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A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes

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Published on: November 7, 2012

Engineering Endolysins for Enhanced Bacteriolytic Activity Using Genetically Encoded Azido-Containing Noncanonical

Kejing Qi¹, Ming Gao², Bowen Lu¹

¹Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Wuhan University, Wuhan 430072, China.

ACS Synthetic Biology

|November 19, 2025

Summary

This summary is machine-generated.

Genetic code expansion enhances endolysins, potent antibacterial proteins, against multidrug-resistant Gram-negative bacteria. Engineered endolysins show improved stability and broad-spectrum activity, offering new antibiotic strategies.

Keywords:

antimicrobial activity endolysin genetic code expansion gram-negative bacteria noncanonical amino acids protein engineering

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Area of Science:

Biochemistry
Molecular Biology
Microbiology

Background:

Multidrug resistance in Gram-negative bacteria is a major global health threat.
Bacteriophage endolysins are specific antibacterial proteins with therapeutic potential.
Genetic code expansion allows site-specific incorporation of noncanonical amino acids (ncAAs) to engineer protein function.

Purpose of the Study:

To engineer endolysins with enhanced bacteriolytic activity and stability using genetic code expansion.
To investigate the impact of incorporating specific noncanonical amino acids (ncAAs) into endolysins targeting Gram-negative bacteria.

Main Methods:

Genetic code expansion was used to introduce ncAAs, such as p-azido-l-phenylalanine (pAzF) and azidonor-leucine (AnzL), into endolysins LysPA26 and LysDLP1.
The bacteriolytic activity and stability of engineered endolysins were assessed under various conditions (temperature, freezing).

Main Results:

Incorporation of pAzF at position R16 of LysPA26 significantly increased its broad-spectrum bacteriolytic activity and stability against temperature and freezing.
The engineered LysPA26-R16pAzF variant showed enhanced activity compared to the wild type.
Incorporation of AnzL into LysPA26 and pAzF into LysDLP1 also resulted in improved bacteriolytic activity.

Conclusions:

Noncanonical amino acids can be effectively incorporated into endolysins to enhance their antimicrobial properties.
Engineered endolysins demonstrate potential as novel therapeutic agents against multidrug-resistant Gram-negative bacteria.
This strategy offers significant implications for lysin engineering and the development of new antibiotics.