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Plant Ureases and Related Peptides: Understanding Their Entomotoxic Properties
Recently, ureases were included in the arsenal of plant defense proteins, alongside many other proteins with biotechnological potential such as insecticides. Isoforms of Canavalia ensiformis urease (canatoxin—CNTX and jack bean urease—JBURE-I) are toxic to insects of different orders. This toxicity...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3317107/ https://www.ncbi.nlm.nih.gov/pubmed/22474566 http://dx.doi.org/10.3390/toxins4020055 |
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author | Stanisçuaski, Fernanda Carlini, Célia R. |
author_facet | Stanisçuaski, Fernanda Carlini, Célia R. |
author_sort | Stanisçuaski, Fernanda |
collection | PubMed |
description | Recently, ureases were included in the arsenal of plant defense proteins, alongside many other proteins with biotechnological potential such as insecticides. Isoforms of Canavalia ensiformis urease (canatoxin—CNTX and jack bean urease—JBURE-I) are toxic to insects of different orders. This toxicity is due in part to the release of a 10 kDa peptide from the native protein, by cathepsin-like enzymes present in the insect digestive tract. The entomotoxic peptide, Jaburetox-2Ec, exhibits potent insecticidal activity against several insects, including many resistant to the native ureases. JBURE-I and Jaburetox-2Ec cause major alterations of post-feeding physiological processes in insects, which contribute to, or can be the cause of, their entomotoxic effect. An overview of the current knowledge on plant urease processing and mechanisms of action in insects is presented in this review. |
format | Online Article Text |
id | pubmed-3317107 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-33171072012-04-03 Plant Ureases and Related Peptides: Understanding Their Entomotoxic Properties Stanisçuaski, Fernanda Carlini, Célia R. Toxins (Basel) Review Recently, ureases were included in the arsenal of plant defense proteins, alongside many other proteins with biotechnological potential such as insecticides. Isoforms of Canavalia ensiformis urease (canatoxin—CNTX and jack bean urease—JBURE-I) are toxic to insects of different orders. This toxicity is due in part to the release of a 10 kDa peptide from the native protein, by cathepsin-like enzymes present in the insect digestive tract. The entomotoxic peptide, Jaburetox-2Ec, exhibits potent insecticidal activity against several insects, including many resistant to the native ureases. JBURE-I and Jaburetox-2Ec cause major alterations of post-feeding physiological processes in insects, which contribute to, or can be the cause of, their entomotoxic effect. An overview of the current knowledge on plant urease processing and mechanisms of action in insects is presented in this review. MDPI 2012-02-01 /pmc/articles/PMC3317107/ /pubmed/22474566 http://dx.doi.org/10.3390/toxins4020055 Text en © 2012 by the authors; licensee MDPI, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0/ This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Review Stanisçuaski, Fernanda Carlini, Célia R. Plant Ureases and Related Peptides: Understanding Their Entomotoxic Properties |
title | Plant Ureases and Related Peptides: Understanding Their Entomotoxic Properties |
title_full | Plant Ureases and Related Peptides: Understanding Their Entomotoxic Properties |
title_fullStr | Plant Ureases and Related Peptides: Understanding Their Entomotoxic Properties |
title_full_unstemmed | Plant Ureases and Related Peptides: Understanding Their Entomotoxic Properties |
title_short | Plant Ureases and Related Peptides: Understanding Their Entomotoxic Properties |
title_sort | plant ureases and related peptides: understanding their entomotoxic properties |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3317107/ https://www.ncbi.nlm.nih.gov/pubmed/22474566 http://dx.doi.org/10.3390/toxins4020055 |
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