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Journal of Virology, August 1999, p. 6235-6244, Vol. 73, No. 8
0022-538X/99/$04.00+0

Characterization of Hepatitis C Virus E2 Glycoprotein Interaction with a Putative Cellular Receptor, CD81

Mike Flint,1 Catherine Maidens,1 Larry D. Loomis-Price,2 Christine Shotton,1 Jean Dubuisson,3 Peter Monk,4 Adrian Higginbottom,4 Shoshana Levy,5 and Jane A. McKeating1,*

School of Animal & Microbial Sciences, University of Reading, Reading RG6 6AJ,1 and Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2UH,4 United Kingdom; Henry M. Jackson Foundation, Rockville, Maryland 208502; CNRS-UMR319, IBL/Institut Pasteur de Lille, 59021 Lille Cedex, France3; and Department of Medicine, Division of Oncology, Stanford Medical School, Stanford, California 943055

Received 9 February 1999/Accepted 20 April 1999

A truncated soluble form of the hepatitis C virus E2 glycoprotein, E2661, binds specifically to the surface of cells expressing human CD81 (hCD81) but not other members of the tetraspanin family (CD9, CD63, and CD151). No differences were noted between the level of E2661 binding to hCD81 expressed on the surface of rat RBL or KM3 cells compared to Daudi and Molt-4 cells, suggesting that additional human-cell-specific factors are not required for the primary interaction of E2 with the cell surface. E2 did not interact with African green monkey (AGM) CD81 on the surface of COS cells, which differs from the hCD81 sequence at four residues within the second extracellular region (EC2) (amino acids [aa] 163, 186, 188, and 196), suggesting that one or more of these residues defines the site of interaction with E2. Various recombinant forms of CD81 EC2 show differences in the ability to bind E2, suggesting that CD81 conformation is important for E2 recognition. Regions of E2 involved in the CD81 interaction were analyzed, and our data suggest that the binding site is of a conformational nature involving aa 480 to 493 and 544 to 551 within the E2 glycoprotein. Finally, we demonstrate that ligation of CD81 by E2661 induced aggregation of lymphoid cells and inhibited B-cell proliferation, demonstrating that E2 interaction with CD81 can modulate cell function.

* Corresponding author. Mailing address: School of Animal & Microbial Sciences, University of Reading, Reading RG6 6AJ, United Kingdom. Phone: (44) 1189 875 123, ext. 7892. Fax: (44) 1189 316 671. E-mail: j.a.mckeating{at}reading.ac.uk.

Journal of Virology, August 1999, p. 6235-6244, Vol. 73, No. 8
0022-538X/99/$04.00+0


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