Complex of digestive proteinases of Galleria mellonella caterpillars. Composition, properties, and limited proteolysis of Bacillus thuringiensis endotoxins

The complex of digestive proteinases in caterpillars of the greater wax moth Galleria mellonella was studied. Using chromogenic substrates and inhibitor analysis, it was found that serine proteinases play a key role in this complex. Three anionic and two cationic forms of trypsin and one anionic and...

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Bibliographic Details
Published in:Biochemistry (Moscow) 2011-05, Vol.76 (5), p.581-589
Main Authors: Bulushova, N. V., Elpidina, E. N., Zhuzhikov, D. P., Lyutikova, L. I., Ortego, F., Kirillova, N. E., Zalunin, I. A., Chestukhina, G. G.
Format: Article
Language:English
Subjects:
Amino acids
Analysis
Animals
Bacillus thuringiensis
Bacillus thuringiensis - chemistry
Bacillus thuringiensis - metabolism
Biocatalysis
Biochemistry
Biomedical and Life Sciences
Biomedicine
Bioorganic Chemistry
Butterflies & moths
Digestive System - chemistry
Digestive System - enzymology
Endotoxins
Endotoxins - chemistry
Enzymes
Galleria mellonella
Hydrolases
Insect Proteins - chemistry
Insect Proteins - isolation & purification
Life Sciences
Microbiology
Moths - chemistry
Moths - enzymology
Peptide Hydrolases - chemistry
Peptide Hydrolases - isolation & purification
Plodia interpunctella
Proteins
Proteolysis
Surface active agents
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Summary:The complex of digestive proteinases in caterpillars of the greater wax moth Galleria mellonella was studied. Using chromogenic substrates and inhibitor analysis, it was found that serine proteinases play a key role in this complex. Three anionic and two cationic forms of trypsin and one anionic and one cationic form of chymotrypsin were identified by zymography in the midgut extract of G. mellonella . The most active trypsin was purified to electrophoretic homogeneity, and its N-terminal amino acid sequence was shown to be identical to that of mature trypsin from Plodia interpunctella . Midgut extract from G. mellonella was capable of processing Cry-proteins from Bacillus thuringiensis ssp. galleriae . Enzymes with tryptic and chymotryptic activities participate in this process, and activation of protoxin Cry9A is not the rate-limiting stage in the toxic action of this protein on the greater wax moth.
ISSN:0006-2979
1608-3040
DOI:10.1134/S0006297911050087