Structural insights into hepatitis C virus neutralization

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...

Full description

Saved in:
Bibliographic Details
Published inCurrent opinion in virology Vol. 60; p. 101316
Main Authors Ströh, Luisa J., Krey, Thomas
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.06.2023
Subjects
Hepacivirus
Hepatitis C
Humans
Protein Binding
Viral Envelope Proteins - metabolism
Online AccessGet full text

Cover

More Information
Summary: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.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-3
content type line 23
ObjectType-Review-1
ISSN:1879-6257
1879-6265
DOI:10.1016/j.coviro.2023.101316