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Next-Generation Sequencing Analysis of the Tineola bisselliella Larval Gut Transcriptome Reveals Candidate Enzymes for Keratin Digestion.
Schwabe, Michael; Griep, Sven; Schmidtberg, Henrike; Plarre, Rudy; Goesmann, Alexander; Vilcinskas, Andreas; Vogel, Heiko; Brinkrolf, Karina.
Afiliação
  • Schwabe M; Department of Bioresources, Fraunhofer Institute for Molecular Biology and Applied Ecology, Ohlebergsweg 12, 35392 Giessen, Germany.
  • Griep S; Bioinformatics and Systems Biology, Justus Liebig University Giessen, Heinrich-Buff-Ring 58, 35392 Giessen, Germany.
  • Schmidtberg H; Institute for Insect Biotechnology, Justus Liebig University Giessen, Heinrich-Buff-Ring 26-32, 35392 Giessen, Germany.
  • Plarre R; Bundesanstalt für Materialforschung und -prüfung (BAM), Unter den Eichen 87, 12205 Berlin, Germany.
  • Goesmann A; Bioinformatics and Systems Biology, Justus Liebig University Giessen, Heinrich-Buff-Ring 58, 35392 Giessen, Germany.
  • Vilcinskas A; Department of Bioresources, Fraunhofer Institute for Molecular Biology and Applied Ecology, Ohlebergsweg 12, 35392 Giessen, Germany.
  • Vogel H; Institute for Insect Biotechnology, Justus Liebig University Giessen, Heinrich-Buff-Ring 26-32, 35392 Giessen, Germany.
  • Brinkrolf K; Entomology Department, Max-Planck Institute for Chemical Ecology, Hans-Knoell-Strasse 8, 07745 Jena, Germany.
Genes (Basel) ; 12(8)2021 07 22.
Article em En | MEDLINE | ID: mdl-34440287
ABSTRACT
The clothes moth Tineola bisselliella is one of a few insects that can digest keratin, leading to the destruction of clothing, textiles and artwork. The mechanism of keratin digestion is not yet fully understood, partly reflecting the lack of publicly available genomic and transcriptomic data. Here we present a high-quality gut transcriptome of T. bisselliella generated from larvae reared on keratin-rich and keratin-free diets. The overall transcriptome consists of 428,221 contigs that were functionally annotated and screened for candidate enzymes involved in keratin utilization. As a mechanism for keratin digestion, we identified cysteine synthases, cystathionine ß-synthases and cystathionine γ-lyases. These enzymes release hydrogen sulfite, which may reduce the disulfide bonds in keratin. The dataset also included 27 differentially expressed contigs with trypsin domains, among which 20 were associated with keratin feeding. Finally, we identified seven collagenases that were upregulated on the keratin-rich diet. In addition to this enzymatic repertoire potentially involved in breaking down keratin, our analysis of poly(A)-enriched and poly(A)-depleted transcripts suggested that T. bisselliella larvae possess an unstable intestinal microbiome that may nevertheless contribute to keratin digestion.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Sequenciamento de Nucleotídeos em Larga Escala / Transcriptoma / Queratinas / Larva / Lepidópteros Idioma: En Ano de publicação: 2021 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Sequenciamento de Nucleotídeos em Larga Escala / Transcriptoma / Queratinas / Larva / Lepidópteros Idioma: En Ano de publicação: 2021 Tipo de documento: Article