RT Journal Article
SR Electronic
T1 The aphid BCR4 structure and activity uncover a new defensin peptide superfamily
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2021.12.17.472939
DO 10.1101/2021.12.17.472939
A1 Karine Loth
A1 Nicolas Parisot
A1 Françoise Paquet
A1 Catherine Sivignon
A1 Isabelle Rahioui
A1 Mélanie Ribeiro Lopes
A1 Karen Gaget
A1 Gabrielle Duport
A1 Agnès F. Delmas
A1 Vincent Aucagne
A1 Abdelaziz Heddi
A1 Federica Calevro
A1 Pedro da Silva
YR 2021
UL http://biorxiv.org/content/early/2021/12/17/2021.12.17.472939.abstract
AB Aphids (Hemiptera: Aphidoidea) are among the most injuring 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), provides an alternative to chemical insecticides for pest control. BCRs have been initially identified in the pea aphid Acyrthosiphon pisum. They are small disulfide bond-rich proteins expressed exclusively in aphid bacteriocytes, the insect derived cells that host intracellular symbiotic bacteria. Here, we show that one out of the A. pisum BCRs, BCR4, displays an outstanding insecticidal activity against the pea aphid, impairing insect survival and nymphal growth, providing evidence for its potential use as a new biopesticides. Our comparative genomics and phylogenetic analysis indicate that BCRs seem restricted to the aphid lineage. The 3D structure of the BCR4 reveals that this peptide belongs to a yet unknown structural class of peptides and defines a new superfamily of defensins.Competing Interest StatementThe authors have declared no competing interest.