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Crystal structure of a charge engineered human lysozyme having enhanced bactericidal activity
Avinash Gill1, Thomas C Scanlon, Daniel C Osipovitch
1Thayer School of Engineering, Dartmouth College, Hanover, New Hampshire, United States of America.
Plos One
|March 17, 2011
Summary
Engineered human lysozyme shows enhanced antibacterial activity by altering its electrostatic potential, overcoming limitations of the wild type enzyme against drug-resistant infections.
Area of Science:
- Biochemistry
- Structural Biology
- Immunology
Background:
- Human lysozyme is crucial for innate immunity but has functional limitations.
- Wild type lysozyme can be inactivated by anionic biopolymers in infections.
- Recombinant lysozymes are explored as therapeutics for drug-resistant infections.
Purpose of the Study:
- To present the crystal structure of a charge-engineered human lysozyme variant.
- To understand the molecular basis for the variant's improved antibacterial activity.
- To elucidate how mutations reduce susceptibility to inhibitory molecules.
Main Methods:
- X-ray crystallography at 2.04 Å resolution.
- Structural analysis of the engineered variant.
- Electrostatic potential mapping and comparison with wild type.
Main Results:
- The variant's structure revealed stabilizing interactions from mutated residues.
- Mutations did not cause significant structural perturbations or loss of stability.
- Substitutions expanded negative electrostatic potential, reducing overall field strength.
Conclusions:
- The remodeled electrostatic field explains reduced inhibition by anionic biopolymers.
- The charge-engineered variant demonstrates enhanced performance against specific infections.
- This variant offers a promising therapeutic strategy for drug-resistant infections.
