Synapse
⌘+K
Synapse
PulseExploreClubsResearchersJournals
Instagram
HomeClubsExplore
May 1, 1990Applied and Environmental MicrobiologyOpen Access

Receptors on the brush border membrane of the insect midgut as determinants of the specificity of Bacillus thuringiensis delta-endotoxins

View Full Paper
Ask AI
Bookmark
Share

Authors

JRJeroen Van RieBASF (United States)SJStefan JansensUniversitat de ValènciaHHHerman HöfteAgroParisTech

Discussion

Loading...

Member takes

Implication

In vitro assays reveal high-affinity midgut receptor binding dictates toxin specificity across three lepidopteran species, indicating receptor variation governs insect sensitivity.

Key Points

  • To identify the biochemical mechanism driving differences in the insecticidal spectrum of Bacillus thuringiensis insecticidal crystal proteins.
  • Assessed toxicity profiles of three distinct Bacillus thuringiensis insecticidal crystal proteins (ICPs) against three lepidopteran target species.
  • Performed membrane-binding assays using 125I-radiolabeled ICPs with brush border membrane vesicles isolated from larval midguts.
  • Toxins exhibited high-affinity, saturable binding to brush border membrane vesicles only in sensitive insect species.
  • ICPs with no insecticidal activity against a specific species showed no saturable binding to midgut vesicles, while receptor site heterogeneity enabled susceptibility to multiple ICP variants.

Cite This Study

Rie et al. (1990) studied this question.

synapsesocial.com/papers/6a767a8053fd60d5b195ca92https://doi.org/10.1128/aem.56.5.1378-1385.1990
View Full Paper
Ask AI
Bookmark
Share

Also Consider

Synapse has enriched 2 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Specificity of Bacillus thuringiensis delta-endotoxins is correlated with the presence of high-affinity binding sites in the brush border membrane of target insect midguts.1988 · 437 citations
  2. 2Specificity of Bacillus thuringiensis var. colmeri insecticidal delta-endotoxin is determined by differential proteolytic processing of the protoxin by larval gut proteases1986 · 151 citations