Phylogenetic survey of soluble saxitoxin-binding activity in pursuit of the function and molecular evolution of saxiphilin, a relative of transferrin

• Published in: Proceedings of the Royal Society. B, Biological sciences Vol. 264; no. 1383; pp. 891 - 902
• Main Authors: Llewellyn, Lyndon E., Bell, Peter M., Moczydlowski, Edward G.
• Format: Journal Article
• Language: English
• Published: England The Royal Society 22.06.1997
• Subjects: Amphibian Proteins; Animals; Binding sites; Biochemistry; Blood plasma; Carrier Proteins - genetics; Carrier Proteins - metabolism; Crabs; Evolution, Molecular; Hemolymph; Humans; Invertebrates; Mammals; Phylogenetics; Phylogeny; Saxitoxin - metabolism; Snakes; Transferrin - genetics; Transferrins; Vertebrates
• ISSN: 0962-8452; 1471-2954
• DOI: 10.1098/rspb.1997.0124

Saxiphilin is a soluble protein of unknown function which binds the neurotoxin, saxitoxin (STX), with high affinity. Molecular characterization of saxiphilin from the North American bullfrog, Rana catesbeiana, has previously shown that it is a member of the transferrin family. In this study we surveyed various animal species to investigate the phylogenetic distribution of saxiphilin, as detected by the presence of soluble [3H]STX binding activity in plasma, haemolymph or tissue extracts. We found that saxiphilin activity is readily detectable in a wide variety of arthropods, fish, amphibians, and reptiles. The pharmacological characteristics of [3H]STX binding activity in phylogenetically diverse species indicates that a protein homologous to bullfrog saxiphilin is likely to be constitutively expressed in many ectothermic animals. The results suggest that the saxiphilin gene is evolutionarily as old as an ancestral gene encoding bilobed transferrin, an Fe3+-binding and transport protein which has been identified in several arthropods and all the vertebrates which have been studied.