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First discovered in the 1980's, late embryogenesis abundant (LEA) proteins now play an important role in the modern paradigm of anhydrobiosis. These proteins are intrinsically disordered in the hydrated state, and gain more defined secondary structure motifs (e.g. beta-sheets and alpha-helices) during the process of dehydration. This gain in secondary structure likely plays a key role in the ability of LEA proteins to protect the machinery important to life sustaining processes within the cell during severe water stress. Methods such as high resolution respirometry offer insight into the level of protection conferred by these proteins during periods of acute water stress. An embryonic cell line derived from the model organism Drosophila melanogaster was used to engineer several clones that transgenically express combinations of five distinct LEA proteins originally found in the brine shrimp Artemia fransiscana. Non-transformed control cells exposed to acute water stress due to hyperosmotic conditions exhibited reduced levels of oxygen consumption. Cell lines which transgenically expressed AfrLEA2, or combinations of the mitochondrial proteins AfrLEA1.3, AfrLEA3m, and the cytoplasmic protein AfrLEA6 showed overall higher residual respiration levels during periods of osmotic stress when compared to control cells. It is clear that the expression of LEA proteins can provide protection to otherwise dehydration sensitive cells during periods of water stress. An important next step in the study of these proteins will be the further elucidation of possibly distinct physiological roles within the cell. One method with the potential for providing key answers to this question involves protein crosslinking in-vivo. The utilization of this method could lead to the identification of binding partners within the cell, leading to a more in-depth understanding of the physiology that makes anhydrobiotic organisms unique.

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