Efficient killing of CD22+ tumor cells by a humanized diabody-RNase fusion protein

Biochem Biophys Res Commun. 2005 Jun 3;331(2):595-602. doi: 10.1016/j.bbrc.2005.03.215.

Abstract

We report on the generation of a dimeric immunoenzyme capable of simultaneously delivering two ribonuclease (RNase) effector domains on one molecule to CD22(+) tumor cells. As targeting moiety a diabody derived from the previously humanized scFv SGIII with grafted specificity of the murine anti-CD22 mAb RFB4 was constructed. Further engineering the interface of this construct (V(L)36(Leu-->Tyr)) resulted in a highly robust bivalent molecule that retained the same high affinity as the murine mAb RFB4 (K(D)=0.2 nM). A dimeric immunoenzyme comprising this diabody and Rana pipiens liver ribonuclease I (rapLRI) was generated, expressed as soluble protein in bacteria, and purified to homogeneity. The dimeric fusion protein killed several CD22(+) tumor cell lines with high efficacy (IC(50)=3-20 nM) and exhibited 9- to 48-fold stronger cytotoxicity than a monovalent rapLRI-scFv counterpart. Our results demonstrate that engineering of dimeric antibody-ribonuclease fusion proteins can markedly enhance their biological efficacy.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Antibodies, Monoclonal / chemistry
  • Antibodies, Monoclonal / genetics
  • Antibodies, Monoclonal / immunology*
  • Antibodies, Monoclonal / isolation & purification
  • Antibody Specificity
  • Antigens, CD / immunology*
  • Antigens, CD / metabolism
  • Antigens, Differentiation, B-Lymphocyte / immunology*
  • Antigens, Differentiation, B-Lymphocyte / metabolism
  • Cell Adhesion Molecules / immunology*
  • Cell Adhesion Molecules / metabolism
  • Cell Death
  • Cell Line, Tumor
  • Cell Survival
  • Cytotoxicity, Immunologic*
  • Dimerization
  • Humans
  • Immunoglobulin Variable Region / chemistry
  • Immunoglobulin Variable Region / genetics
  • Immunoglobulin Variable Region / immunology
  • Inhibitory Concentration 50
  • Lectins / immunology*
  • Lectins / metabolism
  • Mice
  • Neoplasms / immunology*
  • Neoplasms / pathology*
  • Protein Structure, Quaternary
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / immunology
  • Recombinant Fusion Proteins / isolation & purification
  • Recombinant Fusion Proteins / metabolism*
  • Ribonucleases / chemistry
  • Ribonucleases / genetics
  • Ribonucleases / isolation & purification
  • Ribonucleases / metabolism*
  • Sensitivity and Specificity
  • Sialic Acid Binding Ig-like Lectin 2

Substances

  • Antibodies, Monoclonal
  • Antigens, CD
  • Antigens, Differentiation, B-Lymphocyte
  • CD22 protein, human
  • Cd22 protein, mouse
  • Cell Adhesion Molecules
  • Immunoglobulin Variable Region
  • Lectins
  • Recombinant Fusion Proteins
  • Sialic Acid Binding Ig-like Lectin 2
  • Ribonucleases