Biosynthetically lipid-modified human scFv fragments from phage display libraries as targeting molecules for immunoliposomes

FEBS Lett. 1996 Dec 16;399(3):232-6. doi: 10.1016/s0014-5793(96)01335-x.

Abstract

A human anti-CD22 single chain (sc) Fv antibody fragment from a synthetic phage antibody display library was biosynthetically lipid-tagged by using Escherichia coli lipoprotein sequences. The purified anti-CD22 scFv lipoprotein was incorporated into liposomes by detergent dilution. Anti-CD22 immunoliposomes were shown to bind specifically in a dose- and time-dependent manner to CD22+ cell lines and CD22+ B-lymphocytes present in freshly isolated samples of blood mononuclear cells. The immunoliposomes were demonstrated to accumulate in intracellular compartments. Biosynthetically lipid-tagged human scFv antibody fragments isolated from phage display libraries may facilitate the construction of immunoliposomes with improved properties.

MeSH terms

  • Antigens, CD / immunology
  • Antigens, Differentiation, B-Lymphocyte / immunology
  • Bacteriophages / genetics*
  • Binding Sites
  • Cell Adhesion Molecules*
  • Genetic Vectors
  • Humans
  • Immunoglobulin Fragments / chemistry
  • Immunoglobulin Fragments / genetics*
  • Kinetics
  • Lectins*
  • Lipids / chemistry*
  • Liposomes*
  • Sialic Acid Binding Ig-like Lectin 2

Substances

  • Antigens, CD
  • Antigens, Differentiation, B-Lymphocyte
  • CD22 protein, human
  • Cell Adhesion Molecules
  • Immunoglobulin Fragments
  • Lectins
  • Lipids
  • Liposomes
  • Sialic Acid Binding Ig-like Lectin 2
  • immunoglobulin Fv