@article{2fa4f636b1c04494ab51ce3bfcb50cbf,
title = "Site directed biotinylation of filamentous phage structural proteins",
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.",
year = "2011",
doi = "10.1186/1743-422X-8-495",
language = "אנגלית",
volume = "8",
journal = "Virology Journal",
issn = "1743-422X",
publisher = "BioMed Central Ltd.",
}