Site directed biotinylation of filamentous phage structural proteins

Filamentous bacteriophages have been used in numerous applications for the display of antibodies and random peptide libraries. Here we describe the introduction of a 13 amino acid sequence LASIFEAQKIEWR (designated BT, which is biotinylated in vivo by E. coli) into the N termini of four of the five...

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Detalles Bibliográficos
Autores principales: Smelyanski, Larisa, Gershoni, Jonathan M
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2011
Materias:
Methodology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3256129/
https://www.ncbi.nlm.nih.gov/pubmed/22044460
http://dx.doi.org/10.1186/1743-422X-8-495
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author Smelyanski, Larisa
Gershoni, Jonathan M
author_facet Smelyanski, Larisa
Gershoni, Jonathan M
author_sort Smelyanski, Larisa
collection PubMed
description Filamentous bacteriophages have been used in numerous applications for the display of antibodies and random peptide libraries. Here we describe the introduction of a 13 amino acid sequence LASIFEAQKIEWR (designated BT, which is biotinylated in vivo by E. coli) into the N termini of four of the five structural proteins of the filamentous bacteriophage fd (Proteins 3, 7, 8 and 9). The in vivo and in vitro biotinylation of the various phages were compared. The production of multifunctional phages and their application as affinity reagents are demonstrated.
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spelling pubmed-32561292012-01-12 Site directed biotinylation of filamentous phage structural proteins Smelyanski, Larisa Gershoni, Jonathan M Virol J Methodology Filamentous bacteriophages have been used in numerous applications for the display of antibodies and random peptide libraries. Here we describe the introduction of a 13 amino acid sequence LASIFEAQKIEWR (designated BT, which is biotinylated in vivo by E. coli) into the N termini of four of the five structural proteins of the filamentous bacteriophage fd (Proteins 3, 7, 8 and 9). The in vivo and in vitro biotinylation of the various phages were compared. The production of multifunctional phages and their application as affinity reagents are demonstrated. BioMed Central 2011-11-01 /pmc/articles/PMC3256129/ /pubmed/22044460 http://dx.doi.org/10.1186/1743-422X-8-495 Text en Copyright ©2011 Smelyanski and Gershoni; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Methodology
Smelyanski, Larisa
Gershoni, Jonathan M
Site directed biotinylation of filamentous phage structural proteins
title Site directed biotinylation of filamentous phage structural proteins
title_full Site directed biotinylation of filamentous phage structural proteins
title_fullStr Site directed biotinylation of filamentous phage structural proteins
title_full_unstemmed Site directed biotinylation of filamentous phage structural proteins
title_short Site directed biotinylation of filamentous phage structural proteins
title_sort site directed biotinylation of filamentous phage structural proteins
topic Methodology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3256129/
https://www.ncbi.nlm.nih.gov/pubmed/22044460
http://dx.doi.org/10.1186/1743-422X-8-495
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