Abstract
Sunn pest or Sunn bug, Eurygaster integriceps Put., salivary gland proteases are responsible for the deterioration of wheat flour quality during dough mixing, resulting from gluten hydrolysis. These proteases are highly heterogeneous and show low sensitivity to most types of proteinaceous inhibitors, meaning that such inhibitors cannot be used to prevent gluten damage. The present study describes the generation of a specific peptide antibody, raised against the active center of the recombinant gluten‐hydrolyzing protease (GHP3). The recombinant protein, encoding two repeats of the GHP3 sequence element involved in forming the S4 pocket and binding of substrate at position P4, was designed and expressed in Escherichia coli. The antibodies raised to this recombinant protein showed inhibitory activity against the GHP3 protease. The results indicate that it is possible to design specific antibodies to inhibit wheat‐bug gluten‐hydrolyzing proteases.
Highlights
Proteases are involved in many processes occurring in living organisms including, normal digestion, protein processing, and blood clotting but they are involved in damaging pathologies such as infection, inflammation, and thrombosis
To ensure specificity of inhibitor action, that is, that the inhibitory activity would only be against the Sunn pest protease and not beneficial proteases present in nontarget organisms, the selected oligopeptide sequence was compared with digestive protease sequences from a range of species
Antibodies produced to the chimeric recombinant protein, specific for the S4 binding pocket in the active site of GHP3, showed inhibitory activity toward GHP3 protease, using two recombinant peptide substrates
Summary
Proteases are involved in many processes occurring in living organisms including, normal digestion, protein processing, and blood clotting but they are involved in damaging pathologies such as infection, inflammation, and thrombosis. Just as drugs are developed in medicine to suppress the destructive activity of proteases based on proteinaceous inhibitors from plants and animals (Gitlin-Domagalska et al, 2017; Malik et al, 2015), a similar approach could be used to protect wheat grain proteins from damage by Sunn pest proteases. The application of this approach is complicated in the case of Sunn pest proteases by the high heterogeneity of salivary gland proteases and the low sensitivity of these proteases to the main types of known protease inhibitors (Konarev et al, 2011, 2019). Inhibitory activity of the antibody was tested against the recombinant form of Sunn bug protease, rGHP3p2
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