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Cellular toxicities and membrane binding characteristics of insecticidal crystal proteins from Bacillus thuringiensis toward cultured insect cells.
J Invertebr Pathol. 1994 Mar; 63(2):123-9.JI

Abstract

The pattern of in vitro toxicity of activated toxins from several classes of entomocidal inclusion genes from Bacillus thuringiensis was measured using eight established cell lines from lepidopteran insects. Protoxins representing CryIA(b), CryIA(c), and a mixture of all three CryIA toxins (subtypes a, b, and c; from B. thuringiensis subsp. kurstaki HD-1) were compared with the protoxin representing CryIC in a bioassay which measured the viability of cultured insect cells upon exposure to entomocidal toxin proteins. The responses of the various cell lines were very specific toward the individual toxin proteins. CryIC activated protoxin was toxic for cells of Manduca sexta, Plodia interpunctella, and to a lesser extent Spodoptera frugiperda. CryIA(b) and CryIA(c) proteins were toxic toward M. sexta but relatively non-toxic for P. interpunctella or S. frugiperda. The toxicity of CryIA(b), CryIA(c), and the composite CryIA activated toxins toward cells of Choristoneura fumiferana varied substantially, with the CryIA mixture being slightly more toxic than CryIA(c) alone. CryIC toxin had no effect toward C. fumiferana cells. Probit regression analysis of dose-response relationships between insect species and crystal protein composition demonstrated specific patterns of toxicity which may be related to membrane-receptor site binding by specific toxins. Membrane binding analysis of 125I-labeled CryIA(b), CryIA(c), and CryIC toxins to insect cells from three of the cell lines yielded high specific binding only with M. sexta cells toward CryIA(c) toxin. Lower levels of binding were observed with CryIA(b) and CryIC toward cells of C. fumiferana and P. interpunctella. Although relatively low binding levels for CryIC were observed with P. interpunctella cells, toxicity was high for these cells.(

ABSTRACT

TRUNCATED AT 250 WORDS)

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Publisher Full Text

Authors+Show Affiliations

Johnson DE
USDA, ARS, U.S. Grain Marketing Research Laboratory, Manhattan, Kansas 66502.

MeSH

AnimalsBacillus thuringiensis ToxinsBacterial ProteinsBacterial ToxinsCells, CulturedEndotoxinsHemolysin ProteinsInsectaPest Control, Biological

Pub Type(s)

Journal Article

Language

eng

PubMed ID

8176242

Citation

Johnson, D E.. "Cellular Toxicities and Membrane Binding Characteristics of Insecticidal Crystal Proteins From Bacillus Thuringiensis Toward Cultured Insect Cells." Journal of Invertebrate Pathology, vol. 63, no. 2, 1994, pp. 123-9.
Johnson DE. Cellular toxicities and membrane binding characteristics of insecticidal crystal proteins from Bacillus thuringiensis toward cultured insect cells. J Invertebr Pathol. 1994;63(2):123-9.
Johnson, D. E. (1994). Cellular toxicities and membrane binding characteristics of insecticidal crystal proteins from Bacillus thuringiensis toward cultured insect cells. Journal of Invertebrate Pathology, 63(2), 123-9.
Johnson DE. Cellular Toxicities and Membrane Binding Characteristics of Insecticidal Crystal Proteins From Bacillus Thuringiensis Toward Cultured Insect Cells. J Invertebr Pathol. 1994;63(2):123-9. PubMed PMID: 8176242.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Cellular toxicities and membrane binding characteristics of insecticidal crystal proteins from Bacillus thuringiensis toward cultured insect cells. A1 - Johnson,D E, PY - 1994/3/1/pubmed PY - 2000/3/23/medline PY - 1994/3/1/entrez SP - 123 EP - 9 JF - Journal of invertebrate pathology JO - J Invertebr Pathol VL - 63 IS - 2 N2 - The pattern of in vitro toxicity of activated toxins from several classes of entomocidal inclusion genes from Bacillus thuringiensis was measured using eight established cell lines from lepidopteran insects. Protoxins representing CryIA(b), CryIA(c), and a mixture of all three CryIA toxins (subtypes a, b, and c; from B. thuringiensis subsp. kurstaki HD-1) were compared with the protoxin representing CryIC in a bioassay which measured the viability of cultured insect cells upon exposure to entomocidal toxin proteins. The responses of the various cell lines were very specific toward the individual toxin proteins. CryIC activated protoxin was toxic for cells of Manduca sexta, Plodia interpunctella, and to a lesser extent Spodoptera frugiperda. CryIA(b) and CryIA(c) proteins were toxic toward M. sexta but relatively non-toxic for P. interpunctella or S. frugiperda. The toxicity of CryIA(b), CryIA(c), and the composite CryIA activated toxins toward cells of Choristoneura fumiferana varied substantially, with the CryIA mixture being slightly more toxic than CryIA(c) alone. CryIC toxin had no effect toward C. fumiferana cells. Probit regression analysis of dose-response relationships between insect species and crystal protein composition demonstrated specific patterns of toxicity which may be related to membrane-receptor site binding by specific toxins. Membrane binding analysis of 125I-labeled CryIA(b), CryIA(c), and CryIC toxins to insect cells from three of the cell lines yielded high specific binding only with M. sexta cells toward CryIA(c) toxin. Lower levels of binding were observed with CryIA(b) and CryIC toward cells of C. fumiferana and P. interpunctella. Although relatively low binding levels for CryIC were observed with P. interpunctella cells, toxicity was high for these cells.(ABSTRACT TRUNCATED AT 250 WORDS) SN - 0022-2011 UR - https://www.unboundmedicine.com/medline/citation/8176242/Cellular_toxicities_and_membrane_binding_characteristics_of_insecticidal_crystal_proteins_from_Bacillus_thuringiensis_toward_cultured_insect_cells_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0022-2011(84)71024-X DB - PRIME DP - Unbound Medicine ER -