpha-glucan accumulation. Nevertheless, the functions of AmyD and these glucanases were independent from each other. The dynamics of alpha-glucan accumulation showed different patterns between the AmyD overexpression strain and the alpha-glucanase overexpression strains, suggesting AmyD may not be involved in the alpha-glucan degradation process. These results suggest the function of AmyD is to directly suppress alpha-glucan synthesis, but not to facilitate its degradation.