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α-Amylase Mediates Host Acceptance in the Braconid Parasitoid Cotesia flavipes.

Journal of chemical ecology (2018-08-08)
Gladys Bichang'a, Jean-Luc Da Lage, Claire Capdevielle-Dulac, Michel Zivy, Thierry Balliau, Kevin Sambai, Bruno Le Ru, Laure Kaiser, Gerald Juma, Esther Njoki Mwangi Maina, Paul-André Calatayud
ZUSAMMENFASSUNG

Foraging parasitoids use chemical signals in host recognition and selection processes. Although, the volatiles play a relevant role in the localization by parasitoids of their hosts feeding on plants, the host identification process for acceptance occurs mainly during contact between the parasitoid and its host where host products related to feeding activities, fecal pellets and oral secretions, play a crucial role. The purpose of this study was to identify the nature of the contact kairomone(s) that mediate the acceptance for oviposition of the parasitoid Cotesia flavipes Cameron (Hymenoptera, Braconidae), which was released in Kenya in 1993 to control the invasive crambid Chilo partellus (Swinhoe). Using host and non-hosts of C. flavipes, we showed that it is mainly the oral secretions of the larvae that harbour the active compound(s) that mediate host acceptance for oviposition by C. flavipes. Using an integration of behavioral observations and biochemical approaches, the active compound of the oral secretions was identified as an α-amylase. Using synthetized α-amylases from Drosophila melanogaster (an insect model for which syntheses of active and inactive α-amylases are available), we observed that the conformation of the enzyme rather than its catalytic site as well as its substrate and its degradation product is responsible for host acceptance and oviposition mediation of C. flavipes females. The results suggest that the α-amylase from oral secretions of the caterpillar host is a good candidate for an evolutionary solution to host acceptance for oviposition in C. flavipes.

MATERIALIEN
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Produktbeschreibung

Sigma-Aldrich
α-Amylase aus Schweinepankreas, Type VI-B, ≥5 units/mg solid
Sigma-Aldrich
Proteinase K aus Tritirachium album, lyophilized powder, BioUltra, ≥30 units/mg protein, for molecular biology
Sigma-Aldrich
α-Amylase aus Aspergillus oryzae, ≥150 units/mg protein (biuret)
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Urease aus Canavalia ensiformis (Jack bean)
Sigma-Aldrich
Anti-Guinea Pig IgG (whole molecule)−Peroxidase antibody produced in goat, affinity isolated antibody, buffered aqueous solution
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α-Lactalbumin aus Kuhmilch, Marker for non-denaturing PAGE
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Albumin aus Rinderserum, dimer mol wt ~132 kDa