Intestinal proteases profiling from Anticarsia gemmatalis and their binding to inhibitors

• Published in: Archives of insect biochemistry and physiology Vol. 107; no. 3; pp. e21792 - n/a
• Main Authors: Silva‐Júnior, Neilier R., Cabrera, Yaremis M., Barbosa, Samuel L., Barros, Rafael de A., Barros, Edvaldo, Vital, Camilo E., Ramos, Humberto J. O., Oliveira, Maria Goreti A.
• Format: Journal Article
• Language: English
• Published: United States Wiley Subscription Services, Inc 01.07.2021
• Subjects: Anticarsia gemmatalis; Antigens; Binding sites; Control stability; Hydrolase; Insects; intestinal hydrolase; Intestine; Isoforms; LC/MS profile; Molecular docking; Pest control; Pest resistance; Pests; Protease; protease inhibitor; Protease inhibitors; Proteinase inhibitors; Proteolysis; Proteomes; proteomics; Soybeans; Trypsin; protease inhibitor; molecular docking; LC/MS profile; proteomics; pest control; intestinal hydrolase
• ISSN: 0739-4462; 1520-6327
• DOI: 10.1002/arch.21792

Although the importance of intestinal hydrolases is recognized, there is little information on the intestinal proteome of lepidopterans such as Anticarsia gemmatalis. Thus, we carried out the proteomic analysis of the A. gemmatalis intestine to characterize the proteases by LC/MS. We examined the interactions of proteins identified with protease inhibitors (PI) using molecular docking. We found 54 expressed antigens for intestinal protease, suggesting multiple important isoforms. The hydrolytic arsenal featured allows for a more comprehensive understanding of insect feeding. The docking analysis showed that the soybean PI (SKTI) could bind efficiently with the trypsin sequences and, therefore, insect resistance does not seem to involve changing the sequences of the PI binding site. In addition, a SERPIN was identified and the interaction analysis showed the inhibitor binding site is in contact with the catalytic site of trypsin, possibly acting as a regulator. In addition, this SERPIN and the identified PI sequences can be targets for the control of proteolytic activity in the caterpillar intestine and serve as a support for the rational design of a molecule with greater stability, less prone to cleavage by proteases and viable for the control of insect pests such as A. gemmatalis. Highlights Hydrolase profiling by LC/MS from the intestine of Anticarsia gemmatalis. Multiple isoforms identified specifically for trypsin‐like proteases. Docking analysis indicates that insect resistance does not involve modification of the PI binding sites. Identified SERPIN showed the highest affinity to the trypsin catalytic cavity.