Publications & Reports

Expression and characterization of a minimal hepatitis C virus glycoprotein E2 core domain that retains CD81 binding.

McCaffrey K, Boo I, Poumbourios P, Drummer HE
Macfarlane Burnet Institute for Medical Research and Public Health, 85 Commercial Rd., Melbourne, Australia.


The hepatitis C virus glycoprotein E2 receptor-binding domain is encompassed by amino acids 384 to 661 (E2(661)) 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 E2(661) 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.


  • Journal: Journal of Virology
  • Published: 01/09/2007
  • Volume: 81
  • Issue: 17
  • Pagination: 9584-9590


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