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Nucleic Acids Research 2005 33(18):e160; doi:10.1093/nar/gni158
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Published online 13 October 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oxfordjournals.org

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A simple method for displaying recalcitrant proteins on the surface of bacteriophage lambda

Christine N. Zanghi1, Heather A. Lankes1, Birgit Bradel-Tretheway1, Jessica Wegman1 and Stephen Dewhurst1,2,*

1Department of Microbiology and Immunology, University of Rochester Medical Center 601 Elmwood Avenue, Box 672, Rochester, NY 14642, USA 2Cancer Center, University of Rochester School of Medicine and Dentistry Rochester, NY 14642, USA

*To whom correspondence should be addressed. Tel: +1 585 275 3216; Fax: +1 585 473 2361; Email: Stephen_Dewhurst{at}urmc.rochester.edu

Received June 20, 2005. Revised August 11, 2005. Accepted September 24, 2005.

Bacteriophage lambda ({lambda}) permits the display of many foreign peptides and proteins on the gpD major coat protein. However, some recombinant derivatives of gpD are incompatible with the assembly of stable phage particles. This presents a limitation to current {lambda} display systems. Here we describe a novel, plasmid-based expression system in which gpD deficient {lambda} lysogens can be co-complemented with both wild-type and recombinant forms of gpD. This dual expression system permits the generation of mosaic phage particles that contain otherwise recalcitrant recombinant gpD fusion proteins. Overall, this improved gpD display system is expected to permit the expression of a wide variety of peptides and proteins on the surface of bacteriophage {lambda} and to facilitate the use of modified {lambda} phage vectors in mammalian gene transfer applications.

The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors


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C. N. Zanghi, R. Sapinoro, B. Bradel-Tretheway, and S. Dewhurst
A tractable method for simultaneous modifications to the head and tail of bacteriophage lambda and its application to enhancing phage-mediated gene delivery
Nucleic Acids Res., April 3, 2007; 35(8): e59 - e59.
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