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...
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| Veröffentlicht in: | International journal of molecular sciences 2022-10, Vol.23 (20), p.12480 |
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| creator | 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 |
| 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. |
| doi_str_mv | 10.3390/ijms232012480 |
| format | Article |
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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.</description><identifier>ISSN: 1422-0067</identifier><identifier>ISSN: 1661-6596</identifier><identifier>EISSN: 1422-0067</identifier><identifier>DOI: 10.3390/ijms232012480</identifier><identifier>PMID: 36293341</identifier><language>eng</language><publisher>Basel: MDPI AG</publisher><subject>Acyrthosiphon pisum ; Amino acids ; Antimicrobial agents ; Biochemistry, Molecular Biology ; Chemical bonds ; Chemical Sciences ; Defensins ; E coli ; Genes ; Insect cells ; Insects ; Life Sciences ; Peas ; Peptides ; Pest control ; Phylogenetics ; Phylogeny ; Proteins</subject><ispartof>International journal of molecular sciences, 2022-10, Vol.23 (20), p.12480</ispartof><rights>2022 by the authors. Licensee MDPI, Basel, Switzerland. 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| source | MDPI - Multidisciplinary Digital Publishing Institute; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
| subjects | Acyrthosiphon pisum Amino acids Antimicrobial agents Biochemistry, Molecular Biology Chemical bonds Chemical Sciences Defensins E coli Genes Insect cells Insects Life Sciences Peas Peptides Pest control Phylogenetics Phylogeny Proteins |
| title | Aphid BCR4 Structure and Activity Uncover a New Defensin Peptide Superfamily |
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