Site directed biotinylation of filamentous phage structural proteins

Larisa Smelyanski, Jonathan M. Gershoni*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

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 languageEnglish
Article number495
JournalVirology Journal
Volume8
DOIs
StatePublished - 2011

Funding

FundersFunder number
Israel Science Foundation

    Keywords

    • biotinylation
    • combinatorial libraries
    • filamentous bacteriophage
    • phage display

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