SEARCH

SEARCH BY CITATION

Figure S1. Schematic representation of the HCV E1 glycoprotein domains and amino acid conservation in the internal hydrophobic domain. (A) The N-terminal ~160 amino acids make up the ectodomain (Ecto), which contains 8 conserved Cys residues ( | ), believed to form 4 intramolecular disulfide bonds, and up to 5 glycosylation sites (?). The C-terminal ~30 amino acids comprise the transmembrane domain known to be involved in heterodimerization with E2 (6), membrane anchoring (51), and ER retention (52, 53). The internal hydrophobic domain (aa262-290 underlined; numbering beginning from the first amino acid in Core) is proposed to function as the fusion peptide (FP) (13), and its amino acid sequence is shown below. Note that the amino acid designation for the internal hydrophobic domain varies between reports (14). Asterisks denote amino acids mutated in this study, and a putative discontinuous heptad repeat (aa262-289) is labeled with the classical a/d designation. (B) Amino acid conservation within 389 HCV E1 internal hydrophobic domain sequences listed in the Los Alamos HCV Sequence Database is shown with residue numbers on the x-axis. The consensus sequence is shown at the bottom and is represented by the lowermost (black) bars with percentage of other amino acids present at a given position stacked by descending prevalence. Amino acids present in less than 5% of all sequences analyzed were grouped together (uppermost bar). Note that the boxed amino acids (residues 270, 275, and 288) are present in the E1 glycoprotein used in this study and differ from the consensus.

Please note: Wiley-Blackwell are not responsible for the content or functionality of any supporting materials supplied by the authors. Any queries (other than missing material) should be directed to the corresponding author for the article.

FilenameFormatSizeDescription
JVH_1111_sm_Suppl_text.doc112KSupporting info item

Please note: Wiley Blackwell is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.