Project description:In this study we conducted proteomics analyses of historical and contemporary Bombyx mori cocoon shells to case-study the human-driven introduction and diversification of this species in Europe. We employed LC-MS/MS analyses protocols for 81 cocoon shell samples to identify that the cocoon shell of this species contains on average 98±13 (Mean±SD) proteins, Our proteomic datasets provide a valuable foundation for advancing further exploitations of silkworm cocoon shells in multiple scientific perspectives.
Project description:Bombyx mori cocoon has a multi-layer structure that provides optimal protection for silkworm pupa. Research on the mechanical properties of the multi-layer structure revealed structure-property relationships of the cocoon. Here, we investigated the protein components of the B. mori cocoon in terms of its multi-layer structure. Liquid chromatography-tandem mass spectrometry identified 286 proteins from the multiple cocoon layers. In addition to fibroins and sericins, we identified abundant protease inhibitors, seroins and proteins of unknown function. By comparing protein abundance across layers, we found that the outermost layer contained more sericin1 and protease inhibitors and the innermost layer had more seroin1. As many as 36 protease inhibitors were identified in cocoons, indicating efficient inhibitory activities against a fungal protease. Thus, we propose that more abundant protease inhibitors in the outer cocoon layers may provide better protection for the cocoon. This study increases our understanding of the multi-layer mechanism of cocoons, and helps clarify the biological characteristics of cocoons.
Project description:The silkworm cocoon coat is a crucial natural barrier during the pupal stage, protecting the insect from patho-gens and environmental stress and containing silk proteins with notable antioxidant and antimicrobial activities. In this study, water-soluble proteins were extracted from the outer cocoon layer of the Bombyx mori N4 strain using phosphate-buffered saline (PBS) and 8 M urea, and the two buffer systems were compared in terms of protein yield, bioactivity, and proteomic composition. Urea-based extraction markedly increased the total protein yield, whereas the PBS extract showed stronger radical-scavenging capacity and more pronounced inhibition of fungal growth. Proteomic analysis further revealed clear differences between the two methods in sericin-to-fibroin ratios, recovery of defense-related proteins, and extraction efficiency for membrane-associated proteins. These results provide a ba-sis for the functional exploitation of cocoon coat proteins and for selecting appropriate extraction strategies ac-cording to different research or application goals.
2026-03-30 | PXD076349 |
Project description:Cocoon-shaped related brain transcriptomics