ArticleCommunications biology2024
Tardigrade secretory proteins protect biological structures from desiccation.
Article in Communications biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Tardigrade-Derived Strategy for Low-Cost Storage of Cell-Free Expression Lysates.ACS synthetic biology · 2026Article
- Expression of tardigrade extremotolerance-associated proteins improves recovery but not acute stress response of human microvascular endothelial cells.Scientific reports · 2026Article
- Candidate Cyanide Resistance Genes in Eutardigrade (Tardigrada) Genomes and KCN Resistance ofInternational journal of molecular sciences · 2026Article
- Cytoplasmic abundant heat-soluble proteins from tardigrades protect synthetic cells under stress.Nature communications · 2026Article
- Haplotype-resolved telomere-to-telomere genome ofGenome research · 2026Article
- Tardigrades' cytoplasmic abundant heat soluble proteins serve as membrane protectors during dehydration.Research square · 2025Article
- Atomic armor for thermal stability in nanoporous structures.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Adaptive peptide dispersions enable drying-induced biomolecule encapsulation.Nature materials · 2025Article
- Radioprotection redefined: drug discovery at the intersection of tardigrade biology and translational pharmacology.Frontiers in pharmacology · 2025Article
- Crowding in Anhydrobiosis.Sub-cellular biochemistry · 2025Review
- Antioxidant Defense in the Toughest Animals on the Earth: Its Contribution to the Extreme Resistance of Tardigrades.International journal of molecular sciences · 2024Review
- Long-Term Survivability of TardigradeLife (Basel, Switzerland) · 2024Article
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Authors and funding
6 authors.
Funding
Abstract
Tardigrades, microscopic animals that survive a broad range of environmental stresses, express a unique set of proteins termed tardigrade-specific intrinsically disordered proteins (TDPs). TDPs are often expressed at high levels in tardigrades upon desiccation, and appear to mediate stress adaptation. Here, we focus on the proteins belonging to the secreted family of tardigrade proteins termed secretory-abundant heat soluble ("SAHS") proteins, and investigate their ability to protect diverse biological structures. Recombinantly expressed SAHS proteins prevent desiccated liposomes from fusion, and enhance desiccation tolerance of E. coli and Rhizobium tropici upon extracellular application. Molecular dynamics simulation and comparative structural analysis suggest a model by which SAHS proteins may undergo a structural transition upon desiccation, in which removal of water and solutes from a large internal cavity in SAHS proteins destabilizes the beta-sheet structure. These results highlight the potential application of SAHS proteins as stabilizing molecules for preservation of cells.
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Registered trials
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