Author information

• ¹Institute of Virology, Hannover Medical School, Hannover, Germany.
• ²Institute of Virology, Hannover Medical School, Hannover, Germany; Center of Structural and Cell Biology in Medicine, Institute of Biochemistry, University of Lübeck, Lübeck, Germany; German Center for Infection Research (DZIF) partner site Hamburg-Lübeck-Borstel-Riems, Germany; Cluster of Excellence RESIST (EXC 2155), Hannover Medical School, Hannover, Germany; Centre for Structural Systems Biology (CSSB), Hamburg, Germany. Electronic address: krey@biochem.uni-luebeck.de.

Abstract

Inspite of the available antiviral therapy, hepatitis C virus (HCV) remains a global health burden and a prophylactic vaccine would help to eliminate the risk to develop chronic liver diseases. Structural insights into the function of the glycoproteins E1 and E2 in virus entry and the interplay with the host's humoral immune response are key for informed vaccine development. We review recently reported structural insights into receptor binding of HCV glycoproteins and the assembly of an intact membrane-bound E1-E2 heterodimer. These data are used together with available functional data to draw a simplified model of virus entry, which highlights gaps in our current knowledge that warrant further research to fully understand this process at the atomic level.