ArticleBMC biology2023
Engineered domain-inlaid Nme2Cas9 adenine base editors with increased on-target DNA editing and targeting scope.
Article in BMC biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 9 citations in OpenAlex.
- Embedded CRISPRi Enhances Gene-Silencing Efficiency in Drosophila.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- ABE9 fused to SpRY Cas9 nickase enables precise generation of bystander free mouse models.Scientific reports · 2026Article
- Developing safe and efficient CGBE editor based on Cas-embedding strategy.Synthetic and systems biotechnology · 2025Article
- A universal and wide-range cytosine base editor via domain-inlaid and fidelity-optimized CRISPR-FrCas9.Nature communications · 2025Article
- Enhanced Genome Editing Activity with Novel Chimeric ScCas9 Variants in Rice.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Unveiling the potential impact of RNA m5C methyltransferases NSUN2 and NSUN6 on cellular aging.Frontiers in genetics · 2025Article
- Rational Design of Enhanced Nme2Cas9 and Nme2bioRxiv : the preprint server for biology · 2024Article
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Authors and funding
12 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundNme2ABE8e has been constructed and characterized as a compact, accurate adenine base editor with a less restrictive dinucleotide protospacer-adjacent motif (PAM: N4CC) but low editing efficiency at challenging loci in human cells. Here, we engineered a subset of domain-inlaid Nme2Cas9 base editors to bring the deaminase domain closer to the nontarget strand to improve editing efficiency.
resultsOur results demonstrated that Nme2ABE8e-797 with adenine deaminase inserted between amino acids 797 and 798 has a significantly increased editing efficiency with a wide editing window ranging from 4 to 18 bases in mammalian cells, especially at the sites that were difficult to edit by Nme2ABE8e. In addition, by swapping the PAM-interacting domain of Nme2ABE8e-797 with that of SmuCas9 or introducing point mutations of eNme2-C in Nme2ABE8e-797, we created Nme2ABE8e-797
conclusionsThese novel Nme2ABE8es with increased on-target DNA editing and expanded PAM compatibility will expand the base editing toolset for efficient gene modification and therapeutic applications.
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