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Frameshifting in the p6 cDNA phage display system.

Cindy Govarts1, Klaartje Somers, Piet Stinissen

  • 1Biomedical Research Institute, School of Life Sciences, Transnationale Universiteit Limburg and Hasselt University, Diepenbeek, Belgium. veerle.somers@uhasselt.be.

Molecules (Basel, Switzerland)
|December 22, 2010
PubMed
Summary

Phage display allows target identification using ligands. This study shows that C-terminal fusion to phage coat protein p6 can also cause frameshifting, enabling target display in multiple reading frames.

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Area of Science:

  • Molecular Biology
  • Biotechnology
  • Protein Engineering

Background:

  • Phage display is a versatile technique for identifying ligands and their targets.
  • Targets are typically displayed as fusion proteins on the phage surface.
  • Previous studies noted frameshifting in N-terminal phage display, leading to unexpected target enrichment.

Purpose of the Study:

  • To investigate if C-terminal fusion to phage coat protein p6 is susceptible to frameshifting.
  • To determine if frameshifting occurs during the expression of C-terminal fusion proteins in phage display.

Main Methods:

  • Utilized phage display with C-terminal fusion of cDNA fragments to phage coat protein p6.
  • Selected an enriched target lacking an open reading frame.
  • Coupled an E-tag to the C-terminus for display measurement.

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  • Expressed the construct in three different reading frames to assess frameshifting.

    • Main Results:

    • Demonstrated successful display of the target in both the 0 and +1 reading frames.
    • Confirmed that frameshifting occurs with C-terminal fusion to the minor coat protein p6.
    • Indicated that this phenomenon is not limited to N-terminal display strategies.

    Conclusions:

    • C-terminal fusion to phage coat protein p6 can induce frameshifting.
    • Frameshifting in phage display expands the repertoire of displayed targets.
    • This finding has implications for optimizing target selection in phage display applications.