The aphid BCR4 structure and activity uncover a new defensin peptide superfamily

Loth, K.; Parisot, N.; Paquet, F.; Sivignon, C.; Rahioui, I.; Lopes, M. R.; Gaget, K.; Duport, G.; Delmas, A. F.; Aucagne, V.; Heddi, A.; Calevro, F.; da Silva, P.

doi:10.1101/2021.12.17.472939

bioRxiv · 10.1101/2021.12.17.472939

The aphid BCR4 structure and activity uncover a new defensin peptide superfamily

Loth, K.·Parisot, N.·Paquet, F.·Sivignon, C.·Rahioui, I.·Lopes, M. R.·Gaget, K.·Duport, G.·Delmas, A. F.·Aucagne, V.·Heddi, A.·Calevro, F.·da Silva, P.

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Abstract

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.

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Loth, K., Parisot, N., Paquet, F., Sivignon, C., Rahioui, I., Lopes, M. R., Gaget, K., Duport, G., Delmas, A. F., Aucagne, V., Heddi, A., Calevro, F., da Silva, P.. 2021-12-17. The aphid BCR4 structure and activity uncover a new defensin peptide superfamily. https://doi.org/10.1101/2021.12.17.472939

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