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Insects 2017, 8(2), 62; doi:10.3390/insects8020062

β-Cyanoalanine Synthases and Their Possible Role in Pierid Host Plant Adaptation

Institute of Pharmaceutical Biology, Technische Universität Braunschweig, Mendelssohnstrasse 1, D-38106 Braunschweig, Germany
This manuscript is dedicated to the memory of Professor Thomas Hartmann (Institute of Pharmaceutical Biology, Technische Universität Braunschweig, Braunschweig, Germany).
Present address: SeSaM-Biotech GmbH, Forckenbeckstraße 50, D-52056 Aachen, Germany.
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Author to whom correspondence should be addressed.
Academic Editor: Paul A. Weston
Received: 2 May 2017 / Revised: 5 June 2017 / Accepted: 14 June 2017 / Published: 18 June 2017
(This article belongs to the Special Issue Insect-Plant Interactions)
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Abstract

Cyanide is generated in larvae of the glucosinolate-specialist Pieris rapae (Lepidoptera:Pieridae) upon ingestion of plant material containing phenylalanine-derived glucosinolates as chemical defenses. As these glucosinolates were widespread within ancient Brassicales, the ability to detoxify cyanide may therefore have been essential for the host plant shift of Pierid species from Fabales to Brassicales species giving rise to the Pierinae subfamily. Previous research identified β-cyanoalanine and thiocyanate as products of cyanide detoxification in P. rapae larvae as well as three cDNAs encoding the β-cyanoalanine synthases PrBSAS1-PrBSAS3. Here, we analyzed a total of eight species of four lepidopteran families to test if their cyanide detoxification capacity correlates with their feeding specialization. We detected β-cyanoalanine synthase activity in gut protein extracts of all six species tested, which included Pierid species with glucosinolate-containing host plants, Pierids with other hosts, and other Lepidoptera with varying food specialization. Rhodanese activity was only scarcely detectable with the highest levels appearing in the two glucosinolate-feeding Pierids. We then amplified by polymerase chain reaction (PCR) 14 cDNAs encoding β-cyanoalanine synthases from seven species. Enzyme characterization and phylogenetic analysis indicated that lepidopterans are generally equipped with one PrBSAS2 homolog with high affinity for cyanide. A second β-cyanoalanine synthase which grouped with PrBSAS3 was restricted to Pierid species, while a third variant (i.e., homologs of PrBSAS1), was only present in members of the Pierinae subfamily. These results are in agreement with the hypothesis that the host shift to Brassicales was associated with the requirement for a specialized cyanide detoxification machinery. View Full-Text
Keywords: glucosinolates; cyanide detoxification; Pieridae; β-cyanoalanine synthase; coevolution glucosinolates; cyanide detoxification; Pieridae; β-cyanoalanine synthase; coevolution
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Herfurth, A.-M.; Ohlen, M.V.; Wittstock, U. β-Cyanoalanine Synthases and Their Possible Role in Pierid Host Plant Adaptation. Insects 2017, 8, 62.

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