Dataset Information

Multiple Evolutionary Mechanisms Underlie the Venom Composition of the Green Lacewing

ABSTRACT: Venom has independently evolved across many lineages, yet relatively few have been studied in detail, particularly among insects. Of these, Neuroptera (lacewings, antlions and relatives) remain largely unexplored, despite being widespread with agriculturally important groups such as green lacewings. While adults are non-venomous, neuropteran larvae are ferocious predators that use pincer-like mouthparts to inject paralysing and liquefying venom to subdue and consume their prey. Here, we provide a comprehensive investigation of the venom system in Neuroptera by integrating a high-quality genome, long-read transcriptomes spanning all life stages, microCT-reconstruction of venom glands, tissue-specific expression analyses, venom proteomics, and functional assays of the common green lacewing Chrysoperla carnea. We provide a re-description of the neuropteran venom system, demonstrate the venom’s insecticidal and cytotoxic activity, and show the venom comprises diverse toxin gene families and is richer and more similar to the venom of antlions than previously proposed. We show that this toxin arsenal is the result of a multitude of evolutionary events that include co-option, recruitment following gene duplication, diversification of toxin-paralogs by gene duplication, and functional innovation of new paralogs through both small structural and large architectural changes. In addition, we find that alternative splicing of toxin genes is an important contributor to the biochemical arsenal, which is a mechanism rarely documented among venomous animals. Our results demonstrate how multiple genomic and evolutionary mechanisms together contribute to the emergence and evolution of a complex molecular trait, and provide new insights into the evolution of venom in insects.

INSTRUMENT(S):

ORGANISM(S): Chrysoperla Carnea

TISSUE(S): Venom

SUBMITTER: Marius Maurstad

LAB HEAD: Eivind Andreas Baste Undheim

PROVIDER: PXD070278 | Pride | 2026-01-12

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	CJK_201120_Eivind_AT_Cc1.raw	Raw
	CJK_201120_Eivind_AT_Cc2.raw	Raw
	CJK_201120_Eivind_AT_Cc3.raw	Raw
	CJK_201120_Eivind_A_Cc1.raw	Raw
	CJK_201120_Eivind_A_Cc2.raw	Raw

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Publications

The green lacewing venom system and the complex mechanisms underlying its evolution.

Maurstad Marius F MF Ramiro Iris Bea L IBL Oeyen Jan Philip JP Sombke Andy A Büsse Sebastian S Nachtigall Pedro G PG Jakobsen Kjetill S KS Undheim Eivind A B EAB

Molecular biology and evolution 20260101 1

Venom has independently evolved across many lineages, yet relatively few have been studied in detail, particularly among insects. Of these, Neuroptera (lacewings, antlions, and relatives) remain largely unexplored, despite being widespread with agriculturally important groups such as green lacewings. While adults are nonvenomous, neuropteran larvae are ferocious predators that use pincer-like mouthparts to inject paralyzing and liquefying venom to subdue and consume their prey. Here, we provide ...[more]

PMID: 41381409

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Project description:Elucidating the molecular mechanisms underlying snake venom variability provides important clues for understanding how the biological functions of this powerful toxic arsenal evolve. We analyzed in detail individual transcripts and venom protein isoforms produced by five specimens of a venomous snake (Bothrops atrox) from two nearby but genetically distinct populations from the Brazilian Amazon rainforest which show functional similarities in venom properties. Individual variation was observed among the venoms of these specimens, but the overall abundance of each general toxin family was conserved both in transcript and in venom protein levels. However, when expression of independent paralogues was analyzed, remarkable differences were observed within and among each toxin group, both between individuals and between populations. Transcripts for functionally essential venom proteins (“core function” proteins) were highly expressed in all specimens and showed similar transcription/translation rates. In contrast, other paralogues (“adaptive” proteins) showed lower expression levels and the toxins they coded for varied among different individuals. These results provide support for the inferences that (a) expression and translational differences play a greater role in defining adaptive variation in venom phenotypes than does sequence variation in protein coding genes and (b) convergent adaptive venom phenotypes can be generated through different molecular mechanisms. Significance: Analysis of individual transcripts and venom protein isoforms produced by specimens of a venomous snake (Bothrops atrox), from the Brazilian Amazon rainforest, revealed that transcriptional and translational mechanisms contribute to venom phenotypic variation. Our finding of evidence for high expression of toxin proteins with conserved function supports the hypothesis that the venom phenotype consists of two kinds of proteins: conserved “core function” proteins that provide essential functional activities with broader relevance and less conserved “adaptive” proteins that vary in expression and may permit customization of protein function. These observations allowed us to suggest that genetic mechanisms controlling venom variability are not restricted to selection of gene copies or mutations in structural genes but also to selection of the mechanisms controlling gene expression, contributing to the plasticity of this important phenotype for venomous snakes.