Digestive proteolysis in the Colorado potato beetle, Leptinotarsa decemlineata: Activity-based profiling and imaging of a multipeptidase network

0467339 - ÚOCHB 2017 RIV GB eng J - Journal Article
Srp, Jaroslav - Nussbaumerová, Martina - Horn, Martin - Mareš, Michael
Digestive proteolysis in the Colorado potato beetle, Leptinotarsa decemlineata: Activity-based profiling and imaging of a multipeptidase network.
Insect Biochemistry and Molecular Biology. Roč. 78, Nov (2016), s. 1-11. ISSN 0965-1748. E-ISSN 1879-0240
R&D Projects: GA MŠMT LO1302; GA ČR GA15-18929S
Institutional support: RVO:61388963
Keywords : Colorado potato beetle * peptidase * cathepsin * activity-based probe * digestive system * multienzyme network
Subject RIV: CE - Biochemistry
Impact factor: 3.756, year: 2016

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.
Permanent Link: http://hdl.handle.net/11104/0265455