Serpin-Driven Green Camouflage and NIR Fluorescence in Frogs
Ravichandran VigneshiD, Tri VuiD, Grace HarveyiD, Luca MenozziiD, Jesse R. J. DeliaiD, William White, Pohan LiniD, Erini G. GalatisiD, Sönke JohnseniD, Junjie YaoiD, Carlos TaboadaiD
Abstract
Animals have evolved multiple strategies to generate optical traits and coloration. While most amphibians rely on a three-dimensional arrangement of chromatophores in the skin, hundreds of arboreal frog species achieve leaf-like green color through a different mechanism involving reduced pigmentation, subcutaneous biological mirrors, and high concentrations of the blood-derived pigment biliverdin. Although biliverdin is rapidly excreted in most vertebrates, hylid and centrolenid frogs can retain it through the binding to a serpin-family protein (BBS). Here we show that BBSs bind biliverdin with high affinity (Kd 700 nm) rendering these frogs fluorescent in a spectral region where biological tissues are largely transparent. Together, BBSs shed light on serpin evolution, protein thermostability, amphibian color diversity, and the development of NIR molecular probes.
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