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Characterization of silk genes in Ephestia kuehniella and Galleria mellonella revealed duplication of sericin genes and highly divergent sequences encoding fibroin heavy chains

Silk is a secretory product of numerous arthropods with remarkable mechanical properties. In this work, we present the complete sequences of the putative major silk proteins of E. kuehniella and compare them with those of G. mellonella, which belongs to the same moth family Pyralidae. To identify th...

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Autores principales: Wu, Bulah Chia-hsiang, Sauman, Ivo, Maaroufi, Houda Ouns, Zaloudikova, Anna, Zurovcova, Martina, Kludkiewicz, Barbara, Hradilova, Miluse, Zurovec, Michal
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9745057/
https://www.ncbi.nlm.nih.gov/pubmed/36523651
http://dx.doi.org/10.3389/fmolb.2022.1023381
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author Wu, Bulah Chia-hsiang
Sauman, Ivo
Maaroufi, Houda Ouns
Zaloudikova, Anna
Zurovcova, Martina
Kludkiewicz, Barbara
Hradilova, Miluse
Zurovec, Michal
author_facet Wu, Bulah Chia-hsiang
Sauman, Ivo
Maaroufi, Houda Ouns
Zaloudikova, Anna
Zurovcova, Martina
Kludkiewicz, Barbara
Hradilova, Miluse
Zurovec, Michal
author_sort Wu, Bulah Chia-hsiang
collection PubMed
description Silk is a secretory product of numerous arthropods with remarkable mechanical properties. In this work, we present the complete sequences of the putative major silk proteins of E. kuehniella and compare them with those of G. mellonella, which belongs to the same moth family Pyralidae. To identify the silk genes of both species, we combined proteomic analysis of cocoon silk with a homology search in transcriptomes and genomic sequences to complement the information on both species. We analyzed structure of the candidate genes obtained, their expression specificity and their evolutionary relationships. We demonstrate that the silks of E. kuehniella and G. mellonella differ in their hydrophobicity and that the silk of E. kuehniella is highly hygroscopic. In our experiments, we show that the number of genes encoding sericins is higher in G. mellonella than in E. kuehniella. By analyzing the synteny of the chromosomal segment encoding sericin genes in both moth species, we found that the region encoding sericins is duplicated in G. mellonella. Finally, we present the complete primary structures of nine fibH genes and proteins from both families of the suborder Pyraloidea and discuss their specific and conserved features. This study provides a foundation for future research on the evolution of silk proteins and lays the groundwork for future detailed functional studies.
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spelling pubmed-97450572022-12-14 Characterization of silk genes in Ephestia kuehniella and Galleria mellonella revealed duplication of sericin genes and highly divergent sequences encoding fibroin heavy chains Wu, Bulah Chia-hsiang Sauman, Ivo Maaroufi, Houda Ouns Zaloudikova, Anna Zurovcova, Martina Kludkiewicz, Barbara Hradilova, Miluse Zurovec, Michal Front Mol Biosci Molecular Biosciences Silk is a secretory product of numerous arthropods with remarkable mechanical properties. In this work, we present the complete sequences of the putative major silk proteins of E. kuehniella and compare them with those of G. mellonella, which belongs to the same moth family Pyralidae. To identify the silk genes of both species, we combined proteomic analysis of cocoon silk with a homology search in transcriptomes and genomic sequences to complement the information on both species. We analyzed structure of the candidate genes obtained, their expression specificity and their evolutionary relationships. We demonstrate that the silks of E. kuehniella and G. mellonella differ in their hydrophobicity and that the silk of E. kuehniella is highly hygroscopic. In our experiments, we show that the number of genes encoding sericins is higher in G. mellonella than in E. kuehniella. By analyzing the synteny of the chromosomal segment encoding sericin genes in both moth species, we found that the region encoding sericins is duplicated in G. mellonella. Finally, we present the complete primary structures of nine fibH genes and proteins from both families of the suborder Pyraloidea and discuss their specific and conserved features. This study provides a foundation for future research on the evolution of silk proteins and lays the groundwork for future detailed functional studies. Frontiers Media S.A. 2022-11-29 /pmc/articles/PMC9745057/ /pubmed/36523651 http://dx.doi.org/10.3389/fmolb.2022.1023381 Text en Copyright © 2022 Wu, Sauman, Maaroufi, Zaloudikova, Zurovcova, Kludkiewicz, Hradilova and Zurovec. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Molecular Biosciences
Wu, Bulah Chia-hsiang
Sauman, Ivo
Maaroufi, Houda Ouns
Zaloudikova, Anna
Zurovcova, Martina
Kludkiewicz, Barbara
Hradilova, Miluse
Zurovec, Michal
Characterization of silk genes in Ephestia kuehniella and Galleria mellonella revealed duplication of sericin genes and highly divergent sequences encoding fibroin heavy chains
title Characterization of silk genes in Ephestia kuehniella and Galleria mellonella revealed duplication of sericin genes and highly divergent sequences encoding fibroin heavy chains
title_full Characterization of silk genes in Ephestia kuehniella and Galleria mellonella revealed duplication of sericin genes and highly divergent sequences encoding fibroin heavy chains
title_fullStr Characterization of silk genes in Ephestia kuehniella and Galleria mellonella revealed duplication of sericin genes and highly divergent sequences encoding fibroin heavy chains
title_full_unstemmed Characterization of silk genes in Ephestia kuehniella and Galleria mellonella revealed duplication of sericin genes and highly divergent sequences encoding fibroin heavy chains
title_short Characterization of silk genes in Ephestia kuehniella and Galleria mellonella revealed duplication of sericin genes and highly divergent sequences encoding fibroin heavy chains
title_sort characterization of silk genes in ephestia kuehniella and galleria mellonella revealed duplication of sericin genes and highly divergent sequences encoding fibroin heavy chains
topic Molecular Biosciences
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9745057/
https://www.ncbi.nlm.nih.gov/pubmed/36523651
http://dx.doi.org/10.3389/fmolb.2022.1023381
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