The Use of Imaging Mass Spectrometry to Study Peptide Toxin Distribution in Australian Sea Anemones

Mitchell, Michela L.; Hamilton, Brett; Madio, Bruno; Morales, Rodrigo A.V.; Tonkin‐Hill, Gerry; Papenfuss, Anthony T.; Purcell, Anthony W.; King, Glenn F.; Undheim, Eivind A. B.; Norton, Raymond S.

doi:10.1071/ch17228

Cited by 23 publications

(24 citation statements)

References 14 publications

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“…To localize specific toxin peptides to morphological structures, we used MSI. Mass spectrometry imaging was guided by published protocols (Caprioli, Farmer, & Gile, ) but with sample preparation optimized as recently described (Madio et al, ; Mitchell et al, ; Undheim, Sunagar, et al, ). Briefly, specimens of A. tenebrosa were left in 50% RCL2/ethanol at room temperature overnight, then dehydrated sequentially using 50%, 60%, 70%, 90%, 95% and 100% ethanol (3 x 15 min at each concentration), cleared in xylene for 30 min and embedded in paraffin wax.…”

Section: Methodsmentioning

confidence: 99%

A process of convergent amplification and tissue‐specific expression dominates the evolution of toxin and toxin‐like genes in sea anemones

et al. 2019

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Members of phylum Cnidaria are an ancient group of venomous animals and rely on a number of specialized tissues to produce toxins in order to fulfil a range of ecological roles including prey capture, defence against predators, digestion and aggressive encounters. However, limited comprehensive analyses of the evolution and expression of toxin genes currently exist for cnidarian species. In this study, we use genomic and transcriptomic sequencing data to examine gene copy number variation and selective pressure on toxin gene families in phylum Cnidaria. Additionally, we use quantitative RNA-seq and mass spectrometry imaging to understand expression patterns and tissue localization of toxin production in sea anemones. Using genomic data, we demonstrate that the first large-scale expansion and diversification of known toxin genes occurs in phylum Cnidaria, a process we also observe in other venomous lineages, which we refer to as convergent amplification. Our analyses of selective pressure on sea anemone toxin gene families reveal that purifying selection is the dominant mode of evolution for these genes and that phylogenetic inertia is an important determinant of toxin gene complement in this group. The gene expression and tissue localization data revealed that specific genes and proteins from toxin gene families show strong patterns of tissue and developmental-phase specificity in sea anemones. Overall, convergent amplification and phylogenetic inertia have strongly influenced the distribution and evolution of the toxin complement observed in sea

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Section: Methodsmentioning

confidence: 99%

A process of convergent amplification and tissue‐specific expression dominates the evolution of toxin and toxin‐like genes in sea anemones

et al. 2019

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“…Therefore, MSI offers the opportunity to analyse peptide mixtures and evaluate peptide localisation for any species. This approach has been applied to the imaging of venom toxins from sea anemones, snakes and centipedes to date [16,25,[140][141][142][143][144]. Identification of venom components directly from MSI spectra, however, remains non-trivial.…”

Section: Characterising Toxin Expression Patternsmentioning

confidence: 99%

Characterising Functional Venom Profiles of Anthozoans and Medusozoans within Their Ecological Context

et al. 2020

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This review examines the current state of knowledge regarding toxins from anthozoans (sea anemones, coral, zoanthids, corallimorphs, sea pens and tube anemones). We provide an overview of venom from phylum Cnidaria and review the diversity of venom composition between the two major clades (Medusozoa and Anthozoa). We highlight that the functional and ecological context of venom has implications for the temporal and spatial expression of protein and peptide toxins within class Anthozoa. Understanding the nuances in the regulation of venom arsenals has been made possible by recent advances in analytical technologies that allow characterisation of the spatial distributions of toxins. Furthermore, anthozoans are unique in that ecological roles can be assigned using tissue expression data, thereby circumventing some of the challenges related to pharmacological screening.

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“…While there are a number of different modes for ionization during MSI, the observation of peptides and proteins is best achieved using MALDI. MSI has been used to locate venom components in the glandular tissues of centipedes, [164] cnidarians, [55,165] ants, [166] spiders, [167] and snakes. [168] Two studies have also used MSI to examine the distribution of honeybee venom toxins and antigens in tissues of mammalian tissue after injection with venom.…”

Section: Mass Spectrometry Imaging: Where Is Venom Coming From and Whmentioning

confidence: 99%

Deadly Proteomes: A Practical Guide to Proteotranscriptomics of Animal Venoms

et al. 2020

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Animal venoms are renowned for their toxicity, biochemical complexity, and as a source of compounds with potential applications in medicine, agriculture, and industry. Polypeptides underlie much of the pharmacology of animal venoms, and elucidating these arsenals of polypeptide toxins—known as the venom proteome or venome—is an important step in venom research. Proteomics is used for the identification of venom toxins, determination of their primary structure including post‐translational modifications, as well as investigations into the physiology underlying their production and delivery. Advances in proteomics and adjacent technologies has led to a recent upsurge in publications reporting venom proteomes. Improved mass spectrometers, better proteomic workflows, and the integration of next‐generation sequencing of venom‐gland transcriptomes and venomous animal genomes allow quicker and more accurate profiling of venom proteomes with greatly reduced starting material. Technologies such as imaging mass spectrometry are revealing additional insights into the mechanism, location, and kinetics of venom toxin production. However, these numerous new developments may be overwhelming for researchers designing venom proteome studies. Here, the field of venom proteomics is reviewed and some practical solutions for simplifying mass spectrometry workflows to study animal venoms are offered.

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The Use of Imaging Mass Spectrometry to Study Peptide Toxin Distribution in Australian Sea Anemones

Cited by 23 publications

References 14 publications

A process of convergent amplification and tissue‐specific expression dominates the evolution of toxin and toxin‐like genes in sea anemones

A process of convergent amplification and tissue‐specific expression dominates the evolution of toxin and toxin‐like genes in sea anemones

Characterising Functional Venom Profiles of Anthozoans and Medusozoans within Their Ecological Context

Deadly Proteomes: A Practical Guide to Proteotranscriptomics of Animal Venoms

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