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Identification of the Recognition Sequence in Gluten by the Prolyl Endoprotease of Eurygaster integriceps

Eurygaster integriceps Puton, Sunn pest, is the most globally destructive insect pest of bread wheat and durum wheat infecting 15 million hectares (HA) in Western and Central Asia and in Eastern Europe. To discontinue the harmful effects that current pesticide treatments have, environmentally safe biopesticides, inhibitors of the Sunn pest's digestive enzyme, are being sought. The objective of this study is to advance knowledge and understanding of the recognition sequences of the Sunn pest prolyl endoprotease (spPEP) within its natural substrate, gluten, as well as provide information towards the development of peptide inhibitors. The first method to the study is to separate gluten into glutenins (high molecular weight) and gliadins (low molecular weight). Gliadins were separated according to pI with BioRad's Rotofor Cell system and then by molecular weight with 12% SDS gels into their α/β, γ, and ω isoforms, Current results from the SDS gels indicate several gliadins have similar pI's between 7.22 pH and 8.72 pH consistent with the theoretical pI and molecular weight generated using the ExPASy Bioinformatics Resource Portal. The information from the NCBI database for the subdivisions of gliadins allowed identification of the proteins for spPEP in‐gel digestion. To date, γ gliadin has been identified with the predicted characteristics. Once digested, the fragments will be analyzed using MALDI‐Mass spectrometry to determine the mass and amino acid sequence of each fragment. Future experiments will include sending fragments to the Molecular Structure Facility at UC Davis, Davis CA for N‐terminal sequencing. When all the analysis is gathered, the data will be compared with the complete collection of gliadin sequences from NCBI to identify the cut and noncutting sites of the spPep for future design of inhibitors.