Toxicity and Immunogenicity of a Tardigrade Cytosolic Abundant Heat Soluble Protein

Abstract

Tardigrades are microscopic animals recognized for their resilience to extreme stresses, including desiccation, freezing, boiling, low and high pressures, and high doses of radiation. Their ability to survive desiccation is attributed to tardigrade‐specific cytosolic abundant heat soluble (CAHS) proteins. Expression of these proteins in other cells increases the desiccation tolerance of those species, and in vitro, CAHS proteins inhibit desiccation‐induced inactivation of other proteins. We are seeking to test the ability of CAHS proteins to stabilize protein‐based therapeutics, which require refrigeration for transportation and storage. The ability of CAHS proteins to preserve the activity of these pharmaceuticals upon desiccation at room temperature would increase their availability and reduce their cost. To this end, we investigated the toxicity and immunogenicity of CAHS D when injected into mice. Recombinant CAHS D was expressed in E. coli and purified by cation‐exchange chromatography. Purity was verified by mass spectrometry prior to endotoxin removal. Purified CAHS D was injected at various concentrations, and mice were monitored for symptoms of toxicity. No changes in weight or behavior were observed during the 28‐day monitoring period. A large‐scale toxicity study, as well as additional studies to test immunogenicity, is underway.Support or Funding InformationUniversity of North Carolina System Institutional Planning GrantThis abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.