Directed evolution for improved TEV protease variants for biotechnology applications

ChangeBridge: Patent Grants - Biotech (C12N)

Published March 31st, 2026

Detected March 31st, 2026

Summary

USPTO granted patent US12590325B2 to CZ Biohub SF for a yeast-based directed evolution platform that improves tobacco etch virus (TEV) protease catalytic rate. The platform uses proteolytic release of a membrane-anchored transcription factor and a photosensory LOV domain for temporal regulation, enabling selection of faster TEV variants over multiple selection rounds.

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What changed

USPTO granted patent US12590325B2 to CZ Biohub SF, LLC covering a yeast-based platform for directed evolution of TEV protease catalytic properties. The technology involves proteolytic release of a membrane-anchored transcription factor and temporal regulation using a photosensory LOV domain, allowing faster TEV variants to be selected by gradually decreasing light exposure time. The patent includes 20 claims covering both the directed evolution platform and mutant TEV proteases useful for FLARE and SPARK tools.

Patent holders may now commercialize the technology or license it to third parties. Researchers and companies developing protease-based applications should review Freedom to Operate if developing similar products. This is a routine patent issuance that grants intellectual property rights without imposing regulatory compliance obligations.

Source document (simplified)

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Directed evolution for obtaining improved variants of TEV protease for biotechnological applications

Grant US12590325B2 Kind: B2 Mar 31, 2026

Assignee

CZ Biohub SF, LLC

Inventors

Alice Y. Ting, Mateo Isidro Sanchez Lopez

Abstract

Tobacco etch virus protease (TEV) is one of the most widely used proteases in biotechnology because of its exquisite sequence-specificity. A limitation of TEV is its slow catalytic rate, which limits product generation and therefore signal output. Provided is a generalizable yeast-based platform for directed evolution of protease catalytic properties. Protease activity is determined via proteolytic release of a membrane-anchored transcription factor, and access to TEV's cleavage site is temporally regulated using a photosensory LOV domain. By gradually decreasing light exposure time, faster variants of TEV were selected over multiple rounds of selection. The mutant TEV proteases and the directed evolution platform are useful in a wide range of biotechnology applications, such as FLARE and SPARK tools.