Synthetic llama antibody used to rescue mutant proteins

Artificial deubiquitin activating enzyme is a combination of synthetic Nanobodies that recognize proteins that can rescue proteins tagged with destruction.

Researchers have created a new technology using synthetic llamas antibody To prevent certain proteins from being destroyed inside the cell. According to the team, this approach could be used to treat dozens of diseases that result from the destruction of incomplete but fully functional proteins, including cystic fibrosis.

This study was conducted at Columbia University’s Irving Medical Center in the United States. Researchers explain that in many genetic disorders, including cystic fibrosis, mutated proteins can perform their job, but are tagged as disruptive by cell quality control mechanisms. I will.

“If cystic fibrosis mutant proteins can escape the cell’s quality control mechanism, they work pretty well,” said Professor Henry Colecraft, who led the study.

In cells, proteins destined to be destroyed are marked with a small peptide called ubiquitin. The deubiquitinase enzyme (DUB) can remove these tags, but simply increasing DUB activity will indiscriminately rescue and harm all intracellular proteins marked for destruction. ..

Colecraft and his graduate student, Scott Kanner, have found that they can develop solutions that utilize Nanobodies, small antibodies naturally produced by llamas, camels and alpaca, discovered nearly 30 years ago. Unlike normal antibodies, these small Nanobodies bind to the target with high specificity and retain this property intracellularly.

A new technology called artificial ubiquitin activating enzyme (enDUB) combines synthetic Nanobodies that recognize specific proteins with enzymes that can rescue proteins tagged with destruction.

Researchers have found two different enDUBs designed to rescue mutated proteins in cystic fibrosis and long QT syndrome, a hereditary heart disease that can cause arrhythmias and sudden death. We have tested two different enDUBs designed to rescue.

To build each enDUB, researchers extracted binders from a synthetic yeast Nanobody display library containing millions of unique Nanobodies. After creation, each enDUB was tested in cells that produced the mutant protein. In both cases, enDUB prevented the protein from being destroyed, and the protein moved to its normal location on the cell membrane, where it performed its normal function.

“One of the cystic fibrosis proteins we tested offers the amazing relief of returning protein levels in the cell membrane to about 50% of normal,” said Colecraft. “If it happened to the patient, it would change.”

Both diseases investigated in this study are caused by mutations in ion channel proteins, but this approach can be applied to any protein in the cell, not just membrane proteins and proteins altered by gene mutations.

“It has the potential to be applied to any disease that is caused by proteolysis, such as cancer and epilepsy,” says Colecraft.

The study was published in Nature method..

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