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

Autor: Marie-Anne Petit, Nicolas Tarbouriech, Mohammed Habib, Catherine Fallecker, Emmanuel Drouet
Přispěvatelé: Thomas, Frank, Unit of Virus Host Cell Interactions (UVHCI), Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS)
Rok vydání: 2013
Předmět:
[SDV.BBM.BS] Life Sciences [q-bio]/Biochemistry
Molecular Biology/Structural Biology [q-bio.BM]
medicine.drug_class
Biophysics
Antibody engineering
Hepacivirus
Monoclonal antibody
Biochemistry
Single chain Fv fragment
Epitope
Immunoglobulin G
MESH: Antibodies
Monoclonal
law.invention
E1E2
Viral Proteins
03 medical and health sciences
0302 clinical medicine
Antigen
Structural Biology
law
Escherichia coli
Genetics
medicine
MESH: Hepacivirus
Anti-HCV therapy
Molecular Biology
030304 developmental biology
MESH: Single-Chain Antibodies
0303 health sciences
biology
MESH: Escherichia coli
Hepatitis C virus
Chemistry
Antibodies
Monoclonal
Computational Biology
Cell Biology
MESH: Viral Proteins
Virology
Molecular biology
3. Good health
[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Biomolecules [q-bio.BM]
Recombinant DNA
biology.protein
030211 gastroenterology & hepatology
Antibody
Single-Chain Antibodies
MESH: Computational Biology
Conformational epitope
Zdroj: FEBS Letters
FEBS Letters, Wiley, 2013, 587 (20), pp.3335-40
ISSN: 0014-5793
1873-3468
Popis: International audience; 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.
Databáze: OpenAIRE
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