TIGR-tas cytosine base editing system and application thereof

By fusing cytosine deaminase with the TIGR-Tas system effector protein parTasR and utilizing mismatch-programmed tigRNA, the TIGR-Tas cytosine base editing system was constructed, solving the problems of PAM restriction and low editing efficiency. This system achieves efficient and controllable cytosine base editing, making it suitable for disease model construction and gene therapy.

CN122629031APending Publication Date: 2026-08-25AGSINO GENSOURCES CO LTD
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Patent Information

Application Number
CN202610808785.8
Authority / Receiving Office
CN · China
Patent Type
Applications(China)
Current Assignee / Owner
Filing Date
2026-06-05
Publication Date
2026-08-25

AI Technical Summary

Technical Problem

Existing RNA-guided nucleases rely on specific protospacer sequence neighbor motifs (PAMs) to recognize limited target ranges. The TIGR-Tas framework has low editing efficiency in mammalian cells and suffers from increased byproducts, making it difficult to achieve efficient and controllable cytosine base editing.

Method used

By fusing cytosine deaminase with the TIGR-Tas system effector protein parTasR and combining it with mismatch-programmed tigRNA, parTasR was induced to enter a nickase-like catalytic state, thus constructing a PAM-independent TIGR-Tas cytosine base editing system, which was optimized to TIGR-Tas-CBE-V3.

Benefits of technology

It overcomes the limitations of PAM, expands the target range, significantly improves editing efficiency, reduces double-strand break-related byproducts, and maintains good genome and transcriptome specificity, making it suitable for disease model construction and gene therapy.

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Abstract

The application belongs to the field of bioengineering and gene editing technology, and particularly relates to a TIGR-Tas cytosine base editing system and application thereof. The application provides a PAM-independent, efficient controllable and low byproduct TIGR-Tas cytosine base editor and an optimized variant thereof by fusing cytosine deaminase with a TIGR-Tas system effector protein parTasR and combining mismatch programming of tigRNA to induce parTasR to be in a nickase-like catalytic state, so as to realize windowed C→T base conversion in mammalian cells and provide better technical support for disease model construction and gene therapy and the like.
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