Communication to the Editor
Protein cell-surface display through in situ enzymatic modification of proteins with a poly(Ethylene glycol)-lipid
Article first published online: 26 APR 2013
Copyright © 2013 Wiley Periodicals, Inc.
Biotechnology and Bioengineering
Volume 110, Issue 10, pages 2785–2789, October 2013
How to Cite
Tomita, U., Yamaguchi, S., Maeda, Y., Chujo, K., Minamihata, K. and Nagamune, T. (2013), Protein cell-surface display through in situ enzymatic modification of proteins with a poly(Ethylene glycol)-lipid. Biotechnol. Bioeng., 110: 2785–2789. doi: 10.1002/bit.24933
- Issue published online: 24 AUG 2013
- Article first published online: 26 APR 2013
- Accepted manuscript online: 16 APR 2013 06:58AM EST
- Manuscript Accepted: 1 APR 2013
- Manuscript Revised: 27 MAR 2013
- Manuscript Received: 18 DEC 2012
- Japan MEXT (Ministry of Education, Culture, Sports, Science and Technology). Grant Number: 21760634
- Tella, Inc.
- Center for NanoBio Integration at The University of Tokyo
- protein display;
- PEG lipid;
- mammalian cell;
- Fc domain;
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. Biotechnol. Bioeng. 2013;110: 2785–2789. © 2013 Wiley Periodicals, Inc.