Molecular and Insecticidal Characterization of a Novel Cry-Related Protein from Bacillus Thuringiensis Toxic against Myzus persicae

This study describes the insecticidal activity of a novel <i>Bacillus thuringiensis</i> Cry-related protein with a deduced 799 amino acid sequence (~89 kDa) and ~19% pairwise identity to the 95-kDa-aphidicidal protein (sequence number 204) from patent US 8318900 and ~40% pairwise identity to the cancer cell killing Cry proteins (parasporins Cry41Ab1 and Cry41Aa1), respectively. This novel Cry-related protein contained the five conserved amino acid blocks and the three conserved domains commonly found in 3-domain Cry proteins. The protein exhibited toxic activity against the green peach aphid, <i>Myzus persica</i>e (Sulzer) (Homoptera: Aphididae) with the lowest mean lethal concentration (LC₅₀ = 32.7 μg/mL) reported to date for a given Cry protein and this insect species, whereas it had no lethal toxicity against the Lepidoptera of the family Noctuidae <i>Helicoverpa armigera </i>(Hübner), <i>Mamestra brassicae </i>(L.), <i>Spodoptera exigua </i>(Hübner), <i>S. frugiperda</i> (J.E. Smith) and <i>S. littoralis </i>(Boisduval), at concentrations as high as ~3.5 μg/cm². This novel Cry-related protein may become a promising environmentally friendly tool for the biological control of <i>M. persicae</i> and possibly also for other sap sucking insect pests.

This research was supported by the Spanish Ministry of Science and Innovation (Grant Ref. AGL2009-13340-C02) and by the Universidad Pública de Navarra (contract awarded to L.P.). We thank Trevor Williams for his kind revision of the manuscript.

We acknowledge support by the CSIC Open Access Publication Initiative through its Unit of Information Resources for Research (URICI).