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Analysis of cross-resistance to Vip3 proteins in eight insect colonies, from four insect species, selected for resistance to Bacillus thuringiensis insecticidal proteins

Joaquín Gomis-Cebolla, Yuequin Wang, Yudong Quan, Kanglai He, Tom Walsh, Bill James, Sharon Downes, Wendy Kain, Ping Wang, Kathy Leonard, Tom Morgan, Brenda Oppert, Juan Ferré
Journal of invertebrate pathology 2018 v.155 pp. 64-70
Bacillus thuringiensis, Helicoverpa armigera, Ostrinia furnacalis, Plodia interpunctella, Trichoplusia ni, cross resistance, developmental stages, diet, growth retardation, insect colonies, insecticidal proteins, insects, lethal concentration 50, midgut, proteinases, receptors, toxicity, vegetative growth
Bacillus thuringiensis Vip3 proteins are synthesized and secreted during the vegetative growth phase. They are activated by gut proteases, recognize and bind to midgut receptors, form pores and lyse cells. We tested the susceptibility to Vip3Aa and Vip3Ca of Cry1A-, Cry2A-, Dipel- and Vip3-resistant insect colonies from different species to determine whether resistance to other insecticidal proteins confers cross-resistance to Vip3 proteins. As expected, the colonies resistant to Cry1A proteins, Dipel (Helicoverpa armigera, Trichoplusia ni, Ostrinia furnacalis and Plodia interpunctella) or Cry2Ab (H. armigera and T. ni) were not cross-resistant to Vip3 proteins. In contrast, H. armigera colonies resistant to Vip3Aa or Vip3Aa/Cry2Ab showed cross-resistance to the Vip3Ca protein. Moreover, the Vip3Ca protein was highly toxic to O. furnacalis (LC50 not significantly different from that of Cry1Ab), whereas the Vip3Aa protein only showed moderate growth inhibition at the highest concentration tested (100 µg/g of diet). These results extend the cross-resistance studies between Vip3 and Cry proteins, show for the first time cross-resistance between proteins within the Vip3 subfamily, and points to O. furnacalis as a target for the Vip3Ca protein.