The evolutionary success of insects in terms of biodiversity is promoted by their ability to adapt to a wide variety of feeding habits. As a polyphagous pest, the milkweed bug Spilostethus pandurus (Hemiptera: Lygaeidae) feeds on various seeds and plants, using a rich portfolio of peptidases for nutrition acquisition. However, there is only sparse knowledge about its proteolytic system. In the present study, peptidases from S. pandurus were purified using chromatographic techniques, putatively identified using mass spectrometry-based proteomics, by comparative transcriptome analyses and by gene amplification via polymerase chain reaction. Their complete sequences, catalytic functions, and physiological roles were further predicted based on bioinformatic tools and literature review, while their applicability for the hydrolysis of food proteins has been demonstrated. Understanding the proteolytic profile of S. pandurus could offer valuable insights into its interactions with the environment and host plants. Furthermore, these findings could contribute in the future to pest management strategies, plant protection efforts and the application of insect-derived enzymes as essential part of yellow biotechnology applications. • Peptidases from the milkweed bug Spilostethus pandurus were isolated, analyzed by MS-based proteomics and identified via homologous comparison with proteins from the taxonomically related (key species for comparison) bug Oncopeltus fasciatus. • Proteomics enabled the identification of serine, cysteine and metallopeptidases based on the BLAST against the NCBI protein database. • Transcriptome analyses of the identified peptidases confirmed that they are encoded in the S. pandurus genome and provided the complete peptidase sequences. • Information about the identified peptidases may be important for food protein hydrolysis, entomological studies, pest management and yellow biotechnology.
Albuquerque et al. (Fri,) studied this question.