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Antarctonemertes valida venomics

ABSTRACT: Investigation into nemertean venoms and their evolution

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Antarctonemertes Valida

TISSUE(S): Proboscis

SUBMITTER: Eivind Undheim

LAB HEAD: Eivind A. B. Undheim

PROVIDER: PXD033380 | Pride | 2022-05-30

REPOSITORIES: Pride

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			Action	DRS
	20191202_A_valida_LMD_proboscis_IAA_tryp.group	Other
	20191202_A_valida_LMD_proboscis_IAA_tryp.mgf	Mgf
	20191202_A_valida_LMD_proboscis_IAA_tryp.wiff	Wiff
	20191202_A_valida_LMD_proboscis_IAA_tryp.wiff.scan	Wiff
	20191202_A_valida_LMD_proboscis_IAA_tryp__FDR.xlsx	Xlsx

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1 - 5 of 11

Publications

Evolution, Expression Patterns, and Distribution of Novel Ribbon Worm Predatory and Defensive Toxins.

Verdes Aida A Taboada Sergi S Hamilton Brett R BR Undheim Eivind A B EAB Sonoda Gabriel G GG Andrade Sonia C S SCS Morato Esperanza E Marina Ana Isabel AI Cárdenas César A CA Riesgo Ana A

Molecular biology and evolution 20220501 5

Ribbon worms are active predators that use an eversible proboscis to inject venom into their prey and defend themselves with toxic epidermal secretions. Previous work on nemertean venom has largely focused on just a few species and has not investigated the different predatory and defensive secretions in detail. Consequently, our understanding of the composition and evolution of ribbon worm venoms is still very limited. Here, we present a comparative study of nemertean venom combining RNA-seq dif ...[more]

PMID: 35512366

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Toxins from scratch? - Diverse, multimodal gene origins in the predatory robber fly Dasypogon diadema indicate dynamic venom evolution in dipteran insects

Project description:Venoms and the toxins they contain represent molecular adaptations that have evolved on numerous occasions throughout the animal kingdom. However, the processes that shape venom protein evolution are poorly understood because of the scarcity of whole genome data available for comparative analyses of venomous species. Here, we perform a broad comparative toxicogenomic analysis to gain insight into the genomic mechanisms of venom evolution in robber flies (Asilidae). We first sequenced a high-quality draft genome of the hymenopteran hunting robber fly Dasypogon diadema, and analysed its venom by a combined proteotranscriptomic approach, and compared our results to recently described robber fly venoms to assess the general composition and major components of asilid venom. We then applied a comparative genomics approach, based on one additional asilid genome, ten high-quality dipteran genomes, and two lepidopteran outgroup-genomes, to reveal the evolutionary mechanisms and origins of identified venom proteins in robber flies. While some venom proteins were identified in the non-asilid genomes, several of the identified highly expressed venom proteins appear to be unique to robber flies. Our results reveal that the venom of D. diadema likely evolves in a multimodal fashion comprising 1) neofunctionalization after gene duplication, 2) expression-dependent co-option of proteins and 3) asilid lineage-specific orphan genes with enigmatic origin. The role of such orphan genes is currently being disputed in evolutionary genomics, but has not yet discussed in the context of toxin evolution. Our results display an unexpected dynamic venom evolution in asilid insects, which contrasts the findings of the only other insect toxicogenomic evolutionary analysis, in parasitoid wasps (Hymenoptera), were toxin evolution is dominated by single gene co-option.

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Project description:Most species of bee are capable of delivering a defensive sting which is often painful. A solitary lifestyle is the ancestral state of bees and most extant species are solitary, but information on bee venoms comes predominantly from studies on eusocial species. In this study we investigated the venom composition of the Australian great carpenter bee, Xylocopa aruana Ritsema, 1876. We show that the venom is relatively simple, composed mainly of one small amphipathic peptide (XYTX1-Xa1a), with lesser amounts of an apamin homologue (XYTX2-Xa2a) and a venom phospholipase-A2 (PLA2). XYTX1-Xa1a is homologous to, and shares a similar mode-of-action to melittin and the bombilitins, the major components of the venoms of the eusocial Apis mellifera (Western honeybee) and Bombus spp. (bumblebee), respectively. XYTX1-Xa1a and melittin directly activate mammalian sensory neurons and cause spontaneous pain behaviours in vivo, effects which are potentiated in the presence of venom PLA2. The apamin-like peptide XYTX2-Xa2a was a relatively weak blocker of small conductance calcium-activated potassium (KCa) channels and, like A. mellifera apamin and mast cell-degranulating peptide, did not contribute to pain behaviours in mice. While the composition and mode-of-action of the venom of X. aruana are similar to that of A. mellifera, the greater potency, on mammalian sensory neurons, of the major pain-causing component in A. mellifera venom may represent an adaptation to the distinct defensive pressures on eusocial Apidae.

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