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A toxin-binding alkaline phosphatase fragment synergizes Bt toxin Cry1Ac against susceptible and resistant Helicoverpa armigera.
PLoS One. 2015; 10(4):e0126288.Plos

Abstract

Evolution of resistance by insects threatens the continued success of pest control using insecticidal crystal (Cry) proteins from the bacterium Bacillus thuringiensis (Bt) in sprays and transgenic plants. In this study, laboratory selection with Cry1Ac yielded five strains of cotton bollworm, Helicoverpa armigera, with resistance ratios at the median lethal concentration (LC50) of activated Cry1Ac ranging from 22 to 1700. Reduced activity and reduced transcription of an alkaline phosphatase protein that binds Cry1Ac was associated with resistance to Cry1Ac in the four most resistant strains. A Cry1Ac-binding fragment of alkaline phosphatase from H. armigera (HaALP1f) was not toxic by itself, but it increased mortality caused by Cry1Ac in a susceptible strain and in all five resistant strains. Although synergism of Bt toxins against susceptible insects by toxin-binding fragments of cadherin and aminopeptidase N has been reported previously, the results here provide the first evidence of synergism of a Bt toxin by a toxin-binding fragment of alkaline phosphatase. The results here also provide the first evidence of synergism of a Bt toxin by any toxin-binding peptide against resistant insects.

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Authors+Show Affiliations

Chen W
The State Key Laboratory for Biology of Plant Disease and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, West Yuanmingyuan Road, Beijing, 100193, China.
Liu C
The State Key Laboratory for Biology of Plant Disease and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, West Yuanmingyuan Road, Beijing, 100193, China.
Xiao Y
The State Key Laboratory for Biology of Plant Disease and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, West Yuanmingyuan Road, Beijing, 100193, China.
Zhang D
The State Key Laboratory for Biology of Plant Disease and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, West Yuanmingyuan Road, Beijing, 100193, China.
Zhang Y
The State Key Laboratory for Biology of Plant Disease and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, West Yuanmingyuan Road, Beijing, 100193, China.
Li X
Department of Entomology, University of Arizona, Tucson, AZ, 85721, United States of America.
Tabashnik BE
Department of Entomology, University of Arizona, Tucson, AZ, 85721, United States of America.
Wu K
The State Key Laboratory for Biology of Plant Disease and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, West Yuanmingyuan Road, Beijing, 100193, China.

MeSH

Alkaline PhosphataseAnimalsBacillus thuringiensis ToxinsBacterial ProteinsCD13 AntigensEndotoxinsEscherichia coliHemolysin ProteinsInsect ProteinsInsecticide ResistanceMothsPeptide Fragments

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

25885820

Citation

Chen, Wenbo, et al. "A Toxin-binding Alkaline Phosphatase Fragment Synergizes Bt Toxin Cry1Ac Against Susceptible and Resistant Helicoverpa Armigera." PloS One, vol. 10, no. 4, 2015, pp. e0126288.
Chen W, Liu C, Xiao Y, et al. A toxin-binding alkaline phosphatase fragment synergizes Bt toxin Cry1Ac against susceptible and resistant Helicoverpa armigera. PLoS One. 2015;10(4):e0126288.
Chen, W., Liu, C., Xiao, Y., Zhang, D., Zhang, Y., Li, X., Tabashnik, B. E., & Wu, K. (2015). A toxin-binding alkaline phosphatase fragment synergizes Bt toxin Cry1Ac against susceptible and resistant Helicoverpa armigera. PloS One, 10(4), e0126288. https://doi.org/10.1371/journal.pone.0126288
Chen W, et al. A Toxin-binding Alkaline Phosphatase Fragment Synergizes Bt Toxin Cry1Ac Against Susceptible and Resistant Helicoverpa Armigera. PLoS One. 2015;10(4):e0126288. PubMed PMID: 25885820.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - A toxin-binding alkaline phosphatase fragment synergizes Bt toxin Cry1Ac against susceptible and resistant Helicoverpa armigera. AU - Chen,Wenbo, AU - Liu,Chenxi, AU - Xiao,Yutao, AU - Zhang,Dandan, AU - Zhang,Yongdong, AU - Li,Xianchun, AU - Tabashnik,Bruce E, AU - Wu,Kongming, Y1 - 2015/04/17/ PY - 2013/04/01/received PY - 2015/03/31/accepted PY - 2015/4/18/entrez PY - 2015/4/18/pubmed PY - 2016/6/1/medline SP - e0126288 EP - e0126288 JF - PloS one JO - PLoS One VL - 10 IS - 4 N2 - Evolution of resistance by insects threatens the continued success of pest control using insecticidal crystal (Cry) proteins from the bacterium Bacillus thuringiensis (Bt) in sprays and transgenic plants. In this study, laboratory selection with Cry1Ac yielded five strains of cotton bollworm, Helicoverpa armigera, with resistance ratios at the median lethal concentration (LC50) of activated Cry1Ac ranging from 22 to 1700. Reduced activity and reduced transcription of an alkaline phosphatase protein that binds Cry1Ac was associated with resistance to Cry1Ac in the four most resistant strains. A Cry1Ac-binding fragment of alkaline phosphatase from H. armigera (HaALP1f) was not toxic by itself, but it increased mortality caused by Cry1Ac in a susceptible strain and in all five resistant strains. Although synergism of Bt toxins against susceptible insects by toxin-binding fragments of cadherin and aminopeptidase N has been reported previously, the results here provide the first evidence of synergism of a Bt toxin by a toxin-binding fragment of alkaline phosphatase. The results here also provide the first evidence of synergism of a Bt toxin by any toxin-binding peptide against resistant insects. SN - 1932-6203 UR - https://www.unboundmedicine.com/medline/citation/25885820/A_toxin_binding_alkaline_phosphatase_fragment_synergizes_Bt_toxin_Cry1Ac_against_susceptible_and_resistant_Helicoverpa_armigera_ DB - PRIME DP - Unbound Medicine ER -