ArticleJournal of chemical ecology2018
α-Amylase Mediates Host Acceptance in the Braconid Parasitoid Cotesia flavipes.
Article in Journal of chemical ecology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 10 citations in OpenAlex.
- Eavesdropping Kairomone Markers of Interspecific Communication in Predatory and Parasitic Arthropods: A Review.Journal of chemical ecology · 2026Review
- Insect α-Amylases and Their Application in Pest Management.Molecules (Basel, Switzerland) · 2023Review
- Chromosomal scale assembly of parasitic wasp genome reveals symbiotic virus colonization.Communications biology · 2021Article
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
Abstract
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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