AEM
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
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 Abdullah, M. A. F.
Right arrow Articles by Dean, D. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Abdullah, M. A. F.
Right arrow Articles by Dean, D. H.
Agricola
Right arrow Articles by Abdullah, M. A. F.
Right arrow Articles by Dean, D. H.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, September 2003, p. 5343-5353, Vol. 69, No. 9
0099-2240/03/$08.00+0     DOI: 10.1128/AEM.69.9.5343-5353.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Introduction of Culex Toxicity into Bacillus thuringiensis Cry4Ba by Protein Engineering

Mohd Amir F. Abdullah,1,2 Oscar Alzate,1,3 Marwan Mohammad,1 Rebecca J. McNall,4 Michael J. Adang,4 and Donald H. Dean1*

The Protein Research Group and Department of Biochemistry, The Ohio State University, Columbus, Ohio,1 Department of Science in Engineering, Faculty of Engineering, International Islamic University Malaysia, Jalan Gombak, 53100 Kuala Lumpur, Malaysia,2 Parque Tecnológico de Antioquia, Medellín, Colombia,3 Department of Entomology, University of Georgia, Athens, Georgia4

Received 2 April 2003/ Accepted 26 June 2003

Bacillus thuringiensis mosquitocidal toxin Cry4Ba has no significant natural activity against Culex quinquefasciatus or Culex pipiens (50% lethal concentrations [LC50], >80,000 and >20,000 ng/ml, respectively). We introduced amino acid substitutions in three putative loops of domain II of Cry4Ba. The mutant proteins were tested on four different species of mosquitoes, Aedes aegypti, Anopheles quadrimaculatus, C. quinquefasciatus, and C. pipiens. Putative loop 1 and 2 exchanges eliminated activity towards A. aegypti and A. quadrimaculatus. Mutations in a putative loop 3 resulted in a final increase in toxicity of >700-fold and >285-fold against C. quinquefasciatus (LC50 {cong} 114 ng/ml) and C. pipiens (LC50 37 ng/ml), respectively. The enhanced protein (mutein) has very little negative effect on the activity against Anopheles or Aedes. These results suggest that the introduction of short variable sequences of the loop regions from one toxin into another might provide a general rational design approach to enhancing B. thuringiensis Cry toxins.

* Corresponding author. Mailing address: Department of Biochemistry, The Ohio State University, Columbus, OH 43210-1292. Phone: (614) 292-8829. Fax: (614) 292-6773. E-mail: dean.10{at}osu.edu.

Applied and Environmental Microbiology, September 2003, p. 5343-5353, Vol. 69, No. 9
0099-2240/03/$08.00+0     DOI: 10.1128/AEM.69.9.5343-5353.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. Microbiol. Mol. Biol. Rev. Eukaryot. Cell All ASM Journals

Copyright © 2003 by the American Society for Microbiology. All rights reserved.