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Digestive proteolysis in the Colorado potato beetle, Leptinotarsa decemlineata: Activity-based profiling and imaging of a multipeptidase network
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SYSNO ASEP 0467339 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Digestive proteolysis in the Colorado potato beetle, Leptinotarsa decemlineata: Activity-based profiling and imaging of a multipeptidase network Author(s) Srp, Jaroslav (UOCHB-X) RID, ORCID
Nussbaumerová, Martina (UOCHB-X) RID
Horn, Martin (UOCHB-X) RID, ORCID
Mareš, Michael (UOCHB-X) RID, ORCIDSource Title Insect Biochemistry and Molecular Biology. - : Elsevier - ISSN 0965-1748
Roč. 78, Nov (2016), s. 1-11Number of pages 11 s. Language eng - English Country GB - United Kingdom Keywords Colorado potato beetle ; peptidase ; cathepsin ; activity-based probe ; digestive system ; multienzyme network Subject RIV CE - Biochemistry R&D Projects LO1302 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) GA15-18929S GA ČR - Czech Science Foundation (CSF) Institutional support UOCHB-X - RVO:61388963 UT WOS 000388053200001 EID SCOPUS 84983525917 DOI 10.1016/j.ibmb.2016.08.004 Annotation The Colorado potato beetle (CPB), Leptinotarsa decemlineata, is a major pest of potato plants, and its digestive system is a promising target for development of pest control strategies. This work focuses on functional proteomic analysis of the digestive proteolytic enzymes expressed in the CPB gut. We identified a set of peptidases using imaging with specific activity-based probes and activity profiling with selective substrates and inhibitors. The secreted luminal peptidases were classified as: (i) endopeptidases of cathepsin D, cathepsin L, and trypsin types and (ii) exopeptidases with aminopeptidase (cathepsin H), carboxypeptidase (serine carboxypeptidase, prolyl carboxypeptidase), and carboxydipeptidase (cathepsin B) activities. The proteolytic arsenal also includes non-luminal peptidases with prolyl oligopeptidase and metalloaminopeptidase activities. Our results indicate that the CPB gut employs a multienzyme network of peptidases with complementary specificities to efficiently degrade ingested proteins. This proteolytic system functions in both CPB larvae and adults and is controlled mainly by cysteine and aspartic peptidases and supported by serine and metallopeptidases. The component enzymes identified here are potential targets for inhibitors with tailored specificities that could be engineered into potato plants to confer resistance to CPB. Workplace Institute of Organic Chemistry and Biochemistry Contact asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Jana Procházková, Tel.: 220 183 418 Year of Publishing 2017
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