Electrical and Computer Engineering, Department of

 

Department of Electrical and Computer Engineering: Faculty Publications

Accessibility Remediation

If you are unable to use this item in its current form due to accessibility barriers, you may request remediation through our remediation request form.

Identification, cloning and expression of a Cry1Ab cadherin receptor from European corn borer, Ostrinia nubilalis (Hübner) (Lepidoptera: Crambidae)

Ronald D. Flannagan, Pioneer Hi-Bred International Inc.
Cao-Guo Yu, Pioneer Hi-Bred International Inc.
John P. Mathis, Pioneer Hi-Bred International Inc.
Terry E. Meyer, Pioneer Hi-Bred International Inc.
Xiaomei Shi, Pioneer Hi-Bred International Inc.
Herbert A. A. Siqueira, University of Nebraska - Lincoln
Blair D. Siegfried, University of Nebraska - Lincoln

Document Type Article

Published in Insect Biochemistry and Molecular Biology 35:1 (January 2005), pp. 33-40. doi:10.1016/j.ibmb.2004.10.001 http://www.sciencedirect.com/science/journal/09651748 Copyright © 2004 Elsevier Ltd. Used by permission.

Abstract

Transgenic corn expressing the Cry1Ab toxin from Bacillus thuringiensis is highly toxic to European corn borer, Ostrinia nubilalis, larvae. A putative Cry1Ab receptor (OnBt-R1) molecule was cloned and sequenced from a cDNA library prepared from midgut tissue of O. nubilalis larvae. The 5.6 Kb gene is homologous with a number of cadherin genes identified as Cry1 binding proteins in other lepidopterans. Brush border membrane vesicles were prepared using dissected midguts from late instars. A 220-kDa protein was identified as a cadherin-like molecule, which bound to Cry1Ab toxin and cross-reacted with an anti-cadherin serum developed from recombinant expression of a partial O. nubilalis cadherin peptide. Two additional proteins of smaller size cross-reacted with the anti-cadherin serum indicating that Cry1Ab binds to multiple receptors or to different forms of the same protein. Spodoptera frugiperda (SF9) cells transfected with the OnBt- R1 gene were shown to express the receptor molecule which caused functional susceptibility to Cry1Ab at concentrations as low as 0.1 μg/ml. These results in combination suggest strongly that a cadherin-like protein acts as receptor and is involved with Cry1Ab toxicity in O. nubilalis.