Site directed biotinylation of filamentous phage structural proteins

Larisa Smelyanski; Jonathan M. Gershoni

doi:10.1186/1743-422X-8-495

Site directed biotinylation of filamentous phage structural proteins

Larisa Smelyanski, Jonathan M. Gershoni^*

^*Corresponding author for this work

Department of Cell Research and Immunology

Research output: Contribution to journal › Article › peer-review

Abstract

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.

Original language	English
Article number	495
Journal	Virology Journal
Volume	8
DOIs	https://doi.org/10.1186/1743-422X-8-495
State	Published - 2011

Keywords

biotinylation
combinatorial libraries
filamentous bacteriophage
phage display

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1186/1743-422X-8-495

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abstract = "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.",

keywords = "biotinylation, combinatorial libraries, filamentous bacteriophage, phage display",

author = "Larisa Smelyanski and Gershoni, {Jonathan M.}",

note = "Funding Information: This study was supported by the Israel Science Foundation. The authors wish to thank Dr. David Enshell-Seijffers, Dr. Elena Paley, Anna Roitburd-Berman for their comments and assistance in preparation of this manuscript. The authors wish to thank Dr. Peter Kraus for his generous support of this research. This article is in memory of Nicolai Smelyanski.",

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doi = "10.1186/1743-422X-8-495",

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AU - Smelyanski, Larisa

AU - Gershoni, Jonathan M.

N1 - Funding Information: This study was supported by the Israel Science Foundation. The authors wish to thank Dr. David Enshell-Seijffers, Dr. Elena Paley, Anna Roitburd-Berman for their comments and assistance in preparation of this manuscript. The authors wish to thank Dr. Peter Kraus for his generous support of this research. This article is in memory of Nicolai Smelyanski.

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Y1 - 2011

N2 - 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.

AB - 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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Site directed biotinylation of filamentous phage structural proteins

Abstract

Keywords

UN SDGs

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