Presenter: Naomi Young
Authors: Naomi Young
Faculty Advisor: Paul Frandsen
Institution: Brigham Young University
Many arthropods use silk in a variety of ways including reproduction, development, and obtaining food1-4. The multifarious structures and purposes of silk are the reason why synthetic silk has remained an elusive goal in biomaterial research and engineering5-8. In Lepidoptera (butterflies and moths), genotypic diversity is wide, reflecting a potential restructuring of repetitive structural motifs, potentially in response to a dynamic environment. Because of a lack of genome assemblies, these patterns have not been explored across the diversity of silk in butterflies and moths. In Lepidoptera, silk is composed of heavy and light chain fibroin protein in a sericin-based coating with an adhesive glycoprotein lining9-11. The primary protein in this complex is the repetitive heavy chain fibroin12. Recent efforts of the Darwin Tree of Life project at the Sanger Institute in the UK have led to the deposit of many high-quality Lepidoptera genomes available for analysis, resulting in >120 genomes for comparison. Here, we present the results of a large-scale examination of heavy chain fibroin across Lepidoptera. This research represents the first step toward building an understanding of the diversity of silk proteins across butterflies and moths and will form the foundation for future functional research on silk.