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Cloning eleven midgut trypsin cDNAs and evaluating the interaction of proteinase inhibitors with Cry1Ac against the tobacco budworm, Heliothis virescens (F.) (Lepidoptera: Noctuidae).
J Invertebr Pathol. 2012 Oct; 111(2):111-20.JI

Abstract

Midgut trypsins are associated with Bt protoxin activation and toxin degradation. Proteinase inhibitors have potential insecticidal toxicity against a wide range of insect species. This study was conducted to evaluate the interaction of proteinase inhibitors with Bt toxin and to examine midgut trypsin gene profile of Heliothis virescens. A sublethal dose (15 ppb) of Cry1Ac, 0.75% soybean trypsin inhibitor, and 0.1% and 0.2% N-α-tosyl-L-lysine chloromethyl ketone significantly suppressed midgut proteinase activities, and resulted in reductions in larval and pupal size and mass. The treatment with inhibitor+Bt suppressed approximately 65% more larval body mass and 21% more enzymatic activities than the inhibitor-only or Bt-only. Eleven trypsin-like cDNAs were sequenced from the midgut of H. virescens. All trypsins contained three catalytic center residues (H(73), D(153), and S(231)), substrate specificity determinant residues (D(225), G(250), and G(261)), and six cysteines for disulfide bridges. These putative trypsins were separated into three distinct groups, indicating the diverse proteinases evolved in this polyphagous insect. These results indicated that the insecticidal activity of proteinase inhibitors may be used to enhance Bt toxicity and delay resistance development.

Authors+Show Affiliations

USDA-ARS, Stoneville, MS, USA. yc.zhu@ars.usda.govNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

22824002

Citation

Zhu, Yu Cheng, et al. "Cloning Eleven Midgut Trypsin cDNAs and Evaluating the Interaction of Proteinase Inhibitors With Cry1Ac Against the Tobacco Budworm, Heliothis Virescens (F.) (Lepidoptera: Noctuidae)." Journal of Invertebrate Pathology, vol. 111, no. 2, 2012, pp. 111-20.
Zhu YC, Guo Z, Abel C. Cloning eleven midgut trypsin cDNAs and evaluating the interaction of proteinase inhibitors with Cry1Ac against the tobacco budworm, Heliothis virescens (F.) (Lepidoptera: Noctuidae). J Invertebr Pathol. 2012;111(2):111-20.
Zhu, Y. C., Guo, Z., & Abel, C. (2012). Cloning eleven midgut trypsin cDNAs and evaluating the interaction of proteinase inhibitors with Cry1Ac against the tobacco budworm, Heliothis virescens (F.) (Lepidoptera: Noctuidae). Journal of Invertebrate Pathology, 111(2), 111-20. https://doi.org/10.1016/j.jip.2012.07.003
Zhu YC, Guo Z, Abel C. Cloning Eleven Midgut Trypsin cDNAs and Evaluating the Interaction of Proteinase Inhibitors With Cry1Ac Against the Tobacco Budworm, Heliothis Virescens (F.) (Lepidoptera: Noctuidae). J Invertebr Pathol. 2012;111(2):111-20. PubMed PMID: 22824002.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Cloning eleven midgut trypsin cDNAs and evaluating the interaction of proteinase inhibitors with Cry1Ac against the tobacco budworm, Heliothis virescens (F.) (Lepidoptera: Noctuidae). AU - Zhu,Yu Cheng, AU - Guo,Zibiao, AU - Abel,Craig, Y1 - 2012/07/20/ PY - 2012/01/11/received PY - 2012/05/20/revised PY - 2012/07/11/accepted PY - 2012/7/25/entrez PY - 2012/7/25/pubmed PY - 2013/1/29/medline SP - 111 EP - 20 JF - Journal of invertebrate pathology JO - J Invertebr Pathol VL - 111 IS - 2 N2 - Midgut trypsins are associated with Bt protoxin activation and toxin degradation. Proteinase inhibitors have potential insecticidal toxicity against a wide range of insect species. This study was conducted to evaluate the interaction of proteinase inhibitors with Bt toxin and to examine midgut trypsin gene profile of Heliothis virescens. A sublethal dose (15 ppb) of Cry1Ac, 0.75% soybean trypsin inhibitor, and 0.1% and 0.2% N-α-tosyl-L-lysine chloromethyl ketone significantly suppressed midgut proteinase activities, and resulted in reductions in larval and pupal size and mass. The treatment with inhibitor+Bt suppressed approximately 65% more larval body mass and 21% more enzymatic activities than the inhibitor-only or Bt-only. Eleven trypsin-like cDNAs were sequenced from the midgut of H. virescens. All trypsins contained three catalytic center residues (H(73), D(153), and S(231)), substrate specificity determinant residues (D(225), G(250), and G(261)), and six cysteines for disulfide bridges. These putative trypsins were separated into three distinct groups, indicating the diverse proteinases evolved in this polyphagous insect. These results indicated that the insecticidal activity of proteinase inhibitors may be used to enhance Bt toxicity and delay resistance development. SN - 1096-0805 UR - https://www.unboundmedicine.com/medline/citation/22824002/Cloning_eleven_midgut_trypsin_cDNAs_and_evaluating_the_interaction_of_proteinase_inhibitors_with_Cry1Ac_against_the_tobacco_budworm_Heliothis_virescens__F____Lepidoptera:_Noctuidae__ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0022-2011(12)00172-3 DB - PRIME DP - Unbound Medicine ER -