Site directed biotinylation of filamentous phage structural proteins

Virol J. 2011 Nov 1;8:495. doi: 10.1186/1743-422X-8-495.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Affinity Labels / chemistry
  • Amino Acid Sequence
  • Antibodies, Viral / immunology
  • Antibodies, Viral / isolation & purification
  • Antibodies, Viral / metabolism
  • Bacteriophage M13 / genetics
  • Bacteriophage M13 / isolation & purification
  • Bacteriophage M13 / metabolism*
  • Biotinylation
  • Escherichia coli / virology
  • Genetic Vectors
  • Molecular Sequence Data
  • Peptide Library
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / isolation & purification
  • Recombinant Fusion Proteins / metabolism*
  • Staining and Labeling
  • Transduction, Genetic
  • Viral Structural Proteins / genetics
  • Viral Structural Proteins / isolation & purification
  • Viral Structural Proteins / metabolism*

Substances

  • Affinity Labels
  • Antibodies, Viral
  • Peptide Library
  • Recombinant Fusion Proteins
  • Viral Structural Proteins