This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Lee, M. K.
Right arrow Articles by Dean, D. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lee, M. K.
Right arrow Articles by Dean, D. H.
Agricola
Right arrow Articles by Lee, M. K.
Right arrow Articles by Dean, D. H.

 Previous Article  |  Next Article 

Appl. Environ. Microbiol., Aug 1996, 2845-2849, Vol 62, No. 8
Copyright © 1996, American Society for Microbiology

Aminopeptidase N purified from gypsy moth brush border membrane vesicles is a specific receptor for Bacillus thuringiensis CryIAc toxin

MK Lee, TH You, BA Young, JA Cotrill, AP Valaitis and DH Dean
Department of Biochemistry, Ohio State University, Columbus 43210, USA.

We have evaluated the binding of Bacillus thuringiensis Cry toxins to aminopeptidase N (APN) purified from Lymantria dispar (gypsy moth) brush border membrane vesicle (BBMV). CryIAc toxin bound strongly to APN, while either the structurally related CryIAa and CryIAb toxins or CryIC, CryIIA, and CryIIIA toxins showed weak binding to APN. An in vitro competition binding study demonstrated that the binding of CryIAc to L. dispar BBMV was inhibited by APN. Inhibition of short circuit current for CryIAc, measured by voltage clamping of whole L. dispar midgut, was substantially reduced by addition of phosphatidylinositol- specific phospholipase C, which is known to release APN from the midgut membrane. In contrast, addition of phosphatidylinositol-specific phospholipase C had only a marginal effect on the inhibition of short circuit current for CryIAa. These data suggest that APN is the major functional receptor for CryIAc in L. dispar BBMV. A ligand blotting experiment demonstrated that CryIAc recognized a 120-kDa peptide (APN), while CryIAa and CryIAb recognized a 210-kDa molecule in L. dispar BBMV. In contrast, CryIAa and CryIAb bound to both the 120- and 210-kDa molecules in Manduca sexta BBMV, while CryIAc recognized only the 120- kDa peptide. The 120-kDa peptide (APN) in L. dispar BBMV reacted with soybean agglutinin, indicating that N-acetylgalactosamine is a component of this glycoprotein.


This article has been cited by other articles:

  • Atsumi, S., Mizuno, E., Hara, H., Nakanishi, K., Kitami, M., Miura, N., Tabunoki, H., Watanabe, A., Sato, R. (2005). Location of the Bombyx mori Aminopeptidase N Type 1 Binding Site on Bacillus thuringiensis Cry1Aa Toxin. Appl. Environ. Microbiol. 71: 3966-3977 [Abstract] [Full Text]  
  • Mehlo, L., Gahakwa, D., Nghia, P. T., Loc, N. T., Capell, T., Gatehouse, J. A., Gatehouse, A. M. R., Christou, P. (2005). An alternative strategy for sustainable pest resistance in genetically enhanced crops. Proc. Natl. Acad. Sci. USA 102: 7812-7816 [Abstract] [Full Text]  
  • Xie, R., Zhuang, M., Ross, L. S., Gomez, I., Oltean, D. I., Bravo, A., Soberon, M., Gill, S. S. (2005). Single Amino Acid Mutations in the Cadherin Receptor from Heliothis virescens Affect Its Toxin Binding Ability to Cry1A Toxins. J. Biol. Chem. 280: 8416-8425 [Abstract] [Full Text]  
  • Rajagopal, R., Sivakumar, S., Agrawal, N., Malhotra, P., Bhatnagar, R. K. (2002). Silencing of Midgut Aminopeptidase N of Spodoptera litura by Double-stranded RNA Establishes Its Role as Bacillus thuringiensis Toxin Receptor. J. Biol. Chem. 277: 46849-46851 [Abstract] [Full Text]  
  • Jurat-Fuentes, J. L., Gould, F. L., Adang, M. J. (2002). Altered Glycosylation of 63- and 68-Kilodalton Microvillar Proteins in Heliothis virescens Correlates with Reduced Cry1 Toxin Binding, Decreased Pore Formation, and Increased Resistance to Bacillus thuringiensis Cry1 Toxins. Appl. Environ. Microbiol. 68: 5711-5717 [Abstract] [Full Text]  
  • Agrawal, N., Malhotra, P., Bhatnagar, R. K. (2002). Interaction of Gene-Cloned and Insect Cell-Expressed Aminopeptidase N of Spodoptera litura with Insecticidal Crystal Protein Cry1C. Appl. Environ. Microbiol. 68: 4583-4592 [Abstract] [Full Text]  
  • Jenkins, J. L., Lee, M. K., Valaitis, A. P., Curtiss, A., Dean, D. H. (2000). Bivalent Sequential Binding Model of a Bacillus thuringiensis Toxin to Gypsy Moth Aminopeptidase N Receptor. J. Biol. Chem. 275: 14423-14431 [Abstract] [Full Text]  
  • Rausell, C., Martínez-Ramírez, A. C., García-Robles, I., Real, M. D. (2000). A Binding Site for Bacillus thuringiensis Cry1Ab Toxin Is Lost during Larval Development in Two Forest Pests. Appl. Environ. Microbiol. 66: 1553-1558 [Abstract] [Full Text]  
  • Lee, M. K., You, T. H., Gould, F. L., Dean, D. H. (1999). Identification of Residues in Domain III of Bacillus thuringiensis Cry1Ac Toxin That Affect Binding and Toxicity. Appl. Environ. Microbiol. 65: 4513-4520 [Abstract] [Full Text]  
  • Keeton, T. P., Francis, B. R., Maaty, W. S. A., Bulla, L. A. Jr. (1998). Effects of Midgut-Protein-Preparative and Ligand Binding Procedures on the Toxin Binding Characteristics of BT-R1, a Common High-Affinity Receptor in Manduca sexta for Cry1A Bacillus thuringiensis Toxins. Appl. Environ. Microbiol. 64: 2158-2165 [Abstract] [Full Text]  
  • Gomez, I., Oltean, D. I., Gill, S. S., Bravo, A., Soberon, M. (2001). Mapping the Epitope in Cadherin-like Receptors Involved in Bacillus thuringiensis Cry1A Toxin Interaction Using Phage Display. J. Biol. Chem. 276: 28906-28912 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»