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

• DOI: 10.1128/jvi.73.8.6235-6244.1999
• Publication Date: 2019-12-31T18:35:55Z
• Authors: Mike Flint; Catherine Maidens; Larry D. Loomis-P...; Christine Shotton; Jean Dubuisson; Peter Monk; Adrian Higginbottom; Shoshana Levy; Jane A. McKeating
• Keywords: CD81; Tetraspanin

ABSTRACT A truncated soluble form of the hepatitis C virus E2 glycoprotein, 661 , binds specifically to surface cells expressing human CD81 (hCD81) but not other members tetraspanin family (CD9, CD63, and CD151). No differences were noted between level binding hCD81 expressed on rat RBL or KM3 compared Daudi Molt-4 cells, suggesting that additional human-cell-specific factors are required for primary interaction with cell surface. did interact African green monkey (AGM) COS which differs from sequence at four residues within second extracellular region (EC2) (amino acids [aa] 163, 186, 188, 196), one more these defines site E2. Various recombinant forms EC2 show in ability bind E2, conformation is important recognition. Regions involved analyzed, our data suggest a conformational nature involving aa 480 493 544 551 glycoprotein. Finally, we demonstrate ligation by induced aggregation lymphoid inhibited B-cell proliferation, demonstrating can modulate function.