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Altered binding of the Cry1Ac toxin to larval membranes but not to the toxin-binding protein in Plodia interpunctella selected for resistance to different Bacillus thuringiensis isolates.
Appl Environ Microbiol. 1996 Nov; 62(11):4168-73.AE

Abstract

Immunoblotting and cytochemical procedures were used to determine whether toxin binding was altered in strains of the Indianmeal moth, Plodia interpunctella, selected for resistance to various strains of Bacillus thuringiensis. Each of these B. thuringiensis subspecies produces a mixture of protoxins, primarily Cry1 types, and the greatest insect resistance is to the Cry1A protoxins. In several cases, however, there was also resistance to toxins not present in the B. thuringiensis strains used for selection. The Cry1Ab and Cry1Ac toxins bound equally well over a range of toxin concentrations and times of incubation to a single protein of ca. 80-kDa in immunoblots of larval membrane extracts from all of the colonies. This binding protein is essential for toxicity since a mutant Cry1Ac toxin known to be defective in binding and thus less toxic bound poorly to the 80-kDa protein. This binding protein differed in size from the major aminopeptidase N antigens implicated in toxin binding in other insects. Binding of fluorescently labeled Cry1Ac or Cry1Ab toxin to larval sections was found at the tips of the brush border membrane prepared from the susceptible but not from any of the resistant P. interpunctella. Accessibility of a major Cry1A-binding protein appears to be altered in resistant larvae and could account for their broad resistance to several B. thuringiensis toxins.

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Authors+Show Affiliations

Mohammed SI
Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907, USA.
Johnson DE
No affiliation info available
Aronson AI
No affiliation info available

MeSH

AnimalsBacillus thuringiensisBacillus thuringiensis ToxinsBacterial ProteinsBacterial ToxinsCarrier ProteinsEndotoxinsHemolysin ProteinsLarvaMicrovilliMothsPest Control, BiologicalProtein Binding

Pub Type(s)

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

Language

eng

PubMed ID

8900008

Citation

Mohammed, S I., et al. "Altered Binding of the Cry1Ac Toxin to Larval Membranes but Not to the Toxin-binding Protein in Plodia Interpunctella Selected for Resistance to Different Bacillus Thuringiensis Isolates." Applied and Environmental Microbiology, vol. 62, no. 11, 1996, pp. 4168-73.
Mohammed SI, Johnson DE, Aronson AI. Altered binding of the Cry1Ac toxin to larval membranes but not to the toxin-binding protein in Plodia interpunctella selected for resistance to different Bacillus thuringiensis isolates. Appl Environ Microbiol. 1996;62(11):4168-73.
Mohammed, S. I., Johnson, D. E., & Aronson, A. I. (1996). Altered binding of the Cry1Ac toxin to larval membranes but not to the toxin-binding protein in Plodia interpunctella selected for resistance to different Bacillus thuringiensis isolates. Applied and Environmental Microbiology, 62(11), 4168-73.
Mohammed SI, Johnson DE, Aronson AI. Altered Binding of the Cry1Ac Toxin to Larval Membranes but Not to the Toxin-binding Protein in Plodia Interpunctella Selected for Resistance to Different Bacillus Thuringiensis Isolates. Appl Environ Microbiol. 1996;62(11):4168-73. PubMed PMID: 8900008.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Altered binding of the Cry1Ac toxin to larval membranes but not to the toxin-binding protein in Plodia interpunctella selected for resistance to different Bacillus thuringiensis isolates. AU - Mohammed,S I, AU - Johnson,D E, AU - Aronson,A I, PY - 1996/11/1/pubmed PY - 2000/3/23/medline PY - 1996/11/1/entrez SP - 4168 EP - 73 JF - Applied and environmental microbiology JO - Appl Environ Microbiol VL - 62 IS - 11 N2 - Immunoblotting and cytochemical procedures were used to determine whether toxin binding was altered in strains of the Indianmeal moth, Plodia interpunctella, selected for resistance to various strains of Bacillus thuringiensis. Each of these B. thuringiensis subspecies produces a mixture of protoxins, primarily Cry1 types, and the greatest insect resistance is to the Cry1A protoxins. In several cases, however, there was also resistance to toxins not present in the B. thuringiensis strains used for selection. The Cry1Ab and Cry1Ac toxins bound equally well over a range of toxin concentrations and times of incubation to a single protein of ca. 80-kDa in immunoblots of larval membrane extracts from all of the colonies. This binding protein is essential for toxicity since a mutant Cry1Ac toxin known to be defective in binding and thus less toxic bound poorly to the 80-kDa protein. This binding protein differed in size from the major aminopeptidase N antigens implicated in toxin binding in other insects. Binding of fluorescently labeled Cry1Ac or Cry1Ab toxin to larval sections was found at the tips of the brush border membrane prepared from the susceptible but not from any of the resistant P. interpunctella. Accessibility of a major Cry1A-binding protein appears to be altered in resistant larvae and could account for their broad resistance to several B. thuringiensis toxins. SN - 0099-2240 UR - https://www.unboundmedicine.com/medline/citation/8900008/Altered_binding_of_the_Cry1Ac_toxin_to_larval_membranes_but_not_to_the_toxin_binding_protein_in_Plodia_interpunctella_selected_for_resistance_to_different_Bacillus_thuringiensis_isolates_ L2 - https://journals.asm.org/doi/10.1128/aem.62.11.4168-4173.1996?url_ver=Z39.88-2003&rfr_id=ori:rid:crossref.org&rfr_dat=cr_pub=pubmed DB - PRIME DP - Unbound Medicine ER -