4.6 Article

Silk of the common clothes moth, Tineola bisselliella, a cosmopolitan pest belonging to the basal ditrysian moth line

Journal

INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY
Volume 130, Issue -, Pages -

Publisher

PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.ibmb.2021.103527

Keywords

Sericin; Fibroin; Serine protease; Zonadhesin-like; Transcriptome; Peptide fingerprinting; Adhesive

Funding

  1. Czech Republic Ministry of Education, Youth and Sports [LTC17073]
  2. European Regional Development FundProject Mechanisms and dynamics of macromolecular complexes: from single molecules to cells [CZ.02.1.01/0.0/0.0/15_003/0000441]
  3. MEYS CR [LM2018129]
  4. ERDF [CZ.02.1.01/0.0/0.0/16_013/0001775]
  5. Collaborative Research Centre 992 Medical Epigenetics (DFG) [SFB 992/1 2012]
  6. German Federal Ministry of Education and Research (BMBF) [031 A538A/A538C RBC, 031L0101B/031L0101C, 031L0106 de.STAIR]

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Many lepidopteran larvae produce silk secretions for feeding tubes and cocoons. Recent research on the silk of bombycoid and pyralid moths has shown abundant silk components with remarkable mechanical properties. Analysis of cocoon proteins in Tineola bisselliella revealed fibroin, sericins, and protease inhibitors as the most abundant proteins, along with novel candidate silk components.
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.

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