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Thin layer chromatography overlay technique in the analysis of the binding of the solubilized protoxin of Bacillus thuringiensis var. kurstaki to an insect glycosphingolipid of known structure
Author(s) -
Dennis R. D.,
Wiegandt H.,
Haustein D.,
Knowles B. H.,
Ellar D. J.
Publication year - 1986
Publication title -
biomedical chromatography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.4
H-Index - 65
eISSN - 1099-0801
pISSN - 0269-3879
DOI - 10.1002/bmc.1130010108
Subject(s) - glycolipid , bacillus thuringiensis , glycosphingolipid , chemistry , toxin , biochemistry , glycoprotein , glycoconjugate , chromatography , bacteria , biology , genetics
The hypothesis tested was that a particular glycoconjugate(s) in the exposed cell‐surface membrane of susceptible insect cells acts as a receptor and/or modulator for the specific interaction with the protoxin/activated toxin of the δ‐endotoxin of Bacillus thuringiensis var. kurstaki. As candidates, the total neutral and acidic fraction glycolipids, and the isolated neutral glycosphingolipid components, were screened for binding activity by the thin layer chromatogram overlay technique. The main protoxin/activated toxin‐binding glycolipid in the neutral fraction (5B) had the structure: Gal(α1‐3)GalNAc(β1‐4)GlcNAc(β1‐3)Man(β1‐4)Glc(β1‐1)Cer. The main protoxin/activated toxin‐binding glycolipid in the acidic fraction was designated band 1, the structure of which is at present unknown. The possibility that the component 5B carbohydrate sequence may also function as a toxin‐binding site of relevant insect plasma membrane glycoproteins is discussed.