Sophie Vandermoten

Is the (E)-β-farnesene only volatile terpenoid in aphids?: (E)-β-farnesene: the only volatile terpenoid in aphids

Abstract:u2002 Herbivore insects use a broad range of chemical cues to locate their host to feed or to oviposit. Whether several plant volatiles are effective allelochemicals for insects, the latter also emit molecules which have infochemical role. The (E)‐β‐farnesene (EBF) is a well‐known aphid alarm pheromone commonly found in all previously tested species. Analysis of the released molecules from 23 aphid species, mainly collected on their natural host plant from May to July, was performed by gas chromatography–mass spectrometry. While EBF was identified as the main volatile substance in 16 species, alone or associated with other molecules, the alarm pheromone was only a minor component of the volatile molecule pattern of five other species. Moreover, two species, Euceraphis punctipennis and Drepanosiphum platanoides, did not release EBF at all but other terpenes were identified. This original observation raised the question on the utility and the source of the non‐EBF volatiles. Are these potential infochemical substances produced by the aphid or only absorbed from the host plant? Here we determined that terpenes released by insects were not only provided by the host plants. Indeed, Megoura viciae emitted additional molecules than the ones from several aphid species reared on the same host plant. Moreover, no systematic relation between the feeding behaviour of the aphid species and the volatile releases was observed. Aphid terpene composition and proportion would provide reliable cues to identify the emitting organism, plant or insect. The next step of this work will be to determine the infochemical role of terpenes found in the range of tested aphid samples to better understand the relations between the different tritrophic levels.

Aphid alarm pheromone: An overview of current knowledge on biosynthesis and functions

Aphids are important agricultural and forest pests that exhibit complex behaviors elicited by pheromonal signals. The aphid alarm pheromone--of which (E)-β-farnesene is the key (or only) component in most species--plays important roles in mediating interactions among individuals as well as multitrophic interactions among plants, aphids, and aphid natural enemies. Though many important questions remain to be answered, a large body of research has addressed various aspects of the biology, physiology, and ecology of aphid alarm pheromones. Here we review recent advances in our understanding of (a) the identity and composition of aphid alarm signals; (b) their biosynthesis and production; (c) their effects on conspecifics; (d) their role as cues for other insect species; and (e) their potential application for the management of pest organisms.

New insights into short-chain prenyltransferases: structural features, evolutionary history and potential for selective inhibition

Isoprenoids form an extensive group of natural products involved in a number of important biological processes. Their biosynthesis proceeds through sequential 1′-4 condensations of isopentenyl diphosphate (C5) with an allylic acceptor, the first of which is dimethylallyl diphosphate (C5). The reactions leading to the production of geranyl diphosphate (C10), farnesyl diphosphate (C15) and geranylgeranyl diphosphate (C20), which are the precursors of mono-, sesqui- and diterpenes, respectively, are catalyzed by a group of highly conserved enzymes known as short-chain isoprenyl diphosphate synthases, or prenyltransferases. In recent years, the sequences of many new prenyltransferases have become available, including those of several plant and animal geranyl diphosphate synthases, revealing novel mechanisms of product chain-length selectivity and an intricate evolutionary path from a putative common ancestor. Finally, there is considerable interest in designing inhibitors specific to short-chain prenyltransferases, for the purpose of developing new drugs or pesticides that target the isoprenoid biosynthetic pathway.

Characterization and tissue‐specific expression of two lepidopteran farnesyl diphosphate synthase homologs: Implications for the biosynthesis of ethyl‐substituted juvenile hormones

The sesquiterpenoid juvenile hormone (JH) regulates insect development and reproduction. Most insects produce only one chemical form of JH, but the Lepidoptera produce four derivatives featuring ethyl branches. The biogenesis of these JHs requires the synthesis of ethyl‐substituted farnesyl diphosphate (FPP) by FPP synthase (FPPS). To determine if there exist more than one lepidopteran FPPS, and whether one FPPS homolog is better adapted for binding the bulkier ethyl‐branched substrates/products, we cloned three lepidopteran FPPS cDNAs, two from Choristoneura fumiferana and one from Pseudaletia unipuncta. Amino acid sequence comparisons among these and other eukaryotic FPPSs led to the recognition of two lepidopteran FPPS types. Type‐I FPPSs display unique active site substitutions, including several in and near the first aspartate‐rich motif, whereas type‐II proteins have a more “conventional” catalytic cavity. In a yeast assay, a Drosophila FPPS clone provided full complementation of an FPPS mutation, but lepidopteran FPPS clones of either type yielded only partial complementation, suggesting unusual catalytic features and/or requirements of these enzymes. Although a structural analysis of lepidopteran FPPS active sites suggested that type‐I enzymes are better suited than type‐II for generating ethyl‐substituted products, a quantitative real‐time PCR assessment of their relative abundance in insect tissues indicated that type‐I expression is ubiquitous whereas that of type‐II is essentially confined to the JH‐producing glands, where its transcripts are ∼20 times more abundant than those of type‐I. These results suggest that type‐II FPPS plays a leading role in lepidopteran JH biosynthesis in spite of its apparently more conventional catalytic cavity. Proteins 2006.

Characterization of a novel aphid prenyltransferase displaying dual geranyl/farnesyl diphosphate synthase activity

We report on the cDNA cloning and characterization of a novel short‐chain isoprenyl diphosphate synthase from the aphid Myzus persicae. Of the three IPPS cDNAs we cloned, two yielded prenyltransferase activity following expression in Escherichia coli; these cDNAs encode identical proteins except for the presence, in one of them, of an N‐terminal mitochondrial targeting peptide. Although the aphid enzyme was predicted to be a farnesyl diphosphate synthase by BLASTP analysis, rMpIPPS, when isopentenyl diphosphate and dimethylallyl diphosphate are supplied as substrates, typically generated geranyl diphosphate (C10) as its main product, along with significant quantities of farnesyl diphosphate (C15). Analysis of an MpIPPS homology model pointed to substitutions that could confer GPP/FPP synthase activity to the aphid enzyme.

Structural features conferring dual Geranyl/Farnesyl diphosphate synthase activity to an aphid prenyltransferase

In addition to providing lipid chains for protein prenylation, short-chain isoprenyl diphosphate synthases (scIPPSs) play a pivotal role in the biosynthesis of numerous mevalonate pathway end-products, including insect juvenile hormone and terpenoid pheromones. For this reason, they are being considered as targets for pesticide development. Recently, we characterized an aphid scIPPS displaying dual geranyl diphosphate (GPP; C(10))/farnesyl diphosphate (FPP; C(15)) synthase activity in vitro. To identify the mechanism(s) responsible for this dual activity, we assessed the product selectivity of aphid scIPPSs bearing mutations at Gln107 and/or Leu110, the fourth and first residue upstream from the first aspartate-rich motif (FARM), respectively. All but one resulted in significant changes in product chain-length selectivity, effectively increasing the production of either GPP (Q107E, L110W) or FPP (Q107F, Q107F-L110A); the other mutation (L110A) abolished activity. Although some of these effects could be attributed to changes in steric hindrance within the catalytic cavity, molecular dynamics simulations identified other contributing factors, including residue-ligand Van der Waals interactions and the formation of hydrogen bonds or salt bridges between Gln107 and other residues across the catalytic cavity, which constitutes a novel product chain-length determination mechanism for scIPPSs. Thus the aphid enzyme apparently evolved to maintain the capacity to produce both GPP and FPP through a balance between these mechanisms.