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Altered protoxin activation by midgut enzymes from a Bacillus thuringiensis resistant strain of Plodia interpunctella.
Biochem Biophys Res Commun. 1994 Feb 15; 198(3):940-7.BB

Abstract

Processing of Bacillus thuringiensis protoxins to toxins by midgut proteinases from a strain of the Indianmeal moth, Plodia interpunctella (Hubner), resistant to B. thuringiensis subspecies entomocidus (HD-198) was slower than that by midgut proteinases from the susceptible parent strain or a strain resistant to B. thuringiensis subspecies kurstaki (HD-1, Dipel). Midgut extracts from entomocidus-resistant insects exhibited five-fold lower activity toward the synthetic substrate alpha-N-benzoyl-DL-arginine rho-nitroanilide than extracts from susceptible or kurstaki-resistant insects. Midgut enzymes from susceptible or kurstaki-resistant insects converted the 133 kDa CryIA(c) protoxin to 61-63 kDa proteins, while incubations with entomocidus-resistant enzymes resulted in predominantly products of intermediate size, even with increased amounts of midgut extract. The 61-63 kDa proteins were only produced by entomocidus-resistant midgut extracts after long term incubations with the protoxin. The data suggest that altered protoxin activation by midgut proteinases is involved in some types of insect resistance to B. thuringiensis.

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Authors+Show Affiliations

Oppert B
U.S. Grain Marketing Research Laboratory, ARS-USDA, Manhattan, KS 66502-2736.
Kramer KJ
No affiliation info available
Johnson DE
No affiliation info available
MacIntosh SC
No affiliation info available
McGaughey WH
No affiliation info available

MeSH

AnimalsBacillus thuringiensisBacillus thuringiensis ToxinsBacterial ProteinsBacterial ToxinsDigestive SystemElectrophoresis, Polyacrylamide GelEndopeptidasesEndotoxinsHemolysin ProteinsImmunity, InnateInsecticidesLethal Dose 50Molecular WeightMothsProtein PrecursorsProtein Processing, Post-TranslationalSubstrate Specificity

Pub Type(s)

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

Language

eng

PubMed ID

8117300

Citation

Oppert, B, et al. "Altered Protoxin Activation By Midgut Enzymes From a Bacillus Thuringiensis Resistant Strain of Plodia Interpunctella." Biochemical and Biophysical Research Communications, vol. 198, no. 3, 1994, pp. 940-7.
Oppert B, Kramer KJ, Johnson DE, et al. Altered protoxin activation by midgut enzymes from a Bacillus thuringiensis resistant strain of Plodia interpunctella. Biochem Biophys Res Commun. 1994;198(3):940-7.
Oppert, B., Kramer, K. J., Johnson, D. E., MacIntosh, S. C., & McGaughey, W. H. (1994). Altered protoxin activation by midgut enzymes from a Bacillus thuringiensis resistant strain of Plodia interpunctella. Biochemical and Biophysical Research Communications, 198(3), 940-7.
Oppert B, et al. Altered Protoxin Activation By Midgut Enzymes From a Bacillus Thuringiensis Resistant Strain of Plodia Interpunctella. Biochem Biophys Res Commun. 1994 Feb 15;198(3):940-7. PubMed PMID: 8117300.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Altered protoxin activation by midgut enzymes from a Bacillus thuringiensis resistant strain of Plodia interpunctella. AU - Oppert,B, AU - Kramer,K J, AU - Johnson,D E, AU - MacIntosh,S C, AU - McGaughey,W H, PY - 1994/2/15/pubmed PY - 2000/3/23/medline PY - 1994/2/15/entrez SP - 940 EP - 7 JF - Biochemical and biophysical research communications JO - Biochem Biophys Res Commun VL - 198 IS - 3 N2 - Processing of Bacillus thuringiensis protoxins to toxins by midgut proteinases from a strain of the Indianmeal moth, Plodia interpunctella (Hubner), resistant to B. thuringiensis subspecies entomocidus (HD-198) was slower than that by midgut proteinases from the susceptible parent strain or a strain resistant to B. thuringiensis subspecies kurstaki (HD-1, Dipel). Midgut extracts from entomocidus-resistant insects exhibited five-fold lower activity toward the synthetic substrate alpha-N-benzoyl-DL-arginine rho-nitroanilide than extracts from susceptible or kurstaki-resistant insects. Midgut enzymes from susceptible or kurstaki-resistant insects converted the 133 kDa CryIA(c) protoxin to 61-63 kDa proteins, while incubations with entomocidus-resistant enzymes resulted in predominantly products of intermediate size, even with increased amounts of midgut extract. The 61-63 kDa proteins were only produced by entomocidus-resistant midgut extracts after long term incubations with the protoxin. The data suggest that altered protoxin activation by midgut proteinases is involved in some types of insect resistance to B. thuringiensis. SN - 0006-291X UR - https://www.unboundmedicine.com/medline/citation/8117300/Altered_protoxin_activation_by_midgut_enzymes_from_a_Bacillus_thuringiensis_resistant_strain_of_Plodia_interpunctella_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006-291X(84)71134-X DB - PRIME DP - Unbound Medicine ER -