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Disulfide-compatible phage-assisted continuous evolution in the periplasmic space.

Mary S Morrison1,2,3, Tina Wang1,2,3, Aditya Raguram1,2,3

  • 1Merkin Institute of Transformative Technologies in Health Care, Broad Institute of Harvard and MIT, Cambridge, MA, 02142, USA.

Nature Communications
|October 14, 2021
PubMed
Summary
This summary is machine-generated.

We developed periplasmic phage-assisted continuous evolution (pPACE) to enable the continuous evolution of proteins with disulfide bonds. This new system rapidly optimizes antibody binding and expression, expanding the reach of directed evolution technologies.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Engineering

Background:

  • Directed evolution has produced valuable antibodies for research and therapeutics.
  • Disulfide bonds, crucial for antibody stability, limit continuous evolution applications for these proteins.
  • Existing continuous evolution methods are not suitable for disulfide-containing proteins.

Purpose of the Study:

  • To develop a novel continuous evolution system for proteins containing disulfide bonds.
  • To demonstrate the system's efficacy in evolving protein-protein interactions and antibody variants.
  • To enhance the applicability of continuous evolution to a broader range of proteins.

Main Methods:

  • Development of periplasmic phage-assisted continuous evolution (pPACE) in the E. coli periplasm.
  • Application of pPACE to evolve interactions in YibK protein and an anti-GCN4 antibody mutant.
  • Implementation of an intein-mediated selection for soluble periplasmic expression.
  • Evolution of disulfide-containing trastuzumab antibody variants for improved Her2 binding and expression.

Main Results:

  • pPACE successfully evolved novel noncovalent and covalent interactions in YibK protein.
  • A binding-defective antibody mutant was corrected using pPACE.
  • Intein-mediated selection increased soluble antibody expression eight-fold.
  • Evolved trastuzumab variants showed enhanced binding to a Her2-like peptide and improved soluble expression.

Conclusions:

  • pPACE enables continuous evolution in a disulfide-compatible E. coli periplasmic environment.
  • The system rapidly optimizes proteins with disulfide bonds, including antibodies.
  • pPACE significantly broadens the scope of continuous evolution for protein engineering.