Single-domain antibodies that compete with the natural ligand fibroblast growth factor block the internalization of the fibroblast growth factor receptor 1

Gianluca Veggiani, Giuseppe Ossolengo, Marisa Aliprandi, Ugo Cavallaro, Ario de Marco

Research output: Contribution to journalArticle

Abstract

Single-domain antibodies in VHH format specific for fibroblast growth factor receptor 1 (FGFR1) were isolated from a phage-display llama naïve library. In particular, phage elution in the presence of the natural receptor ligand fibroblast growth factor (FGF) allowed for the identification of recombinant antibodies that compete with FGF for the same region on the receptor surface. These antibodies posses a relatively low affinity for FGFR1 and were never identified when unspecific elution conditions favoring highly affine binders were applied to panning procedures. Two populations of competitive antibodies were identified that labeled specifically the receptor-expressing cells in immunofluorescence and recognize distinct epitopes. Antibodies from both populations effectively prevented FGF-dependent internalization and nuclear accumulation of the receptor in cultured cells. This achievement indicates that these antibodies have a capacity to modulate the receptor physiology and, therefore, constitute powerful reagents for basic research and a potential lead for therapeutic applications.

Original languageEnglish
Pages (from-to)692-696
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume408
Issue number4
DOIs
Publication statusPublished - May 20 2011

Keywords

  • Competitive elution
  • Fibroblast growth factor receptor 1
  • Llama VHH
  • MCF7 cells
  • Receptor internalization
  • Single-domain antibodies

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Molecular Biology

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