Repeated convergent evolution of bradykinin mimics as defensive toxins.
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| Title: | Repeated convergent evolution of bradykinin mimics as defensive toxins. |
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| Authors: | Shi, Naiqi (AUTHOR), Touchard, Axel (AUTHOR), Schendel, Vanessa (AUTHOR), Koch, Thomas Lund (AUTHOR), Starobova, Hana (AUTHOR), Niu, Pancong (AUTHOR), Tran, Hue (AUTHOR), Ragnarsson, Lotten (AUTHOR), Safavi-Hemami, Helena (AUTHOR), Vetter, Irina (AUTHOR), Robinson, Samuel D. (AUTHOR) |
| Source: | Science. 3/5/2026, Vol. 391 Issue 6789, p1046-1052. 7p. |
| Subjects: | Bradykinin, Toxins, Natural selection, Mimicry (Biology), Venom, Convergent evolution, Peptide hormones |
| Abstract: | Natural selection can drive the evolution of similar traits through convergent evolution. Short peptides identical to the vertebrate hormone bradykinin (BK) have been reported from the venoms and skin secretions of certain species of wasps (order Hymenoptera) and frogs (order Anura), respectively. In this study, we demonstrate that the genes encoding the BK-like peptides of hymenopteran venoms and anuran skin secretions do not share common ancestry with that of the vertebrate hormone but instead independently evolved multiple times from peptide toxin genes. These peptides serve a defensive function against vertebrate predators and their resemblance to BK was driven by selection for efficacy at the predators' receptors. Our findings highlight how natural selection can drive repeated convergent evolution of similar molecules across distantly related lineages. Editor's summary: Bradykinin is a peptide hormone that causes pain and vasodilation in mammals during wound response. Although bradykinin arose in early vertebrates, similar or identical molecules exist in venoms and toxins in certain wasps and frogs. Shi et al. looked across representative species from the orders Hymenoptera and Anura to determine these genes' evolutionary origin. They found that these molecules arose independently from those found in mammals, including those in the frog species, which maintain their own endogenous bradykinin that differs from the one used in their toxins. The authors posit that these venoms and toxins convergently evolved their similarity to bradykinin due to predation pressure from mammals. —Corinne Simonti INTRODUCTION: Bradykinin is a short peptide hormone found in vertebrates. It is released from its precursor protein kininogen in response to tissue damage, causing local vasodilation, increased vascular permeability, and both acute and long-lasting pain through its action on bradykinin receptors. Peptides that are similar to bradykinin have been reported in the venoms of some wasps and ants (order Hymenoptera) and in the defensive skin secretions of some frogs (order Anura). Given the similarity between the wasp venom peptides, frog skin peptides, and vertebrate bradykinin, it had been assumed that they share a common evolutionary origin. RATIONALE: Similar traits in different species can reflect common ancestry but can also arise independently through convergent evolution. We hypothesized that the hymenopteran and anuran bradykinin-like peptides evolved independently of vertebrate bradykinin and instead are products of convergent evolution to mimic it. RESULTS: We analyzed the genes encoding hymenopteran venom bradykinin-like peptides and revealed that they do not share common ancestry with bradykinin. Instead, they evolved through duplication and neofunctionalization of other hymenopteran venom peptide genes, and this happened on at least four independent occasions. We demonstrated that hymenopteran venom bradykinin-like peptides are potent activators of vertebrate bradykinin receptors and that some have similar activity to mammalian bradykinin in models of mammalian nociception, suggesting that defense against vertebrate predators was the selective driver underlying their repeated evolution. Analysis of the genes encoding the anuran skin bradykinin-like peptides revealed that they also evolved independently of bradykinin and that this happened multiple times within the Anura. Experiments demonstrating specificity of bradykinins of different species for their conspecific receptors provided strong evidence that the similarity of wasp and frog bradykinin-like peptides to specific vertebrate bradykinins reflects selection for efficacy at vertebrate predators' receptors. CONCLUSION: The BK-like peptides of hymenopterans and anurans are the product of repeated convergent evolution driven by molecular mimicry. The repeated evolution of bradykinin-like peptides highlights the contextual malleability of genes and their products. With a suitable genetic substrate and shared environmental pressure, natural selection can result in repeated convergent evolution of identical molecules across distantly related species. Peptides that mimic the vertebrate hormone bradykinin have evolved repeatedly as defensive toxins.: Canonical bradykinin peptide sequences for selected vertebrate lineages [Mammalia, Sauropsida (excluding Serpentes), Serpentes, and Teleostei] are highlighted blue. Representative bradykinin-like peptides that have evolved independently as defensive toxins in other lineages are highlighted purple. Counterclockwise from top left: Polistes humilis (Vespidae), Heterodontonyx darwinii (Pompilidae), Triscolia ardens (Scoliidae), Neoponera goeldii (Formicidae), Physalaemus nattereri (Hylidae), Rana temporaria (Ranidae), and Bombina bombina (Bombinatoridae). B2R, human bradykinin B2 receptor (gray) with human bradykinin bound (cyan) (Protein Data Bank: SF2O). Illustrations by Ilusea Studio. [ABSTRACT FROM AUTHOR] |
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| Database: | Psychology and Behavioral Sciences Collection |
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