Digestive proteolysis in the Colorado potato beetle, Leptinotarsa decemlineata: Activity-based profiling and imaging of a multipeptidase network
Language English Country Great Britain, England Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
27539253
DOI
10.1016/j.ibmb.2016.08.004
PII: S0965-1748(16)30114-X
Knihovny.cz E-resources
- Keywords
- Activity-based probe, Cathepsin, Colorado potato beetle, Digestive system, Multienzyme network, Peptidase,
- MeSH
- Coleoptera enzymology genetics growth & development metabolism MeSH
- Animal Nutritional Physiological Phenomena MeSH
- Gastrointestinal Tract enzymology MeSH
- Insect Proteins genetics metabolism MeSH
- Larva genetics growth & development metabolism MeSH
- Peptide Hydrolases genetics metabolism MeSH
- Proteolysis MeSH
- Proteomics MeSH
- Plant Proteins metabolism MeSH
- Digestion MeSH
- Animals MeSH
- Check Tag
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Insect Proteins MeSH
- Peptide Hydrolases MeSH
- Plant Proteins MeSH
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.
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