A recombinant, fully human monoclonal antibody with antitumor activity constructed from phage-displayed antibody fragments

G. Huls, I.A.F.M. Heijnen, M.E. Cuomo, J.C. Koningsberger, L.J. Wiegman, E. Boel, A.R. van der Vuurst de Vries, S.A.J. Loyson, W. Helfrich, G.P. van Berge Henegouwen, M. van Meijer, C.A. de Kruif, T. Logtenberg

Research output: Contribution to journalArticleAcademicpeer-review

81 Citations (Scopus)

Abstract

A single-chain Fv antibody fragment specific for the tumor-associated Ep-CAM molecule was isolated from a semisynthetic phage display library and converted into an intact, fully human IgG1 monoclonal antibody (huMab). The purified huMab had an affinity of 5 nM and effectively mediated tumor cell killing in in vitro and in vivo assays. These experiments show that nonimmunized phage antibody display libraries can be used to obtain high- affinity, functional, and clinically applicable huMabs directed against a tumor-associated antigen.

Original languageEnglish
Pages (from-to)276-281
Number of pages6
JournalNature Biotechnology
Volume17
Issue number3
DOIs
Publication statusPublished - 1999

Keywords

  • Ep-CAM
  • Immunotherapy
  • Phage display
  • Recombinant antibodies
  • Single-chain Fv

Fingerprint

Dive into the research topics of 'A recombinant, fully human monoclonal antibody with antitumor activity constructed from phage-displayed antibody fragments'. Together they form a unique fingerprint.

Cite this