Characterization of the endothiapepsin-like protein in the entomopathogenic fungus Beauveria bassiana and its virulence effect on the silkworm, Bombyx mori.

•An endothiapepsin-like protein in Beauveria bassiana was characterized.•The predicted structure shows that the protein belongs to aspartic proteinase family.•This secreted proteinase has an N-glycosylation site and a mutant amino acid.•Recombinant endothiapepsin-like protein could degrade cuticle of the silkworm.•Deleting this protein gene would reduce virulence for the insect silkworm.