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Journal of General Virology (2000), 81, 2451-2459.
© 2000 Society for General Microbiology

Animal: RNA Viruses

Recombinant human monoclonal antibodies against different conformational epitopes of the E2 envelope glycoprotein of hepatitis C virus that inhibit its interaction with CD81

Tobias Allander1,2, Katarina Drakenberg1, Aster Beyene1, Domenico Rosa3, Sergio Abrignani3, Michael Houghton4, Anders Widell5, Lena Grillner2 and Mats A. A. Persson1

Karolinska Institute, Department of Medicine1 and Department of Laboratory Medicine2, Center for Molecular Medicine (L8:01), Karolinska Hospital, S-171 76 Stockholm, Sweden
Chiron-Biocine, IRIS, Siena, Italy3
Chiron Corporation, Department of Virology, Emeryville, CA, USA4
Lund University, Department of Clinical Microbiology, Malmö University Hospital, Malmö, Sweden5

Author for correspondence: Mats Persson. Fax +46 8 5177 61 80. e-mail Mats.Persson{at}cmm.ki.se

The antibody response to the envelope proteins of hepatitis C virus (HCV) may play an important role in controlling the infection. To allow molecular analyses of protective antibodies, we isolated human monoclonal antibodies to the E2 envelope glycoprotein of HCV from a combinatorial Fab library established from bone marrow of a chronically HCV-infected patient. Anti-E2 reactive clones were selected using recombinant E2 protein. The bone marrow donor carried HCV genotype 2b, and E2 used for selection was of genotype 1a. The antibody clones were expressed as Fab fragments in E. coli, and as Fab fragments and IgG1 in CHO cells. Seven different antibody clones were characterized, and shown to have high affinity for E2, genotype 1a. Three clones also had high affinity for E2 of genotype 1b. They all bind to conformation-dependent epitopes. Five clones compete for the same or overlapping binding sites, while two bind to one or two other epitopes of E2. Four clones corresponding to the different epitopes were tested as purified IgG1 for blocking the CD81–E2 interaction in vitro; all four were positive at 0·3–0·5  µg/ml. Thus, the present results suggest the existence of at least two conserved epitopes in E2 that mediate inhibition of the E2–CD81 interaction, of which one appeared immunodominant in this donor.




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