Open AccessIdentification of the Hepatitis C Virus E2 Glycoprotein Binding Site on the Large Extracellular Loop of CD81
Author(s) -
Heidi E. Drummer,
Kirilee A. Wilson,
Pantelis Poumbourios
Publication year - 2002
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.76.21.11143-11147.2002
Subject(s) - cd81 , biology , glycoprotein , binding site , microbiology and biotechnology , plasma protein binding , extracellular , site directed mutagenesis , chimera (genetics) , virology , biochemistry , virus , hepatitis c virus , mutant , gene
The binding of hepatitis C virus glycoprotein E2 to the large extracellular loop (LEL) of CD81 has been shown to modulate human T-cell and NK cell activity in vitro. Using random mutagenesis of a chimera of maltose-binding protein and LEL residues 113 to 201, we have determined that the E2-binding site on CD81 comprises residues Ile(182), Phe(186), Asn(184), and Leu(162). These findings reveal an E2-binding surface of approximately 806 A(2) and potential target sites for the development of small-molecule inhibitors of E2 binding.