The Acrolepiopsis assectella silk cocoon: kairomonal function and chemical characterisation.
Two soluble sericin-like polypeptides, B1 and B2, from leek moth (Acrolepiopsis assectella) cocoons trigger host-acceptance behaviour in the parasitoid, Diadromus pulchellus (Proc. Roy. Soc. London B 269 (2002) 1879). We found that these polypeptides were particularly cysteine-rich and lost their ability to trigger host-acceptance behaviour after being denatured and purified. This suggests that inter-disulphide bonds and the secondary structure of B1 and B2 are important for their biological activity. We also isolated six insoluble polypeptides (or polypeptides of low solubility) from A. assectella cocoons. At least four of these polypeptides triggered host-acceptance behaviour. The strongest responses were observed with P22, a light-chain fibroin or a seroin-peptide, and P100, a sericin-like polypeptide that is probably more strongly associated with the silk core than are B1 and B2. In conclusion, several polypeptides from different parts of the A. assectella silk-cocoon (the insoluble core and coating of the silk thread) are able to elicit host-acceptance behaviour in D. pulchellus females. These polypeptides belong to different silk protein families and are used as kairomones by this specialist parasitoid.
Gauthier
N
N
Centre de Biologie et de Gestion des Populations, IRD-UMR, Campus international de Baillarguet, CS 30016, 34988 Montferrier sur Lez, France. nathalie.gauthier@mpl.ird.fr
Mandon
N
N
Renault
S
S
Bénédet
F
F
D000818:Animals; D005260:Female; D006927:Hymenoptera / Q000502:physiology*; D007915:Lepidoptera / Q000469:parasitology* / Q000502:physiology*; D008970:Molecular Weight; D011489:Protein Denaturation; D017433:Protein Structure, Secondary; D047011:Silk / Q000737:chemistry* / Q000502:physiology*
D047011:Silk