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Updated: Aug 12, 2026

Two Methods of Heterokaryon Formation to Discover HCV Restriction Factors
Published on: July 16, 2012
Proteomics computational analyses suggest that hepatitis C virus E1 and pestivirus E2 envelope glycoproteins are
Robert F Garry1, Srikanta Dash
1Department of Microbiology and Immunology, Tulane University Health Sciences Center, New Orleans, LA 70112, USA. rfgarry@tulane.edu
Abstract:
Class II fusion proteins encoded by tick-borne encephalitis virus (TBEV), dengue virus, and Semliki Forest virus have a fusion peptide located at the end of a rod-like molecule comprised of three antiparallel beta sheet domains. Proteomics computational analyses suggest that hepatitis C virus (HCV) envelope glycoprotein E1 and pestivirus envelope glycoprotein E2 are truncated class II fusion proteins. Similarities were also detected between the receptor-binding portion of TBEV E and HCV E2, and between TBEV small membrane protein precursor prM and pestivirus E1. The proposed models of Flaviviridae envelope proteins can facilitate drug and vaccine development.
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