Tardigrade Proteins Unlock Human Health Breakthrough, UW Scientists Discover

Silvia Sanchez-Martinez, a senior research scientist, assists Maxwell Packebush, a student at the University of Washington from Littleton, Colorado, in purifying one of the proteins from tardigrades. These proteins were used in a recent study demonstrating their ability to stabilize a crucial pharmaceutical used to treat hemophilia and other conditions, eliminating the need for refrigeration. (Photo credit: Thomas Boothby)

In a study published in Scientific Reports, Thomas Boothby, an assistant professor of molecular biology, and his team have demonstrated that tardigrade proteins, both natural and engineered, can stabilize a critical pharmaceutical used to treat hemophilia and other medical conditions without the requirement of refrigeration, even in extreme temperatures.

Researchers at the University of Wyoming have made a breakthrough in the study of tardigrades, or water bears, microscopic creatures that can survive extreme conditions stabilized human blood clotting Factor VIII, a vital therapeutic used to treat genetic diseases and extreme bleeding, using proteins found in tardigrades, also known as water bears.

Tardigrades, also known as water bears, are microscopic, water-dwelling animals that are known for their extreme resilience and ability to survive in harsh conditions. They are typically less than half a millimeter long and can survive being completely dried out, frozen to just above absolute zero, heated to over 300 degrees Fahrenheit, irradiated several thousand times beyond what a human could withstand, and even survive the vacuum of outer space. They are able to do so, in part, by manufacturing a sugar called trehalose and a protein called CAHS D.

Factor VIII is inherently unstable, and without refrigeration within a precise temperature range, it will break down. This means that people in underdeveloped regions, during natural disasters, space flights, or on battlefields, may not have access to Factor VIII.

The researchers fine-tuned the biophysical properties of trehalose and a protein called CAHS D found in tardigrades to stabilize Factor VIII, allowing it to be stored in austere conditions without refrigeration, including long-term dry storage, extreme heat, and repeated dehydration/rehydration.

The same technique could be applied to other biologics, such as vaccines, antibodies, stem cells, blood, and blood products. The discovery offers a logistically simple and economically viable means of stabilizing life-saving medicines, which could benefit global health initiatives in remote or developing parts of the world, as well as space exploration. The researchers hope their discoveries can also be applied to address other societal and global health issues, such as water scarcity and generating crops that can cope with harsh environments.

The human blood clotting cascade. The clotting cascade of human blood plasma follows two prominent pathways; intrinsic, measured by Activated Partial Thromboplastin Time (aPTT) and extrinsic, measured by Prothrombin Time (PT). To activate the intrinsic pathway, Human Blood Clotting Factor XII (FXII) acts as the first protein in a cascade of clotting factor activation. FXII activates FXI which activates FIX which finally activates FVIII. FVIII subsequently binds to and activates FX. To activate the extrinsic pathway, FVII forms a complex with Tissue Factor, activating FX. After activation of FX, both coagulation pathways converge. FX forms a complex with FV, converting prothrombin into thrombin. Thrombin then converts fibrinogen into fibrin, in turn creating a fibrin clot. Human plasma deficient in Factor VIII (highlighted in red) is unable to clot properly through the intrinsic pathway, unless supplemented with this factor, and thus clots more slowly. Adapted from Zaragoza and Espinoza-Villafuerte, 2017. Credit: Scientific Reports (2023). DOI: 10.1038/s41598-023-31586-9


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