The mosquito larvicidal activity of 130 kDa delta-endotoxin of Bacillus thuringiensis var. israelensis resides in the 72 kDa amino-terminal fragment

Biochem Biophys Res Commun. 1988 May 31;153(1):294-300. doi: 10.1016/s0006-291x(88)81221-x.

Abstract

Bacillus thuringiensis var. israelensis produces 130 kDa delta-endotoxin which is highly toxic to mosquito-larvae. The mosquito-larvicidal activity was delineated by sequential deletions from ends of the 1136 amino acids delta-endotoxin. A maximum of 459 amino acids could be removed from the carboxy-terminal of the toxin without a significant loss of the larvicidal activity. However, no more than 38 amino acids could be deleted from the amino-terminal without losing the toxicity. The truncated peptide of 72 kDa exhibited similar toxicity to the 130 kDa toxin and was between 39th and 677th amino acids.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bacillus thuringiensis / analysis*
  • Bacillus thuringiensis Toxins
  • Bacterial Proteins*
  • Bacterial Toxins*
  • Base Sequence
  • Chromosome Deletion
  • Culicidae / drug effects*
  • Endotoxins / genetics
  • Endotoxins / pharmacology*
  • Hemolysin Proteins
  • Larva / drug effects
  • Molecular Sequence Data
  • Molecular Weight
  • Peptide Fragments / analysis*

Substances

  • Bacillus thuringiensis Toxins
  • Bacterial Proteins
  • Bacterial Toxins
  • Endotoxins
  • Hemolysin Proteins
  • Peptide Fragments
  • insecticidal crystal protein, Bacillus Thuringiensis