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Applied and Environmental Microbiology, November 1999, p. 4760-4766, Vol. 65, No. 11
0099-2240/99/$04.00+0

Partial Purification and Characterization of Bacillus thuringiensis Cry1A Toxin Receptor A from Heliothis virescens and Cloning of the Corresponding cDNA

Daniela I. Oltean,1,2 Ashok K. Pullikuth,3,dagger Hyun-Ku Lee,3 and Sarjeet S. Gill1,2,3,*

Environmental Toxicology1 and Entomology3 Graduate Programs and Department of Neuroscience,2 University of California, Riverside, California 92521

Received 21 May 1999/Accepted 2 August 1999

Although extensively studied, the mechanism of action of insecticidal Bacillus thuringiensis Cry toxins remains elusive and requires further elucidation. Toxin receptors in the brush border membrane demand particular attention as they presumably initiate the cascade of events leading to insect mortality after toxin activation. The 170-kDa Cry1Ac toxin-binding aminopeptidase from the tobacco budworm (Heliothis virescens) was partially purified, and its corresponding cDNA was cloned. The cDNA encodes a protein with a putative glycosyl phosphatidylinositol anchor and a polythreonine stretch clustered near the C terminus with predicted O-glycosylation. Partial purification of the 170-kDa aminopeptidase also resulted in isolation of a 130-kDa protein that was immunologically identical to the 170-kDa protein, and the two proteins had identical N termini. These proteins were glycosylated, as suggested by soybean agglutinin lectin blot results. Cry1Ac toxin affinity data for the two proteins indicated that the 130-kDa protein had a higher affinity than the 170-kDa protein. The data suggest that posttranslational modifications can have a significant effect on Cry1A toxin interactions with specific insect midgut proteins.

* Corresponding author. Mailing address: Environmental Toxicology Graduate Program, 5419 Boyce Hall, University of California, Riverside, CA 92521. Phone: (909) 787-4621. Fax: (909) 787-3087. E-mail: Sarjeet.gill{at}ucr.edu.

dagger Present address: Department of Biochemistry and Molecular Biology, St. Louis University School of Medicine, St. Louis, MO 63104.

Applied and Environmental Microbiology, November 1999, p. 4760-4766, Vol. 65, No. 11
0099-2240/99/$04.00+0


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