Escherichia coli inner membrane display system for high-throughput screening of dimeric proteins

Migyeong Jo, Bora Hwang, Hyun Woung Yoon, Sang Taek Jung

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)


Multimer formation is indispensable to the intrinsicbiologicalfunctions of many natural proteins. For example, the human immunoglobulin G (IgG) antibody has two variable regions (heavy chain variable domain [VH] and light chain variable domain [VL]) that must be assembled for specific antigen binding, and homodimerization of the antibody's Fc domain is essential for eliciting therapeutic effector functions. For the more efficient high-throughput directed evolution of multimeric proteins with ease of cultivation and handling, here we report a membrane protein drift and assembly (MPDA) system, in which a multimeric protein is displayed on a bacterial inner membrane by drifting and auto-assembling membrane-anchored subunit polypeptides. This system enabled the auto-assembly of membrane-tethered Fv domains (VH and VL) or the monomeric Fc domain into a functional hetero- or homodimeric protein complex on the bacterial inner membrane. This system could also be used to enrich a desired engineered Fc variant from a mixture containing a million-fold excess of wild-type Fc domain, indicating the applicability of the MPDA system for the high-throughput directed evolution of a variety of multimeric proteins, such as cytokines, enzymes, or structural proteins.

Original languageEnglish
Pages (from-to)2849-2858
Number of pages10
JournalBiotechnology and Bioengineering
Issue number12
Publication statusPublished - 2018 Dec
Externally publishedYes


  • antibody
  • bacterial display
  • directed evolution
  • library screening
  • multimeric protein

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology


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