2026-05-06 ミシガン大学
Yongkang Xi, research fellow in mechanical engineering, observes a microscopic image of tardigrade proteins within vesicles at G.G. Brown on North Campus of the University of Michigan on April 22, 2026. Image credit: Jeremy Little, Michigan Engineering
＜関連情報＞
- https://news.umich.edu/death-defying-protein-found-in-tardigrades-preserves-synthetic-cells/
- https://www.nature.com/articles/s41467-026-72328-5
クマムシ由来の細胞質に豊富に存在する熱可溶性タンパク質は、ストレス下にある合成細胞を保護する Cytoplasmic abundant heat-soluble proteins from tardigrades protect synthetic cells under stress
Yongkang Xi,Jianming Mao,Samuel J. Chen,Hossein Moghimianavval,Young Jin Lee,Ayush Panda,Alexander J. Huang,Daniel H. Zhou,L. Andy Xu,Kayla Y. Fu,Solomon Adera,Andrew L. Ferguson & Allen P. Liu
Nature Communications Published:02 May 2026
DOI:https://doi.org/10.1038/s41467-026-72328-5 Unedited version
Abstract
Cytoplasmic abundant heat-soluble (CAHS) proteins, a stress-responsive intrinsically disordered protein from tardigrades, have been discovered to form gel-like networks providing structural support during dehydration, thus enabling anhydrobiosis. However, the mechanism by which CAHS proteins protect the dehydrating cellular membrane remains enigmatic. Using giant unilamellar vesicles (GUVs) as a model membrane system, here we show that encapsulated CAHS12 undergoes a reversible structural transformation that reinforces membrane integrity and preserves encapsulated components, mimicking natural anhydrobiosis. CAHS12-containing GUVs demonstrated stability for weeks and mechanical robustness under dehydration, elevated temperature, and osmotic stresses. Molecular simulations suggest that CAHS12 forms a filamentous network within the vesicle lumen that mitigates membrane collapse and preserves compartmental architecture. Synthetic cells with cell-free transcription-translation capabilities withstand desiccation and recover biochemical activities, akin to the tun state of the tardigrade. This discovery opens up synthetic cell applications in bioengineering, cold-chain-independent biomanufacturing, and adaptive biointerfaces.
