AEM
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Other Versions of this Article:
AEM.01511-06v1
73/1/337    most recent
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 Google Scholar
Google Scholar
Right arrow Articles by Ruiz de Escudero, I.
Right arrow Articles by Caballero, P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ruiz de Escudero, I.
Right arrow Articles by Caballero, P.
Agricola
Right arrow Articles by Ruiz de Escudero, I.
Right arrow Articles by Caballero, P.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, January 2007, p. 337-340, Vol. 73, No. 1
0099-2240/07/$08.00+0     doi:10.1128/AEM.01511-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

SHORT REPORT

Potential of the Bacillus thuringiensis Toxin Reservoir for the Control of Lobesia botrana (Lepidoptera: Tortricidae), a Major Pest of Grape Plants{triangledown}

Iñigo Ruiz de Escudero,1 Anna Estela,2 Baltasar Escriche,2 and Primitivo Caballero1*

Departamento de Producción Agraria, Universidad Pública de Navarra, 31006 Pamplona, Spain,1 Departamento de Genética, Universitat de València, 46100 Burjassot, Spain2

Received 30 June 2006/ Accepted 25 October 2006

The potential of Bacillus thuringiensis Cry proteins to control the grape pest Lobesia botrana was explored by testing first-instar larvae with Cry proteins belonging to the Cry1, Cry2, and Cry9 groups selected for their documented activities against Lepidoptera. Cry9Ca, a toxin from B. thuringiensis, was the protein most toxic to L. botrana larvae, followed in decreasing order by Cry2Ab, Cry1Ab, Cry2Aa, and Cry1Ia7, with 50% lethal concentration values of 0.09, 0.1, 1.4, 3.2, and 8.5 µg/ml of diet, respectively. In contrast, Cry1Fa and Cry1JA were not active at the assayed concentration (100 µg/ml). In vitro binding and competition experiments showed that none of the toxins tested (Cry1Ia, Cry2Aa, Cry2Ab, and Cry9C) shared binding sites with Cry1Ab. We conclude that either Cry1Ia or Cry9C could be used in combination with Cry1Ab to control this pest, either as the active components of B. thuringiensis sprays or expressed together in transgenic plants.


* Corresponding author. Mailing address: Departamento de Producción Agraria, Universidad Pública de Navarra, 31006 Pamplona, Spain. Phone: (34) 948 16 91 29. Fax: (34) 948 16 97 32. E-mail: pcm92{at}unavarra.es.

{triangledown} Published ahead of print on 3 November 2006.


Applied and Environmental Microbiology, January 2007, p. 337-340, Vol. 73, No. 1
0099-2240/07/$08.00+0     doi:10.1128/AEM.01511-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.







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

Copyright © 2007 by the American Society for Microbiology. All rights reserved.