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

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F16%3A00467339" target="_blank" >RIV/61388963:_____/16:00467339 - isvavai.cz</a>

Alternative codes found

RIV/00216208:11310/16:10326057

Result on the web

<a href="http://dx.doi.org/10.1016/j.ibmb.2016.08.004" target="_blank" >http://dx.doi.org/10.1016/j.ibmb.2016.08.004</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.ibmb.2016.08.004" target="_blank" >10.1016/j.ibmb.2016.08.004</a>

Result language

angličtina

Original language name

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

Original language description

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.

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CE - Biochemistry

OECD FORD branch

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Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2016

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Insect Biochemistry and Molecular Biology

ISSN

0965-1748

e-ISSN

—

Volume of the periodical

78

Issue of the periodical within the volume

Nov

Country of publishing house

GB - UNITED KINGDOM

Number of pages

11

Pages from-to

1-11

UT code for WoS article

000388053200001

EID of the result in the Scopus database

2-s2.0-84983525917