Demonstrates enhanced protein engineering in Vibrio natriegens, suggesting an innovative approach for synthetic biology.
Genetic diversification serves as the foundation for in vivo molecular evolution. The fusion of a cytidine deaminase with T7 RNA polymerase (MutaT7) enables efficient diversification of DNA sequences downstream of the T7 promoter in model microbial hosts E. coli and S. cerevisiae . Vibrio natriegens, currently the fastest-growing nonpathogenic bacterium with a doubling time half that of E. coli, emerged as a promising alternative chassis for synthetic biology. Here, we report the establishment of MutaT7 in V. natriegens (dubbed VnMutaT7), achieving rapid evolution of the model protein TEM-1 to confer high-level ceftazidime resistance in just 36 h. This work establishes the potential of V. natriegens as an accelerated platform for protein engineering.
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Zhu et al. (2026) studied this question.
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