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

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
摘要

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.

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Sigma-Aldrich
α-淀粉酶 来源于猪胰腺, Type VI-B, ≥5 units/mg solid
Sigma-Aldrich
α-淀粉酶 来源于米曲霉, ≥150 units/mg protein (biuret)
Sigma-Aldrich
蛋白酶 K 来源于林伯氏白色念球菌, lyophilized powder, BioUltra, ≥30 units/mg protein, for molecular biology
Sigma-Aldrich
尿素酶 来源于洋刀豆 (刀豆)
Sigma-Aldrich
抗-豚鼠IgG(全分子)−过氧化物酶 山羊抗, affinity isolated antibody, buffered aqueous solution
Sigma-Aldrich
α-乳清蛋白 来源于牛奶, Marker for non-denaturing PAGE
Sigma-Aldrich
牛血清白蛋白 来源于牛血清, dimer mol wt ~132 kDa