A toxic protein, bassiacridin, was purified from a strain of the entomopathogenic fungus Beauveria bassiana isolated from a locust, using chromatographic methods. The final toxic fraction contained between 0.1 and 0.3% of the proteins of the crude extract. Bassiacridin showed no affinity for ion exchangers, was characterised as a monomer with a mol. wt of 60 kDa and an isoelectric point of 9.5, and exhibited β-glucosidase, β-galactosidase and N-acetylglucosaminidase activities. Injection of fourth instar nymphs of Locusta migratoria with the pure protein at relatively low dosage (3.3 μg toxin g body wt−1) caused a rate of mortality near to 50%. The effects of the crude and pure fractions were characterized at tissular and cellular levels. The formation of melanised spots on tracheae and air sacs and of melanised nodules in contact with the fat body was observed in injected locusts. Alterations of the fine structure of epithelial cells of tracheae, air bags, and integument were also revealed. The insecticidal protein showed a specific activity against locusts. Bassiacridin is different from the other macromolecular toxins of entomopathogenic fungi already described. Microsequencing of peptides generated by trypsic digestion of bassiacridin confirmed that it is a novel molecule and showed that it exhibits a probably limited similarity with a chitin binding protein from yeast.