ArticleScientific reports2023
The tardigrade protein CAHS D interacts with, but does not retain, water in hydrated and desiccated systems.
Article in Scientific reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 20 citations in OpenAlex.
- Expression of tardigrade extremotolerance-associated proteins improves recovery but not acute stress response of human microvascular endothelial cells.Scientific reports · 2026Article
- Cytoplasmic abundant heat-soluble proteins from tardigrades protect synthetic cells under stress.Nature communications · 2026Article
- Integrative bioinformatics analysis of potential convergent evolution in tardigrade stress-response proteins.Stress biology · 2026Article
- A phase transition modulates the protective function of a tardigrade disordered protein during desiccation.Protein science : a publication of the Protein Society · 2025Article
- Life on the dry side: a roadmap to understanding desiccation tolerance and accelerating translational applications.Nature communications · 2025Review
- Crowding in Anhydrobiosis.Sub-cellular biochemistry · 2025Review
- An evaluation of thermal tolerance in six tardigrade species in an active and dry state.Biology open · 2024Article
- Leveraging tardigrade proteins Dsup and CAHS D for enhanced neural protection in neurosurgery and neuroscience.Neurosurgical review · 2024Review
- Trimethylamine N-oxide (TMAO) doubly locks the hydrophobic core and surfaces of protein against desiccation stress.Protein science : a publication of the Protein Society · 2024Article
- Protecting Proteins from Desiccation Stress Using Molecular Glasses and Gels.Chemical reviews · 2024Review
- Labile assembly of a tardigrade protein induces biostasis.Protein science : a publication of the Protein Society · 2024Article
- Helicity of a tardigrade disordered protein contributes to its protective function during desiccation.Protein science : a publication of the Protein Society · 2024Article
- The major inducible small heat shock protein HSP20-3 in the tardigrade Ramazzottius varieornatus forms filament-like structures and is an active chaperone.Cell stress & chaperones · 2024Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Tardigrades are a group of microscopic animals renowned for their ability to survive near complete desiccation. A family of proteins, unique to tardigrades, called Cytoplasmic Abundant Heat Soluble (CAHS) proteins are necessary to mediate robust desiccation tolerance in these animals. However, the mechanism(s) by which CAHS proteins help to protect tardigrades during water-loss have not been fully elucidated. Here we use thermogravimetric analysis to empirically test the proposed hypothesis that tardigrade CAHS proteins, due to their propensity to form hydrogels, help to retain water during desiccation. We find that regardless of its gelled state, both in vitro and in vivo, a model CAHS protein (CAHS D) retains no more water than common proteins and control cells in the dry state. However, we find that while CAHS D proteins do not increase the total amount of water retained in a dry system, they interact with the small amount of water that does remain. Our study indicates that desiccation tolerance mediated by CAHS D cannot be simply ascribed to water retention and instead implicates its ability to interact more tightly with residual water as a possible mechanism underlying its protective capacity. These results advance our fundamental understanding of tardigrade desiccation tolerance which could provide potential avenues for new technologies to aid in the storage of dry shelf-stable pharmaceuticals and the generation of stress tolerant crops to ensure food security in the face of global climate change.
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