Experientia

, Volume 46, Issue 5, pp 475–477 | Cite as

The toxicity of twoBacillus thuringiensisδ-endotoxins to gypsy moth larvae is inversely related to the affinity of binding sites on midgut brush border membranes for the toxins

  • M. G. Wolfersberger
Research Articles

Summary

Theδ-endotoxin fromBacillus thuringiensis subspecieskurstaki strain HD1-9 is almost 400 times more potent than theδ-endotoxin from strain HD-73 as a gypsy moth larvicide. The twoδ-endotoxins compete for a high-affinity binding site on the brush border membrane of larval gypsy moth midguts. The affinity for theδ-endotoxin from strain HD-73 is much greater than the affinity for theδ-endotoxin from strain HD1-9.

Key words

Membrane vesicles Lymantria dispar 

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Copyright information

© Birkhäuser Verlag 1990

Authors and Affiliations

  • M. G. Wolfersberger
    • 1
  1. 1.Department of BiologyTemple UniversityPhiladelphiaUSA

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