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Carl B

Carl Borrebaeck

Professor

Carl B

Modulation of the CD40-CD40 ligand interaction using human anti-CD40 single-chain antibody fragments obtained from the n-CoDeR phage display library

Author

  • Peter Ellmark
  • Camilla Ottosson
  • Carl Borrebaeck
  • Ann-Christin Malmborg Hager
  • Christina Furebring

Summary, in English

CD40 plays a central regulatory role in the immune system and antibodies able to modulate CD40 signalling may consequently have a potential in immunotherapy, in particular for treatment of lymphomas and autoimmune disease like multiple sclerosis. As a first step to achieve this goal, we describe the selection and characterization of a novel set of fully human anti-CD40 antibody fragments (scFv) from a phage display library (n-CoDeR). In order to determine their biological potential, these antibody fragments have been analysed for their ability to promote B-cell activation, rescue from apoptosis and to block the CD40-CD40 ligand (CD40L) interaction. The selected cohort of human scFv could be subcategorized, each expressing a distinct functional signature. Thus scFv were generated that induced B-cell proliferation, rescued B cells from apoptosis and blocked the CD40-CD40L interaction to different extents. In particular, one of the scFv clones (F33) had the ability to abrogate completely this interaction. The epitope recognition patterns as well as individual rate constants were also determined and the affinity was shown to vary from low to high nanomolar range. In conclusion, this panel of human anti-CD40 scFv fragments displays a number of distinct properties, which may constitute a valuable source when evaluating candidates for in vivo trials.

Department/s

  • Department of Immunotechnology

Publishing year

2002

Language

English

Pages

456-463

Publication/Series

Immunology

Volume

106

Issue

4

Document type

Journal article

Publisher

Wiley-Blackwell

Topic

  • Immunology in the medical area

Status

Published

ISBN/ISSN/Other

  • ISSN: 0019-2805