TY - JOUR
T1 - Cytolytic Peptide Fragments of Cyt1Aa from Bacillus thuringiensis subsp. israelensis
AU - Nisnevitch, Marina
AU - Nikonov, Svetlana
AU - Nitzan, Yeshayahu
N1 - 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).
PY - 2013/3
Y1 - 2013/3
N2 - 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.
AB - 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.
KW - Bacillus thuringiensisisraelensis
KW - Cyt1Aa
KW - Cytolytic peptides
KW - Liposomes
KW - Proteolysis
UR - http://www.scopus.com/inward/record.url?scp=84874241879&partnerID=8YFLogxK
U2 - 10.1007/s12013-012-9405-7
DO - 10.1007/s12013-012-9405-7
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C2 - 22875467
AN - SCOPUS:84874241879
SN - 1085-9195
VL - 65
SP - 121
EP - 127
JO - Cell Biochemistry and Biophysics
JF - Cell Biochemistry and Biophysics
IS - 2
ER -