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

Bacteriophage lambda (λ) 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 λ display systems. Here we describe a nov...

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Detalles Bibliográficos
Autores principales: Zanghi, Christine N., Lankes, Heather A., Bradel-Tretheway, Birgit, Wegman, Jessica, Dewhurst, Stephen
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2005
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1258178/
https://www.ncbi.nlm.nih.gov/pubmed/16224099
http://dx.doi.org/10.1093/nar/gni158
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author Zanghi, Christine N.
Lankes, Heather A.
Bradel-Tretheway, Birgit
Wegman, Jessica
Dewhurst, Stephen
author_facet Zanghi, Christine N.
Lankes, Heather A.
Bradel-Tretheway, Birgit
Wegman, Jessica
Dewhurst, Stephen
author_sort Zanghi, Christine N.
collection PubMed
description Bacteriophage lambda (λ) 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 λ display systems. Here we describe a novel, plasmid-based expression system in which gpD deficient λ 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 λ and to facilitate the use of modified λ phage vectors in mammalian gene transfer applications.
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spelling pubmed-12581782005-10-24 A simple method for displaying recalcitrant proteins on the surface of bacteriophage lambda Zanghi, Christine N. Lankes, Heather A. Bradel-Tretheway, Birgit Wegman, Jessica Dewhurst, Stephen Nucleic Acids Res Methods Online Bacteriophage lambda (λ) 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 λ display systems. Here we describe a novel, plasmid-based expression system in which gpD deficient λ 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 λ and to facilitate the use of modified λ phage vectors in mammalian gene transfer applications. Oxford University Press 2005 2005-10-13 /pmc/articles/PMC1258178/ /pubmed/16224099 http://dx.doi.org/10.1093/nar/gni158 Text en © The Author 2005. Published by Oxford University Press. All rights reserved
spellingShingle Methods Online
Zanghi, Christine N.
Lankes, Heather A.
Bradel-Tretheway, Birgit
Wegman, Jessica
Dewhurst, Stephen
A simple method for displaying recalcitrant proteins on the surface of bacteriophage lambda
title A simple method for displaying recalcitrant proteins on the surface of bacteriophage lambda
title_full A simple method for displaying recalcitrant proteins on the surface of bacteriophage lambda
title_fullStr A simple method for displaying recalcitrant proteins on the surface of bacteriophage lambda
title_full_unstemmed A simple method for displaying recalcitrant proteins on the surface of bacteriophage lambda
title_short A simple method for displaying recalcitrant proteins on the surface of bacteriophage lambda
title_sort simple method for displaying recalcitrant proteins on the surface of bacteriophage lambda
topic Methods Online
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1258178/
https://www.ncbi.nlm.nih.gov/pubmed/16224099
http://dx.doi.org/10.1093/nar/gni158
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