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Updated: May 9, 2025

Protein Engineering by Yeast Surface Display
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[Fundamental Research into Enhancing Fab Functionality by Protein Engineering].

Hitomi Nakamura1

  • 1Faculty of Pharmaceutical Sciences, Sojo University.

Yakugaku Zasshi : Journal of the Pharmaceutical Society of Japan
|April 30, 2025
PubMed
Summary

Protein engineering enhanced antibody fragments (Fabs) for improved therapeutic use. Modifications increased serum half-life and reduced aggregation and immunogenicity, creating safer, more functional Fabs.

Keywords:
aggregationantigen-binding fragment (Fab)disulfide bondglycosylationthermal stability

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Area of Science:

  • Biotechnology
  • Protein Engineering
  • Immunology

Background:

  • Antigen-binding fragments (Fabs) are crucial in therapeutic antibody formats.
  • Enhancing Fab functionality is key to improving their therapeutic utility.

Purpose of the Study:

  • To engineer Fabs for improved functionality, increased serum half-life, and reduced immunogenicity.
  • To develop a robust Pichia pastoris expression system for recombinant Fabs.

Main Methods:

  • Constructed a Pichia pastoris expression system for efficient recombinant Fab production.
  • Engineered a Fab mutant with a shifted interchain disulfide bond for site-directed PEGylation.
  • Introduced an N-glycosylation site (H: L178N) into the Fab heavy chain.

Main Results:

  • Achieved efficient recombinant Fab preparation in P. pastoris.
  • PEGylated Fabs demonstrated increased serum half-life.
  • N-glycosylation inhibited Fab aggregation and reduced immunogenicity compared to wild-type Fabs.

Conclusions:

  • Protein engineering strategies successfully enhanced Fab functionality and safety.
  • Modified Fabs exhibit increased therapeutic potential due to improved pharmacokinetics and reduced adverse effects.
  • These findings support the design of advanced Fab-based therapeutics.