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Evolution of adhesive systems in amphibians by shifts in gene expression
Some amphibians defend themselves against predators by producing a highly adhesive skin secretion, effectively preventing their ingestion. This study shows how changes in the structure and expression of two proteins underlay the parallel evolution of these defence glues in different frog lineages.
As close relatives of these glue-secreting taxa often produce nonadhesive (and often toxic) skin secretions, glue represents an example of parallel functional innovation: one that changes the phenotype at a molecular scale but manifests its effect - antipredator defence - at the macroscopic level. To investigate whether these parallel shifts towards increased disorder and hydrophilicity represent adaptive evolution, we searched for evidence of positive selection by estimating ratios of nonsynonymous over synonymous codon substitutions 32 of all IgGFcBD found in PRITs. Commercially available biotinylated lectins (Con A, WGA, RCA 120, UEA I, PHA-L, PNA, SBA; Vector Laboratories; Newark, CA, United States) were diluted in BSA-T to a final concentration of 25 μg/ml and applied to the samples for 2 h at 4 °C.
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