Blocking binding of Bacillus thuringiensis Cry1Aa to Bombyx mori cadherin receptor results in only a minor reduction of toxicity

BACKGROUND: Bacillus thuringiensis Cry1Aa insecticidal protein is the most active known B. thuringiensis toxin against the forest insect pest Lymantria dispar (gypsy moth), unfortunately it is also highly toxic against the non-target insect Bombyx mori (silk worm). RESULTS: Surface exposed hydrophob...

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Autores principales: You, Taek H, Lee, Mi K, Jenkins, Jeremy L, Alzate, Oscar, Dean, Donald H
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2008
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2245940/
https://www.ncbi.nlm.nih.gov/pubmed/18218126
http://dx.doi.org/10.1186/1471-2091-9-3
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author You, Taek H
Lee, Mi K
Jenkins, Jeremy L
Alzate, Oscar
Dean, Donald H
author_facet You, Taek H
Lee, Mi K
Jenkins, Jeremy L
Alzate, Oscar
Dean, Donald H
author_sort You, Taek H
collection PubMed
description BACKGROUND: Bacillus thuringiensis Cry1Aa insecticidal protein is the most active known B. thuringiensis toxin against the forest insect pest Lymantria dispar (gypsy moth), unfortunately it is also highly toxic against the non-target insect Bombyx mori (silk worm). RESULTS: Surface exposed hydrophobic residues over domains II and III were targeted for site-directed mutagenesis. Substitution of a phenylalanine residue (F328) by alanine reduced binding to the Bombyx mori cadherin by 23-fold, reduced biological activity against B. mori by 4-fold, while retaining activity against Lymantria dispar. CONCLUSION: The results identify a novel receptor-binding epitope and demonstrate that virtual elimination of binding to cadherin BR-175 does not completely remove toxicity in the case of B. mori.
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spelling pubmed-22459402008-02-16 Blocking binding of Bacillus thuringiensis Cry1Aa to Bombyx mori cadherin receptor results in only a minor reduction of toxicity You, Taek H Lee, Mi K Jenkins, Jeremy L Alzate, Oscar Dean, Donald H BMC Biochem Research Article BACKGROUND: Bacillus thuringiensis Cry1Aa insecticidal protein is the most active known B. thuringiensis toxin against the forest insect pest Lymantria dispar (gypsy moth), unfortunately it is also highly toxic against the non-target insect Bombyx mori (silk worm). RESULTS: Surface exposed hydrophobic residues over domains II and III were targeted for site-directed mutagenesis. Substitution of a phenylalanine residue (F328) by alanine reduced binding to the Bombyx mori cadherin by 23-fold, reduced biological activity against B. mori by 4-fold, while retaining activity against Lymantria dispar. CONCLUSION: The results identify a novel receptor-binding epitope and demonstrate that virtual elimination of binding to cadherin BR-175 does not completely remove toxicity in the case of B. mori. BioMed Central 2008-01-24 /pmc/articles/PMC2245940/ /pubmed/18218126 http://dx.doi.org/10.1186/1471-2091-9-3 Text en Copyright © 2008 You et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
You, Taek H
Lee, Mi K
Jenkins, Jeremy L
Alzate, Oscar
Dean, Donald H
Blocking binding of Bacillus thuringiensis Cry1Aa to Bombyx mori cadherin receptor results in only a minor reduction of toxicity
title Blocking binding of Bacillus thuringiensis Cry1Aa to Bombyx mori cadherin receptor results in only a minor reduction of toxicity
title_full Blocking binding of Bacillus thuringiensis Cry1Aa to Bombyx mori cadherin receptor results in only a minor reduction of toxicity
title_fullStr Blocking binding of Bacillus thuringiensis Cry1Aa to Bombyx mori cadherin receptor results in only a minor reduction of toxicity
title_full_unstemmed Blocking binding of Bacillus thuringiensis Cry1Aa to Bombyx mori cadherin receptor results in only a minor reduction of toxicity
title_short Blocking binding of Bacillus thuringiensis Cry1Aa to Bombyx mori cadherin receptor results in only a minor reduction of toxicity
title_sort blocking binding of bacillus thuringiensis cry1aa to bombyx mori cadherin receptor results in only a minor reduction of toxicity
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2245940/
https://www.ncbi.nlm.nih.gov/pubmed/18218126
http://dx.doi.org/10.1186/1471-2091-9-3
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