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Antisera-mediated in vivo reduction of Cry1Ac toxicity in Helicoverpa armigera.
J Insect Physiol. 2010 Jul; 56(7):718-24.JI

Abstract

A functional assessment of Bacillus thuringiensis (Bt) toxin receptors in the midgut of lepidopteran insects will facilitate understanding of the toxin mode of action and provide effective strategies to counter the development of resistance. In this study, we produced anti-aminopeptidase (APN) and anti-cadherin sera with purified Cry1Ac toxin-binding APN or cadherin fragments from Heliocoverpa armigera. Antisera were evaluated for their effects on Cry1Ac toxicity through bioassays. Our results indicated that both the anti-APN and anti-cadherin sera reduced Cry1Ac toxicity in vivo, although cadherin antiserum reduced toxicity more than APN antiserum. These results suggest that both APN and cadherin are involved in Cry1Ac intoxication of H. armigera, evidence that the pore formation model may be representative of Cry1Ac toxin mode of action in this insect.

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Authors+Show Affiliations

Liu C
State Key Laboratory of Plant Disease and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Science, West Yuanmingyuan Road, Beijing 100193, China.
Gao Y
No affiliation info available
Ning C
No affiliation info available
Wu K
No affiliation info available
Oppert B
No affiliation info available
Guo Y
No affiliation info available

MeSH

AminopeptidasesAnimalsBacillus thuringiensis ToxinsBacterial ProteinsCadherinsEndotoxinsHemolysin ProteinsImmune SeraInsect ProteinsMothsProtein BindingRabbits

Pub Type(s)

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

Language

eng

PubMed ID

20035762

Citation

Liu, Chenxi, et al. "Antisera-mediated in Vivo Reduction of Cry1Ac Toxicity in Helicoverpa Armigera." Journal of Insect Physiology, vol. 56, no. 7, 2010, pp. 718-24.
Liu C, Gao Y, Ning C, et al. Antisera-mediated in vivo reduction of Cry1Ac toxicity in Helicoverpa armigera. J Insect Physiol. 2010;56(7):718-24.
Liu, C., Gao, Y., Ning, C., Wu, K., Oppert, B., & Guo, Y. (2010). Antisera-mediated in vivo reduction of Cry1Ac toxicity in Helicoverpa armigera. Journal of Insect Physiology, 56(7), 718-24. https://doi.org/10.1016/j.jinsphys.2009.12.012
Liu C, et al. Antisera-mediated in Vivo Reduction of Cry1Ac Toxicity in Helicoverpa Armigera. J Insect Physiol. 2010;56(7):718-24. PubMed PMID: 20035762.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Antisera-mediated in vivo reduction of Cry1Ac toxicity in Helicoverpa armigera. AU - Liu,Chenxi, AU - Gao,Yulin, AU - Ning,Changming, AU - Wu,Kongming, AU - Oppert,Brenda, AU - Guo,Yuyuan, Y1 - 2009/12/27/ PY - 2009/11/05/received PY - 2009/12/11/revised PY - 2009/12/17/accepted PY - 2009/12/29/entrez PY - 2009/12/29/pubmed PY - 2010/9/15/medline SP - 718 EP - 24 JF - Journal of insect physiology JO - J Insect Physiol VL - 56 IS - 7 N2 - A functional assessment of Bacillus thuringiensis (Bt) toxin receptors in the midgut of lepidopteran insects will facilitate understanding of the toxin mode of action and provide effective strategies to counter the development of resistance. In this study, we produced anti-aminopeptidase (APN) and anti-cadherin sera with purified Cry1Ac toxin-binding APN or cadherin fragments from Heliocoverpa armigera. Antisera were evaluated for their effects on Cry1Ac toxicity through bioassays. Our results indicated that both the anti-APN and anti-cadherin sera reduced Cry1Ac toxicity in vivo, although cadherin antiserum reduced toxicity more than APN antiserum. These results suggest that both APN and cadherin are involved in Cry1Ac intoxication of H. armigera, evidence that the pore formation model may be representative of Cry1Ac toxin mode of action in this insect. SN - 1879-1611 UR - https://www.unboundmedicine.com/medline/citation/20035762/Antisera_mediated_in_vivo_reduction_of_Cry1Ac_toxicity_in_Helicoverpa_armigera_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0022-1910(09)00393-X DB - PRIME DP - Unbound Medicine ER -