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Sticking Together an Updated Model for Temporary Adhesion.
Bertemes, Philip; Grosbusch, Alexandra L; Geschwindt, Anik; Kauffmann, Bob; Salvenmoser, Willi; Mertens, Birte; Pjeta, Robert; Egger, Bernhard; Ladurner, Peter.
Afiliação
  • Bertemes P; Institute of Zoology, University of Innsbruck, 6020 Innsbruck, Austria.
  • Grosbusch AL; Center of Molecular Biosciences Innsbruck, University of Innsbruck, 6020 Innsbruck, Austria.
  • Geschwindt A; Institute of Zoology, University of Innsbruck, 6020 Innsbruck, Austria.
  • Kauffmann B; Center of Molecular Biosciences Innsbruck, University of Innsbruck, 6020 Innsbruck, Austria.
  • Salvenmoser W; Institute of Zoology, University of Innsbruck, 6020 Innsbruck, Austria.
  • Mertens B; Center of Molecular Biosciences Innsbruck, University of Innsbruck, 6020 Innsbruck, Austria.
  • Pjeta R; Institute of Zoology, University of Innsbruck, 6020 Innsbruck, Austria.
  • Egger B; Center of Molecular Biosciences Innsbruck, University of Innsbruck, 6020 Innsbruck, Austria.
  • Ladurner P; Institute of Zoology, University of Innsbruck, 6020 Innsbruck, Austria.
Mar Drugs ; 20(6)2022 May 27.
Article em En | MEDLINE | ID: mdl-35736161
Non-parasitic flatworms are known to temporarily attach to the substrate by secreting a multicomponent bioadhesive to counteract water movements. However, to date, only species of two higher-level flatworm taxa (Macrostomorpha and Proseriata) have been investigated for their adhesive proteins. Remarkably, the surface-binding protein is not conserved between flatworm taxa. In this study, we sequenced and assembled a draft genome, as well as a transcriptome, and generated a tail-specific positional RNA sequencing dataset of the polyclad Theama mediterranea. This led to the identification of 15 candidate genes potentially involved in temporary adhesion. Using in situ hybridisation and RNA interference, we determined their expression and function. Of these 15 genes, 4 are homologues of adhesion-related genes found in other flatworms. With this work, we provide two novel key components on the flatworm temporary adhesion system. First, we identified a Kringle-domain-containing protein (Tmed-krg1), which was expressed exclusively in the anchor cell. This in silico predicted membrane-bound Tmed-krg1 could potentially bind to the cohesive protein, and a knockdown led to a non-adhesive phenotype. Secondly, a secreted tyrosinase (Tmed-tyr1) was identified, which might crosslink the adhesive proteins. Overall, our findings will contribute to the future development of reversible synthetic glues with desirable properties for medical and industrial applications.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Platelmintos Tipo de estudo: Prognostic_studies Limite: Animals Idioma: En Ano de publicação: 2022 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Platelmintos Tipo de estudo: Prognostic_studies Limite: Animals Idioma: En Ano de publicação: 2022 Tipo de documento: Article