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- Title
Tardigrade secretory proteins protect biological structures from desiccation.
- Authors
Lim, Samuel; Reilly, Charles B.; Barghouti, Zeina; Marelli, Benedetto; Way, Jeffrey C.; Silver, Pamela A.
- 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. Tardigrade secretory-abundant heat soluble (SAHS) proteins protect biological structures such as liposomes and microbial cells from dehydration-induced damages, potentially through undergoing structural transition upon desiccation.
- Subjects
MORPHOLOGY; ESCHERICHIA coli; CELL preservation; MOLECULAR dynamics; MICROBIAL cells; LIPOSOMES; HEAT shock proteins
- Publication
Communications Biology, 2024, Vol 7, Issue 1, p1
- ISSN
2399-3642
- Publication type
Article
- DOI
10.1038/s42003-024-06336-w