|GOMIS-CEBOLLA, JOAQUIN - University Of Valencia|
|WANG, YUEQUIN - Chinese Academy Of Agricultural Sciences|
|QUAN, YUDONG - University Of Valencia|
|HE, KANGLAI - Chinese Academy Of Agricultural Sciences|
|WALSH, TOM - Cornell University - New York|
|JAMES, BILL - Csiro, Black Mountain Laboratories|
|DOWNES, SHARON - Csiro, Australian Cotton Research Institute, Narrabri|
|KAIN, WENDY - Csiro, Australian Cotton Research Institute, Narrabri|
|WANG, PING - Cornell University - New York|
|FERRE, JUAN - University Of Valencia|
Submitted to: Journal of Invertebrate Pathology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 5/14/2018
Publication Date: 5/16/2018
Publication URL: https://handle.nal.usda.gov/10113/5971215
Citation: Gomis-Cebolla, J., Wang, Y., Quan, Y., He, K., Walsh, T., James, B., Downes, S., Kain, W., Wang, P., Leonard, K.H., Morgan, T.D., Oppert, B.S., Ferre, J. 2018. Analysis of cross-resistance to Vip3 proteins in eight insect colonies, from four insect species, selected for resistance to Bacillus thuringiensis insecticidal proteins. Journal of Invertebrate Pathology. 155:64-70. https://doi.org/10.1016/j.jip.2018.05.004.
Interpretive Summary: The proteins called “Vip3” are specific kinds of vegetative proteins made by the bacterium Bacillus thuringiensis. We compared the effect of Vip3 proteins on a number of different insects that are susceptible or resistant to another kind of bacterial protein called “Cry” (or crystal) proteins. We found that most insect species did not demonstrate cross resistance to Vip3 and Cry toxins. However, a Cry-resistant strain of one insect, the cotton bollworm, also was resistant to Vip3 toxins. These data help producers to identify control strategies that will be effective for field pests.
Technical Abstract: 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 toVip3 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.