Silk of the common clothes moth, Tineola bisselliella, a cosmopolitan pest belonging to the basal ditrysian moth line
Language English Country England, Great Britain Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
33476773
DOI
10.1016/j.ibmb.2021.103527
PII: S0965-1748(21)00010-2
Knihovny.cz E-resources
- Keywords
- Adhesive, Fibroin, Peptide fingerprinting, Sericin, Serine protease, Transcriptome, Zonadhesin-like,
- MeSH
- Biological Evolution * MeSH
- Fibroins metabolism MeSH
- Silk * chemistry genetics metabolism MeSH
- Insect Proteins genetics metabolism MeSH
- Protease Inhibitors metabolism MeSH
- Larva genetics metabolism physiology MeSH
- Moths * genetics metabolism physiology MeSH
- Proteomics methods MeSH
- Sericins metabolism MeSH
- Animals MeSH
- Check Tag
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Fibroins MeSH
- Silk * MeSH
- Insect Proteins MeSH
- Protease Inhibitors MeSH
- Sericins MeSH
Many lepidopteran larvae produce silk secretions to build feeding tubes and cocoons that play important protective roles in their lives. Recent research on the silk of bombycoid and pyralid moths has shown that it contains several highly abundant silk components with remarkable mechanical properties. It was also found to contain a number of other proteins of which the functions have yet to be identified. To gain an overview of the silk composition in more primitive lepidopteran species and to identify the core silk components common to most species, we analyzed the cocoon proteins of Tineola bisselliella, which belongs to the basal ditrysian moth line. Using de novo transcriptome sequencing combined with mass spectrometry (MS)-based proteomics, we detected more than 100 secretory proteins in the silk cocoons. Fibroin, sericins, and protease inhibitors were found to be the most abundant proteins, along with several novel candidate silk components. We also verified the tissue and developmental stage specificity of the silk protein expression and characterized the morphology of both the silk glands and silk in T. bisselliella. Our study provides a detailed analysis of silk in the primitive moth, expands the known set of silk-specific genes in Lepidoptera, and helps to elucidate their evolutionary relationships.
References provided by Crossref.org
Characterization and comparative analysis of sericin protein 150 in Bombyx mori
Using the multi-omics approach to reveal the silk composition in Plectrocnemia conspersa
The Role of Filippi's Glands in the Silk Moths Cocoon Construction