Cytolytic Peptide Fragments of Cyt1Aa from Bacillus thuringiensis subsp. israelensis

Marina Nisnevitch, Svetlana Nikonov, Yeshayahu Nitzan

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2 Scopus citations


Cyt1Aa is the major and most active component of the parasporal crystal of the Gram-positive soil entomopathogenic bacterium Bacillus thuringiensis subsp. israelensis. The Cyt1Aa protoxin exhibits some hemolytic and cytolytic activity. However, highly active 22-25 kDa toxins are obtained after proteolysis of Cyt1Aa from both the N- and the C-termini. As shown in this study, preliminary binding of the protoxin to polylamellary liposomes or partial denaturation of Cyt1Aa and further processing by several exogenous proteases yielded short 4. 9-11. 5 kDa cytolytic peptide fragments of Cyt1Aa. The shortest 51 amino acid peptide was obtained after pre-incubation of Cyt1Aa with SDS and proteolysis with proteinase K. This peptide was purified, identified as the Ile87-Asp137 fragment of Cyt1Aa and was shown to exhibit more than 30 % hemolysis of rabbit erythrocytes.

Original languageEnglish
Pages (from-to)121-127
Number of pages7
JournalCell Biochemistry and Biophysics
Issue number2
StatePublished - Mar 2013

Bibliographical note

Funding Information:
Acknowledgments This research was supported in part by the Research Authority of the Ariel University Center of Samaria and the Rappaport Foundation for Medical Microbiology, Bar-Ilan University, Israel (to YN).


  • Bacillus thuringiensisisraelensis
  • Cyt1Aa
  • Cytolytic peptides
  • Liposomes
  • Proteolysis


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