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Mutagenesis and Functional Selection Protocols for Directed Evolution of Proteins in E. coli
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Directed evolution of bacterial polysialyltransferases.

Bettina Janesch1, Lars Baumann2, Alison Mark1

  • 1Department of Chemistry and Biology, Ryerson University, Toronto, ON, Canada.

Glycobiology
|April 13, 2019
PubMed
Summary

Directed evolution improved bacterial polysialyltransferases (polySTs) for therapeutic applications. Researchers enhanced enzyme activity and stability using FACS-based screening, creating better catalysts for protein modification.

Keywords:
Directed evolutionNeisseriapolysialyltransferasescreening

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Area of Science:

  • Biochemistry
  • Glycobiology
  • Enzymology

Background:

  • Polysialyltransferases (polySTs) synthesize sialic acid polymers, crucial in vertebrates and bacterial pathogens.
  • Bacterial polySTs offer potential for modifying therapeutic proteins to extend half-life and for tissue engineering.
  • Recombinant polySTs exhibit poor solubility, low expression, and limited thermal stability, hindering their application.

Purpose of the Study:

  • To enhance the physicochemical and biochemical properties of bacterial polySTs.
  • To develop a robust screening strategy for directed evolution of polySTs.
  • To identify improved polyST mutants for in vitro polysialylation of therapeutics.

Main Methods:

  • Applied a directed evolution approach to bacterial polySTs.
  • Utilized a fluorescence-activated cell sorting (FACS)-based ultrahigh-throughput assay for screening.
  • Performed plate-based high-throughput secondary screening of mutant libraries.

Main Results:

  • Successfully enriched a large mutant library of bacterial polySTs.
  • Discovered enzyme mutants with significantly increased enzymatic activity compared to wildtype.
  • Identified mutants exhibiting improved thermal stability and solubility.

Conclusions:

  • Directed evolution coupled with FACS screening is a powerful strategy for improving bacterial polySTs.
  • The identified mutants serve as enhanced catalysts for in vitro polysialylation.
  • This approach facilitates the development of improved polySTs for biotechnological applications, particularly in therapeutic protein modification.