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Comparative analysis of proteinase activities of Bacillus thuringiensis-resistant and -susceptible Ostrinia nubilalis (Lepidoptera: Crambidae).
Insect Biochem Mol Biol. 2004 Aug; 34(8):753-62.IB

Abstract

Proteinase activities were compared in soluble and membrane fractions of guts obtained from larvae of Bacillus thuringiensis-resistant and -susceptible Ostrinia nubilalis. Overall, serine proteinases from soluble fractions of the susceptible strain were more active than those of the resistant strain. The soluble trypsin-like proteinase activity of the resistant strain was approximately half that of the susceptible strain. The number and relative molecular masses of soluble and membrane serine proteinases were different. However, there were no significant differences in the activities of serine proteinases and aminopeptidases extracted from midgut membranes of the two strains. Cry1Ab protoxin hydrolysis by soluble proteinase extracts of the resistant strain was reduced approximately 20-30% relative to that of the susceptible strain. Reduced protoxin processing due to decreased activities of Bt protoxin activation proteinases may be associated with resistance to Bt toxin in this resistant strain of O. nubilalis.

Authors+Show Affiliations

Li H
Department of Entomology, Kansas State University, Manhattan 66506, USA.
Oppert B
No affiliation info available
Higgins RA
No affiliation info available
Huang F
No affiliation info available
Zhu KY
No affiliation info available
Buschman LL
No affiliation info available

MeSH

AminopeptidasesAnimalsBacillus thuringiensisBacillus thuringiensis ToxinsBacterial ProteinsBacterial ToxinsChymotrypsinDigestive SystemEndopeptidasesEndotoxinsHemolysin ProteinsLarvaLepidopteraPancreatic ElastaseTrypsin

Pub Type(s)

Comparative Study
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

Language

eng

PubMed ID

15262280

Citation

Li, Huarong, et al. "Comparative Analysis of Proteinase Activities of Bacillus Thuringiensis-resistant and -susceptible Ostrinia Nubilalis (Lepidoptera: Crambidae)." Insect Biochemistry and Molecular Biology, vol. 34, no. 8, 2004, pp. 753-62.
Li H, Oppert B, Higgins RA, et al. Comparative analysis of proteinase activities of Bacillus thuringiensis-resistant and -susceptible Ostrinia nubilalis (Lepidoptera: Crambidae). Insect Biochem Mol Biol. 2004;34(8):753-62.
Li, H., Oppert, B., Higgins, R. A., Huang, F., Zhu, K. Y., & Buschman, L. L. (2004). Comparative analysis of proteinase activities of Bacillus thuringiensis-resistant and -susceptible Ostrinia nubilalis (Lepidoptera: Crambidae). Insect Biochemistry and Molecular Biology, 34(8), 753-62.
Li H, et al. Comparative Analysis of Proteinase Activities of Bacillus Thuringiensis-resistant and -susceptible Ostrinia Nubilalis (Lepidoptera: Crambidae). Insect Biochem Mol Biol. 2004;34(8):753-62. PubMed PMID: 15262280.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Comparative analysis of proteinase activities of Bacillus thuringiensis-resistant and -susceptible Ostrinia nubilalis (Lepidoptera: Crambidae). AU - Li,Huarong, AU - Oppert,Brenda, AU - Higgins,Randall A, AU - Huang,Fangneng, AU - Zhu,Kun Yan, AU - Buschman,Lawrent L, PY - 2003/04/02/received PY - 2004/03/24/accepted PY - 2004/7/21/pubmed PY - 2004/10/23/medline PY - 2004/7/21/entrez SP - 753 EP - 62 JF - Insect biochemistry and molecular biology JO - Insect Biochem Mol Biol VL - 34 IS - 8 N2 - Proteinase activities were compared in soluble and membrane fractions of guts obtained from larvae of Bacillus thuringiensis-resistant and -susceptible Ostrinia nubilalis. Overall, serine proteinases from soluble fractions of the susceptible strain were more active than those of the resistant strain. The soluble trypsin-like proteinase activity of the resistant strain was approximately half that of the susceptible strain. The number and relative molecular masses of soluble and membrane serine proteinases were different. However, there were no significant differences in the activities of serine proteinases and aminopeptidases extracted from midgut membranes of the two strains. Cry1Ab protoxin hydrolysis by soluble proteinase extracts of the resistant strain was reduced approximately 20-30% relative to that of the susceptible strain. Reduced protoxin processing due to decreased activities of Bt protoxin activation proteinases may be associated with resistance to Bt toxin in this resistant strain of O. nubilalis. SN - 0965-1748 UR - https://www.unboundmedicine.com/medline/citation/15262280/Comparative_analysis_of_proteinase_activities_of_Bacillus_thuringiensis_resistant_and__susceptible_Ostrinia_nubilalis__Lepidoptera:_Crambidae__ DB - PRIME DP - Unbound Medicine ER -