期刊
JOURNAL OF INVERTEBRATE PATHOLOGY
卷 107, 期 3, 页码 185-192出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jip.2011.04.007
关键词
Bacillus thuringiensis; Bt maize; Ostrinia nubilalis; Resistance; Toxin binding; Luminal gut proteases
类别
资金
- Agricultural Biotechnology Stewardship Technical Committee
- National Science Foundation Center for Integrated Pest Management
The cross-resistance spectrum and biochemical mechanism of resistance to the Bacillus thuringiensis Cry1Ab toxin was studied in a field-derived strain of Ostrinia nubilalis (Hilbner)(Lepidoptera: Crambidae) that was further selected in the laboratory for high levels (> 1000-fold) of resistance to Cry1Ab. The resistant strain exhibited high levels of cross-resistance to Cry1Ac and Cry1Aa but only low levels of cross-resistance (< 4-fold) to CryIF. In addition, there was no significant difference between the levels of resistance to full-length and trypsin-activated Cry1Ab protein. No differences in activity of luminal gut proteases or altered proteolytic processing of the toxin were observed in the resistant strain. Significantly reduced binding of radiolabeled Cry1Aa was observed in the resistant strain whereas binding of Cry1Ab and Cry1Ac was practically the same in both resistant and susceptible strains. The interpretation of the overall data seems to suggest the involvement of an alteration in the binding of Cry1A toxins to a common receptor, which is more clearly revealed by the binding assays using radiolabeled Cry1Aa. (C) 2011 Elsevier Inc. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据