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Resistance to Bacillus thuringiensis by the Indian meal moth, Plodia interpunctella: comparison of midgut proteinases from susceptible and resistant larvae.
J Invertebr Pathol. 1990 Mar; 55(2):235-44.JI

Abstract

Midgut homogenates from susceptible and resistant strains of the Indian meal moth, Plodia interpunctella, were compared for their ability to activate the entomocidal parasporal crystal protein from Bacillus thuringiensis. The properties of midgut proteinases from both types of larvae were also examined. Electrophoretic patterns of crystal protein from B. thuringiensis subspecies kurstaki (HD-1) and aizawai (HD-133 and HD-144) were virtually unchanged following digestion by either type of midgut homogenate. Changes in pH (9.5 to 11.5) or midgut homogenate concentration during digestion failed to substantially alter protein electrophoretic patterns of B. thuringiensis HD-1 crystal toxin. In vitro toxicity of crystal protein activated by either type of midgut preparation was equal toward cultured insect cells from either Manduca sexta or Choristoneura fumiferana. Electrophoresis of midgut extracts in polyacrylamide gels containing gelatin as substrate also yielded matching mobility patterns of proteinases from both types of midguts. Quantitation of midgut proteolytic activity using tritiated casein as a substrate revealed variation between midgut preparations, but no statistically significant differences between proteolytic activities from susceptible and resistant Indian meal moth larvae. Inhibition studies indicated that a trypsin-like proteinase with maximal activity at pH 10 is a major constituent of Indian meal moth midguts. The results demonstrated that midguts from susceptible and resistant strains of P. interpunctella are similar both in their ability to activate B. thuringiensis protoxin and in their proteolytic activity.

Authors+Show Affiliations

Johnson DE
U.S. Grain Marketing Research Laboratory, U.S. Department of Agriculture, Manhattan, Kansas 66502.
Brookhart GL
No affiliation info available
Kramer KJ
No affiliation info available
Barnett BD
No affiliation info available
McGaughey WH
No affiliation info available

MeSH

AnimalsBacillus thuringiensisBacillus thuringiensis ToxinsBacterial ProteinsBacterial ToxinsEndopeptidasesEndotoxinsHemolysin ProteinsLarvaLepidopteraMothsPest Control, Biological

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

2181026

Citation

Johnson, D E., et al. "Resistance to Bacillus Thuringiensis By the Indian Meal Moth, Plodia Interpunctella: Comparison of Midgut Proteinases From Susceptible and Resistant Larvae." Journal of Invertebrate Pathology, vol. 55, no. 2, 1990, pp. 235-44.
Johnson DE, Brookhart GL, Kramer KJ, et al. Resistance to Bacillus thuringiensis by the Indian meal moth, Plodia interpunctella: comparison of midgut proteinases from susceptible and resistant larvae. J Invertebr Pathol. 1990;55(2):235-44.
Johnson, D. E., Brookhart, G. L., Kramer, K. J., Barnett, B. D., & McGaughey, W. H. (1990). Resistance to Bacillus thuringiensis by the Indian meal moth, Plodia interpunctella: comparison of midgut proteinases from susceptible and resistant larvae. Journal of Invertebrate Pathology, 55(2), 235-44.
Johnson DE, et al. Resistance to Bacillus Thuringiensis By the Indian Meal Moth, Plodia Interpunctella: Comparison of Midgut Proteinases From Susceptible and Resistant Larvae. J Invertebr Pathol. 1990;55(2):235-44. PubMed PMID: 2181026.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Resistance to Bacillus thuringiensis by the Indian meal moth, Plodia interpunctella: comparison of midgut proteinases from susceptible and resistant larvae. AU - Johnson,D E, AU - Brookhart,G L, AU - Kramer,K J, AU - Barnett,B D, AU - McGaughey,W H, PY - 1990/3/1/pubmed PY - 2000/3/11/medline PY - 1990/3/1/entrez SP - 235 EP - 44 JF - Journal of invertebrate pathology JO - J Invertebr Pathol VL - 55 IS - 2 N2 - Midgut homogenates from susceptible and resistant strains of the Indian meal moth, Plodia interpunctella, were compared for their ability to activate the entomocidal parasporal crystal protein from Bacillus thuringiensis. The properties of midgut proteinases from both types of larvae were also examined. Electrophoretic patterns of crystal protein from B. thuringiensis subspecies kurstaki (HD-1) and aizawai (HD-133 and HD-144) were virtually unchanged following digestion by either type of midgut homogenate. Changes in pH (9.5 to 11.5) or midgut homogenate concentration during digestion failed to substantially alter protein electrophoretic patterns of B. thuringiensis HD-1 crystal toxin. In vitro toxicity of crystal protein activated by either type of midgut preparation was equal toward cultured insect cells from either Manduca sexta or Choristoneura fumiferana. Electrophoresis of midgut extracts in polyacrylamide gels containing gelatin as substrate also yielded matching mobility patterns of proteinases from both types of midguts. Quantitation of midgut proteolytic activity using tritiated casein as a substrate revealed variation between midgut preparations, but no statistically significant differences between proteolytic activities from susceptible and resistant Indian meal moth larvae. Inhibition studies indicated that a trypsin-like proteinase with maximal activity at pH 10 is a major constituent of Indian meal moth midguts. The results demonstrated that midguts from susceptible and resistant strains of P. interpunctella are similar both in their ability to activate B. thuringiensis protoxin and in their proteolytic activity. SN - 0022-2011 UR - https://www.unboundmedicine.com/medline/citation/2181026/Resistance_to_Bacillus_thuringiensis_by_the_Indian_meal_moth_Plodia_interpunctella:_comparison_of_midgut_proteinases_from_susceptible_and_resistant_larvae_ DB - PRIME DP - Unbound Medicine ER -