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PEDS Advance Access published online on October 9, 2007
Protein Engineering Design and Selection, doi:10.1093/protein/gzm044
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© The Author 2007. Published by Oxford University Press. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

Functional phage display of two murine {alpha}/ß T-cell receptors is strongly dependent on fusion format, mode and periplasmic folding assistance

G.Å. Løset1,4, E. Lunde1, B. Bogen2, O.H. Brekke3 and I. Sandlie1,4

1Department of Molecular Biosciences, University of Oslo, N-0316 Oslo, Norway 2Institute of Immunology, University of Oslo, N-0316 Oslo, Norway 3 Birkeland Innovation, N-0316 Oslo, Norway

4 To whom correspondence should be addressed. E-mail: g.a.loset{at}imbv.uio.no or inger.sandlie{at}imbv.uio.no

Phage display has been instrumental for the success of antibody (Ab) technology. The aim of the present study was to explore phage display of soluble T-cell receptors (TCRs). A library platform that supports engineering and selection of improved TCRs to be used as detection reagents for specific antigen presentation will be very useful. In such applications, high, equal and clone independent display levels are a prerequisite for ‘fair’ selection. Therefore, we explored how different pIII fusion formats and modes affected the display levels of two murine {alpha}/ß TCRs. Both are derived from T-cell clones associated with the MOPC315 myeloma model. The results show that the design of the pIII fusion particle significantly affects the subsequent display levels. Furthermore, successful display may be obtained both in phagemid and phage versions. Importantly, improvement of poor display can be achieved by over-expressing the periplasmic chaperone FkpA.

Keywords: FkpA/phage display/T-cell receptor

Received January 16, 2007; revised May 30, 2007; accepted July 6, 2007.


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