Skip to page content
USDA Forest Service
  
Treesearch

Research & Development Treesearch

 
Treesearch Home
About Treesearch
Contact Us
Research & Development
Forest Products Lab
International Institute of Tropical Forestry
Northern
Pacific Northwest
Pacific Southwest
Rocky Mountain
Southern Research Station
Help
 

Science.gov - We Participate


USA.gov  Government Made Easy


Global Forest Information Service

US Forest Service
P.O. Box 96090
Washington, D.C.
20090-6090

(202) 205-8333

You are here: Home / Search / Publication Information
Bookmark and Share

Publication Information

View PDF (208 KB)

Title: Changes in protease activity and Cry3Aa toxin binding in the Colorado potato beetle: implications for insect resistance to Bacillus thuringiensis toxins

Author: Loseva, Olga; Ibrahim, Mohamed; Candas, Mehmet; Koller, C. Noah; Bauer, Leah S.; Bulla, Lee A. Jr.;

Date: 2002

Source: Insect Biochemistry and Molecular Biology. 32: 567?577.

Publication Series: Scientific Journal (JRNL)

Description: Widespread commercial use of Bacillus thuringiensis Cry toxins to control pest insects has increased the likelihood for development of insect resistance to this entomopathogen. In this study, we investigated protease activity profiles and toxin-binding capacities in the midgut of a strain of Colorado potato beetle (CPB) that has developed resistance to the Cry3Aa toxin of B. thuringiensis subsp. tenebrionis. Histological examination revealed that the structural integrity of the midgut tissue in the toxin-resistant (R) insect was retained whereas the same tissue was devastated by toxin action in the susceptible (S) strain. Function-based activity profiling using zymographic gels showed specific proteolytic bands present in midgut extracts and brush border membrane vesicles (BBMV) of the R strain not apparent in the S strain. Aminopeptidase activity associated with insect midgut was higher in the R strain than in the S strain. Enzymatic processing of toxin did not differ in either strain and, apparently, is not a factor in resistance. BBMV from the R strain bound ~60% less toxin than BBMV from the S strain, whereas the kinetics of toxin saturation of BBMV was 30 times less in the R strain than in the S strain. However, homologous competition inhibition binding of 125I-Cry3Aa to BBMV did not reveal any differences in binding affinity (Kd~0.1 µM) between the S and R strains. The results indicate that resistance by the CPB to the Cry3Aa toxin correlates with specific alterations in protease activity in the midgut as well as with decreased toxin binding. We believe that these features reflect adaptive responses that render the insect refractory to toxin action, making this insect an ideal model to study host innate responses and adaptive changes brought on by bacterial toxin interaction.

Keywords: Colorado potato beetle, Bacillus thuringiensis, Cry3Aa, protease, resistance

Publication Notes:

  • We recommend that you also print this page and attach it to the printout of the article, to retain the full citation information.
  • This article was written and prepared by U.S. Government employees on official time, and is therefore in the public domain.
  • This publication may be available in hard copy. Check the Northern Research Station web site to request a printed copy of this publication.
  • Our on-line publications are scanned and captured using Adobe Acrobat. During the capture process some typographical errors may occur. Please contact Sharon Hobrla, shobrla@fs.fed.us if you notice any errors which make this publication unusable.

XML: View XML

Citation:


Loseva, Olga; Ibrahim, Mohamed; Candas, Mehmet; Koller, C. Noah; Bauer, Leah S.; Bulla, Lee A. Jr. 2002. Changes in protease activity and Cry3Aa toxin binding in the Colorado potato beetle: implications for insect resistance to Bacillus thuringiensis toxins. Insect Biochemistry and Molecular Biology. 32: 567?577.

 


 [ Get Acrobat ]  Get the latest version of the Adobe Acrobat reader or Acrobat Reader for Windows with Search and Accessibility

USDA logo which links to the department's national site. Forest Service logo which links to the agency's national site.