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Aphid BCR4 Structure and Activity Uncover a New Defensin Peptide Superfamily
Aphids (Hemiptera: Aphidoidea) are among the most detrimental insects for agricultural plants, and their management is a great challenge in agronomical research. A new class of proteins, called Bacteriocyte-specific Cysteine-Rich (BCR) peptides, provides an alternative to chemical insecticides for p...
Autores principales: | , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9604261/ https://www.ncbi.nlm.nih.gov/pubmed/36293341 http://dx.doi.org/10.3390/ijms232012480 |
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author | Loth, Karine Parisot, Nicolas Paquet, Françoise Terrasson, Hugo Sivignon, Catherine Rahioui, Isabelle Ribeiro Lopes, Mélanie Gaget, Karen Duport, Gabrielle Delmas, Agnès F. Aucagne, Vincent Heddi, Abdelaziz Calevro, Federica da Silva, Pedro |
author_facet | Loth, Karine Parisot, Nicolas Paquet, Françoise Terrasson, Hugo Sivignon, Catherine Rahioui, Isabelle Ribeiro Lopes, Mélanie Gaget, Karen Duport, Gabrielle Delmas, Agnès F. Aucagne, Vincent Heddi, Abdelaziz Calevro, Federica da Silva, Pedro |
author_sort | Loth, Karine |
collection | PubMed |
description | Aphids (Hemiptera: Aphidoidea) are among the most detrimental insects for agricultural plants, and their management is a great challenge in agronomical research. A new class of proteins, called Bacteriocyte-specific Cysteine-Rich (BCR) peptides, provides an alternative to chemical insecticides for pest control. BCRs were initially identified in the pea aphid Acyrthosiphon pisum. They are small disulfide bond-rich proteins expressed exclusively in aphid bacteriocytes, the insect cells that host intracellular symbiotic bacteria. Here, we show that one of the A. pisum BCRs, BCR4, displays prominent insecticidal activity against the pea aphid, impairing insect survival and nymphal growth, providing evidence for its potential use as a new biopesticide. Our comparative genomics and phylogenetic analyses indicate that BCRs are restricted to the aphid lineage. The 3D structure of BCR4 reveals that this peptide belongs to an as-yet-unknown structural class of peptides and defines a new superfamily of defensins. |
format | Online Article Text |
id | pubmed-9604261 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-96042612022-10-27 Aphid BCR4 Structure and Activity Uncover a New Defensin Peptide Superfamily Loth, Karine Parisot, Nicolas Paquet, Françoise Terrasson, Hugo Sivignon, Catherine Rahioui, Isabelle Ribeiro Lopes, Mélanie Gaget, Karen Duport, Gabrielle Delmas, Agnès F. Aucagne, Vincent Heddi, Abdelaziz Calevro, Federica da Silva, Pedro Int J Mol Sci Article Aphids (Hemiptera: Aphidoidea) are among the most detrimental insects for agricultural plants, and their management is a great challenge in agronomical research. A new class of proteins, called Bacteriocyte-specific Cysteine-Rich (BCR) peptides, provides an alternative to chemical insecticides for pest control. BCRs were initially identified in the pea aphid Acyrthosiphon pisum. They are small disulfide bond-rich proteins expressed exclusively in aphid bacteriocytes, the insect cells that host intracellular symbiotic bacteria. Here, we show that one of the A. pisum BCRs, BCR4, displays prominent insecticidal activity against the pea aphid, impairing insect survival and nymphal growth, providing evidence for its potential use as a new biopesticide. Our comparative genomics and phylogenetic analyses indicate that BCRs are restricted to the aphid lineage. The 3D structure of BCR4 reveals that this peptide belongs to an as-yet-unknown structural class of peptides and defines a new superfamily of defensins. MDPI 2022-10-18 /pmc/articles/PMC9604261/ /pubmed/36293341 http://dx.doi.org/10.3390/ijms232012480 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Loth, Karine Parisot, Nicolas Paquet, Françoise Terrasson, Hugo Sivignon, Catherine Rahioui, Isabelle Ribeiro Lopes, Mélanie Gaget, Karen Duport, Gabrielle Delmas, Agnès F. Aucagne, Vincent Heddi, Abdelaziz Calevro, Federica da Silva, Pedro Aphid BCR4 Structure and Activity Uncover a New Defensin Peptide Superfamily |
title | Aphid BCR4 Structure and Activity Uncover a New Defensin Peptide Superfamily |
title_full | Aphid BCR4 Structure and Activity Uncover a New Defensin Peptide Superfamily |
title_fullStr | Aphid BCR4 Structure and Activity Uncover a New Defensin Peptide Superfamily |
title_full_unstemmed | Aphid BCR4 Structure and Activity Uncover a New Defensin Peptide Superfamily |
title_short | Aphid BCR4 Structure and Activity Uncover a New Defensin Peptide Superfamily |
title_sort | aphid bcr4 structure and activity uncover a new defensin peptide superfamily |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9604261/ https://www.ncbi.nlm.nih.gov/pubmed/36293341 http://dx.doi.org/10.3390/ijms232012480 |
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