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Sticking Together an Updated Model for Temporary Adhesion
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. Remar...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9229212/ https://www.ncbi.nlm.nih.gov/pubmed/35736161 http://dx.doi.org/10.3390/md20060359 |
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author | Bertemes, Philip Grosbusch, Alexandra L. Geschwindt, Anik Kauffmann, Bob Salvenmoser, Willi Mertens, Birte Pjeta, Robert Egger, Bernhard Ladurner, Peter |
author_facet | Bertemes, Philip Grosbusch, Alexandra L. Geschwindt, Anik Kauffmann, Bob Salvenmoser, Willi Mertens, Birte Pjeta, Robert Egger, Bernhard Ladurner, Peter |
author_sort | Bertemes, Philip |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-9229212 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-92292122022-06-25 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 Mar Drugs Article 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. MDPI 2022-05-27 /pmc/articles/PMC9229212/ /pubmed/35736161 http://dx.doi.org/10.3390/md20060359 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Bertemes, Philip Grosbusch, Alexandra L. Geschwindt, Anik Kauffmann, Bob Salvenmoser, Willi Mertens, Birte Pjeta, Robert Egger, Bernhard Ladurner, Peter Sticking Together an Updated Model for Temporary Adhesion |
title | Sticking Together an Updated Model for Temporary Adhesion |
title_full | Sticking Together an Updated Model for Temporary Adhesion |
title_fullStr | Sticking Together an Updated Model for Temporary Adhesion |
title_full_unstemmed | Sticking Together an Updated Model for Temporary Adhesion |
title_short | Sticking Together an Updated Model for Temporary Adhesion |
title_sort | sticking together an updated model for temporary adhesion |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9229212/ https://www.ncbi.nlm.nih.gov/pubmed/35736161 http://dx.doi.org/10.3390/md20060359 |
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