Silk of the common clothes moth, Tineola bisselliella, a cosmopolitan pest belonging to the basal ditrysian moth line.
Adhesive
Fibroin
Peptide fingerprinting
Sericin
Serine protease
Transcriptome
Zonadhesin-like
Journal
Insect biochemistry and molecular biology
ISSN: 1879-0240
Titre abrégé: Insect Biochem Mol Biol
Pays: England
ID NLM: 9207282
Informations de publication
Date de publication:
03 2021
03 2021
Historique:
received:
07
12
2020
revised:
10
01
2021
accepted:
11
01
2021
pubmed:
22
1
2021
medline:
31
7
2021
entrez:
21
1
2021
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 33476773
pii: S0965-1748(21)00010-2
doi: 10.1016/j.ibmb.2021.103527
pii:
doi:
Substances chimiques
Insect Proteins
0
Protease Inhibitors
0
Sericins
0
Silk
0
Fibroins
9007-76-5
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
103527Informations de copyright
Copyright © 2021 Elsevier Ltd. All rights reserved.