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Proteomics of the venom from Apis mellifera

ABSTRACT: Venoms have convergently evolved in all major animal lineages and are ideal candidates to unravel the underlying genomic processes of convergent trait evolution. However, few animal groups have been studied in detail, and large-scale comparative genomic analyses to address toxin gene evolution are rare. Hyper-diverse hymenopterans are the most speciose group of venomous animals, but the origin of their toxin genes have been largely overlooked. We combined proteo-transcriptomics with comparative genomics compiling an up-to-date list of core bee venom proteins to investigate the origin of 11 venom genes in 30 hymenopteran genomes including two new stingless bees.

INSTRUMENT(S): Q Exactive HF-X

ORGANISM(S): Apis Mellifera (honeybee)

TISSUE(S): Venom Gland

SUBMITTER: Günter Lochnit

LAB HEAD: Sebastien Dutertre

PROVIDER: PXD029934 | Pride | 2023-09-28

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	VENOMICS_191203_HFX_Apimel104.mgf	Mgf
	VENOMICS_191203_HFX_Apimel104.raw	Raw
	de_novo_only_peptides.csv	Csv
	de_novo_only_spectra.mgf	Mgf
	peptides.pep.xml	Pepxml

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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.

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Proteomics of the venom from Apis mellifera

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