Insights into the structural changes that trigger receptor binding upon proteolytic activation of bacillus thuringiensis vip3aa insecticidal protein

HIGHLIGHTS

• What: The authors show that Vip3Aa protoxin had low binding to Spodoptera frugiperda brush border membrane vesicles (BBMV) unlike the activated toxin that bound specifically in a concentration dependent way suggesting that a structural change upon Vip3Aa proteolytic activation is required for efficient receptor binding. The authors show here that Vip3Aa-protoxin shows very low or no toxicity to Sf9 cells in contrast to Vip3Aa-activated toxin that showed higher toxicity (Fig 2). In agreement, the authors show that Vip3Aa-activated toxin binding to BBMV was competed by Vip3Aa but not by Cry1Fa, confirming that Vip3Aa and . . .
  

   

  

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