ArticleProceedings of the National Academy of Sciences of the United States of America2020
Multiple origins of green coloration in frogs mediated by a novel biliverdin-binding serpin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 46 citations in OpenAlex.
- Serpin-driven green camouflage and NIR fluorescence in frogs.Science advances · 2026Article
- Label-free photoacoustic imaging of glassfrog development.Photoacoustics · 2025Article
- Long-term evolutionary persistence of a cryptic color polymorphism in frogs.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The first de novo genome assembly and annotation of a green-blooded skink (Prasinohaema aff. flavipes) from a historic museum sample.The Journal of heredity · 2025Article
- Expression patterns of melanin-related genes are linked to crypsis and conspicuousness in a pumpkin toadlet.Molecular ecology · 2025Article
- A green dichromophoric protein enabling foliage mimicry in arthropods.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Infrared camouflage in leaf-sitting frogs: a cautionary tale on adaptive convergence.Journal of the Royal Society, Interface · 2025Article
- Three-dimensional diffractive acoustic tomography.Nature communications · 2025Article
- De Novo Genes.Annual review of genetics · 2024Review
- Single-cell analysis of the amphioxus hepatic caecum and vertebrate liver reveals genetic mechanisms of vertebrate liver evolution.Nature ecology & evolution · 2024Article
- It's not easy being green: Comparing typical skin colouration among amphibians with colour abnormalities associated with chromatophore deficits.Ecology and evolution · 2024Article
- A hundred-year-old mystery-the reproductive mode and larval morphology of the enigmatic frog genus Allophryne (Amphibia; Anura; Allophrynidae).Die Naturwissenschaften · 2024Article
- Multiple Routes to Color Convergence in a Radiation of Neotropical Poison Frogs.Systematic biology · 2023Article
- Article
- Biophosphorescence in fluorescent millipedes (Diplopoda: Xystodesmidae) and its relationships with bioluminescence.Scientific reports · 2023Article
- Host macrocyclic acylcarnitines mediate symbiotic interactions between frogs and their skin microbiome.iScience · 2023Article
- Glassfrogs conceal blood in their liver to maintain transparency.Science (New York, N.Y.) · 2022Article
- Modulation of biliverdin dynamics and spectral properties by Sandercyanin.RSC advances · 2022Article
- Microstructural design for mechanical-optical multifunctionality in the exoskeleton of the flower beetleProceedings of the National Academy of Sciences of the United States of America · 2021Article
- QnAs with Carlos Taboada.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
Corrections and comments
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Authors and funding
13 authors at 6 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many vertebrates have distinctive blue-green bones and other tissues due to unusually high biliverdin concentrations-a phenomenon called chlorosis. Despite its prevalence, the biochemical basis, biology, and evolution of chlorosis are poorly understood. In this study, we show that the occurrence of high biliverdin in anurans (frogs and toads) has evolved multiple times during their evolutionary history, and relies on the same mechanism-the presence of a class of serpin family proteins that bind biliverdin. Using a diverse combination of techniques, we purified these serpins from several species of nonmodel treefrogs and developed a pipeline that allowed us to assemble their complete amino acid and nucleotide sequences. The described proteins, hereafter named biliverdin-binding serpins (BBS), have absorption spectra that mimic those of phytochromes and bacteriophytochromes. Our models showed that physiological concentration of BBSs fine-tune the color of the animals, providing the physiological basis for crypsis in green foliage even under near-infrared light. Additionally, we found that these BBSs are most similar to human glycoprotein alpha-1-antitrypsin, but with a remarkable functional diversification. Our results present molecular and functional evidence of recurrent evolution of chlorosis, describe a biliverdin-binding protein in vertebrates, and introduce a function for a member of the serpin superfamily, the largest and most ubiquitous group of protease inhibitors.
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