Structural and functional characterization of the single-chain Fv fragment from a unique HCV E1E2-specific monoclonal antibody. - Université Grenoble Alpes Accéder directement au contenu
Article Dans Une Revue FEBS Letters Année : 2013

Structural and functional characterization of the single-chain Fv fragment from a unique HCV E1E2-specific monoclonal antibody.

Résumé

The nucleotide sequence of the unique neutralizing monoclonal antibody D32.10 raised against a conserved conformational epitope shared between E1 and E2 on the serum-derived hepatitis C virus (HCV) envelope was determined. Subsequently, the recombinant single-chain Fv fragment (scFv) was cloned and expressed in Escherichia coli, and its molecular characterization was assessed using multi-angle laser light scattering. The scFv mimicked the antibody in binding to the native serum-derived HCV particles from patients, as well as to envelope E1E2 complexes and E1, E2 glycoproteins carrying the viral epitope. The scFv D32.10 competed with the parental IgG for binding to antigen, and therefore could be a promising candidate for therapeutics and diagnostics.
Fichier non déposé

Dates et versions

hal-01243601 , version 1 (15-12-2015)

Identifiants

  • HAL Id : hal-01243601 , version 1
  • PUBMED : 24021643

Citer

Catherine Fallecker, Nicolas Tarbouriech, Mohammed Habib, Marie-Anne Petit, Emmanuel Drouet. Structural and functional characterization of the single-chain Fv fragment from a unique HCV E1E2-specific monoclonal antibody.. FEBS Letters, 2013, 587 (20), pp.3335-40. ⟨hal-01243601⟩
42 Consultations
0 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More