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Hepatitis is an inflammatory condition of the liver most commonly caused by hepatotropic viruses (A–E), though non-infectious causes such as alcohol and drugs also exist.Hepatitis AHepatitis A virus (HAV) is a non-enveloped RNA virus of the Picornaviridae family. It is primarily transmitted via the fecal-oral route, typically through ingestion of contaminated food or water. After ingestion, HAV enters the bloodstream through the oropharynx or intestinal epithelium and reaches the liver. The...

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Related Experiment Video

Updated: Jun 27, 2026

Two Methods of Heterokaryon Formation to Discover HCV Restriction Factors

Two Methods of Heterokaryon Formation to Discover HCV Restriction Factors

Published on: July 16, 2012

Mapping Determinants of Hepatitis C Virus E1/E2 Transmembrane Interactions Using Intergenotypic Chimeras.

Margherita Fanalista^1,2, Christina Holmboe Olesen^1,2, Rodrigo Velázquez-Moctezuma^1,2,3

¹Copenhagen Hepatitis C Program (CO-HEP), Department of Infectious Diseases, Copenhagen University Hospital, 2650 Hvidovre, Denmark.

|June 26, 2026

Summary

Investigating Hepatitis C virus (HCV) transmembrane regions revealed their critical role in viral infectivity. Adaptive mutations in E1/E2 regions are key for recovery, informing future HCV vaccine development.

Keywords:

E1/E2 glycoproteins HCV glycoprotein assembly membrane interactions transmembrane domains viral entry

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Last Updated: Jun 27, 2026

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Published on: May 10, 2022

Area of Science:

Virology
Molecular Biology
Immunology

Background:

Hepatitis C virus (HCV) poses a significant global health challenge with no available preventive vaccine.
The E1/E2 envelope glycoproteins complex is crucial for viral entry, but its assembly and stability mechanisms are not fully understood.

Purpose of the Study:

To investigate the role of E1/E2 transmembrane (TM) regions in HCV infectivity.
To explore the impact of swapping TM domains between different HCV genotypes on viral function.

Main Methods:

Constructed chimeric HCV recombinants by swapping C-terminal TM domains (TME1, TME2, TME1E2) of E1/E2 glycoproteins between different genotypes (H77, S52, J6).
Assessed infectivity of TM-swap chimeras and analyzed adaptive mutations following serial passaging.
Investigated the effect of extending TME1 swaps and including internal E1 TM regions (iTME1).

Main Results:

Most TM-swap chimeras exhibited reduced infectivity.
Serial passaging led to partial infectivity recovery through adaptive mutations in E1/E2, including TM, stem, and iTME1 regions.
Extending TME1 swaps improved infectivity in some cases, while iTME1 inclusion abolished it.

Conclusions:

HCV E1/E2 transmembrane regions and associated membrane-proximal domains significantly influence viral infectivity.
Functional interactions exist between membrane-associated regions and ectodomains of E1/E2.
Findings are relevant for developing E1/E2-based HCV vaccines.