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Journal of Virology, September 2007, p. 9584-9590, Vol. 81, No. 17
0022-538X/07/$08.00+0     doi:10.1128/JVI.02782-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Expression and Characterization of a Minimal Hepatitis C Virus Glycoprotein E2 Core Domain That Retains CD81 Binding{triangledown}

Kathleen McCaffrey, Irene Boo, Pantelis Poumbourios, and Heidi E. Drummer*

Macfarlane Burnet Institute for Medical Research and Public Health, 85 Commercial Rd., Melbourne, Australia 3004

Received 17 December 2006/ Accepted 13 June 2007

The hepatitis C virus glycoprotein E2 receptor-binding domain is encompassed by amino acids 384 to 661 (E2661) and contains two hypervariable sequences, HVR1 and HVR2. E2 sequence comparisons revealed a third variable region, located between residues 570 and 580, that varies widely between genotypes, designated here as igVR, the intergenotypic variable region. A secreted E2661 glycoprotein with simultaneous deletions of the three variable sequences retained its ability to bind CD81 and conformation-dependent monoclonal antibodies (MAbs) and displayed enhanced binding to a neutralizing MAb directed to E2 immunogenic domain B. Our data provide insights into the E2 structure by suggesting that the three variable regions reside outside a conserved E2 core.

* Corresponding author. Mailing address: Macfarlane Burnet Institute for Medical Research and Public Health, 85 Commercial Rd., Melbourne, Australia 3004. Phone: 613 92822179. Fax: 613 92822100. E-mail: hdrummer{at}burnet.edu.au

{triangledown} Published ahead of print on 20 June 2007.

Journal of Virology, September 2007, p. 9584-9590, Vol. 81, No. 17
0022-538X/07/$08.00+0     doi:10.1128/JVI.02782-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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