Protein cell-surface display through in situ enzymatic modification of proteins with a poly(Ethylene glycol)-lipid

Urara Tomita, Satoshi Yamaguchi, Yasukazu Maeda, Kazuki Chujo, Kosuke Minamihata, Teruyuki Nagamune

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

Cell-surface display of functional proteins is a powerful and useful tool for regulating and reinforcing cellular functions. Direct incorporation of site-specifically lipidated proteins from the extracellular medium is more rapid, easily controllable and reliable in displaying active proteins than expression through gene transfer. However, undesirable amphiphilic reagents such as organic co-solvents and detergents were required for suppressing aggregation of ordinary lipidated proteins in solution. We report here sortase A-catalyzed modification of proteins with a poly(ethylene glycol)(PEG)-lipid in situ on the surface of living cells. Proteins fused with a recognition tag were site-specifically ligated with the PEG-lipid which was preliminary incorporated into cell membranes. Accordingly, target proteins were successfully displayed on living cells without aggregation under an amphiphilic reagent-free condition. Furthermore, to demonstrate the availability of the present method, Fc domains of immunoglobulin G were displayed on cancer cells, and the phagocytosis of cancer cells with dendritic cells were enhanced through the Fc-Fc receptor interaction. Thus, the present facile chemoenzymatic method for protein display can be utilized for modulating cell-cell interactions in cell and tissue engineering fields.

Original languageEnglish
Pages (from-to)2785-2789
Number of pages5
JournalBiotechnology and Bioengineering
Volume110
Issue number10
DOIs
Publication statusPublished - Oct 2013
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

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