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Complex of digestive proteinases of Galleria mellonella Caterpillars: composition, properties, and limited proteolysis of Bacillus thuringiensis endotoxins.
Biochemistry (Mosc). 2011 May; 76(5):581-9.B

Abstract

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.

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Publisher Full Text (DOI)

Authors+Show Affiliations

Bulushova NV
Scientific Research Institute for Genetics and Selection of Industrial Microorganisms, Moscow, Russia.
Elpidina EN
No affiliation info available
Zhuzhikov DP
No affiliation info available
Lyutikova LI
No affiliation info available
Ortego F
No affiliation info available
Kirillova NE
No affiliation info available
Zalunin IA
No affiliation info available
Chestukhina GG
No affiliation info available

MeSH

AnimalsBacillus thuringiensisBiocatalysisDigestive SystemEndotoxinsInsect ProteinsMothsPeptide Hydrolases

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

21639838

Citation

Bulushova, N V., et al. "Complex of Digestive Proteinases of Galleria Mellonella Caterpillars: Composition, Properties, and Limited Proteolysis of Bacillus Thuringiensis Endotoxins." Biochemistry. Biokhimiia, vol. 76, no. 5, 2011, pp. 581-9.
Bulushova NV, Elpidina EN, Zhuzhikov DP, et al. Complex of digestive proteinases of Galleria mellonella Caterpillars: composition, properties, and limited proteolysis of Bacillus thuringiensis endotoxins. Biochemistry (Mosc). 2011;76(5):581-9.
Bulushova, N. V., Elpidina, E. N., Zhuzhikov, D. P., Lyutikova, L. I., Ortego, F., Kirillova, N. E., Zalunin, I. A., & Chestukhina, G. G. (2011). Complex of digestive proteinases of Galleria mellonella Caterpillars: composition, properties, and limited proteolysis of Bacillus thuringiensis endotoxins. Biochemistry. Biokhimiia, 76(5), 581-9. https://doi.org/10.1134/S0006297911050087
Bulushova NV, et al. Complex of Digestive Proteinases of Galleria Mellonella Caterpillars: Composition, Properties, and Limited Proteolysis of Bacillus Thuringiensis Endotoxins. Biochemistry (Mosc). 2011;76(5):581-9. PubMed PMID: 21639838.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Complex of digestive proteinases of Galleria mellonella Caterpillars: composition, properties, and limited proteolysis of Bacillus thuringiensis endotoxins. AU - Bulushova,N V, AU - Elpidina,E N, AU - Zhuzhikov,D P, AU - Lyutikova,L I, AU - Ortego,F, AU - Kirillova,N E, AU - Zalunin,I A, AU - Chestukhina,G G, PY - 2011/6/7/entrez PY - 2011/6/7/pubmed PY - 2011/9/20/medline SP - 581 EP - 9 JF - Biochemistry. Biokhimiia JO - Biochemistry (Mosc) VL - 76 IS - 5 N2 - 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. SN - 1608-3040 UR - https://www.unboundmedicine.com/medline/citation/21639838/Complex_of_digestive_proteinases_of_Galleria_mellonella_Caterpillars:_composition_properties_and_limited_proteolysis_of_Bacillus_thuringiensis_endotoxins_ L2 - https://doi.org/10.1134/S0006297911050087 DB - PRIME DP - Unbound Medicine ER -