Proteomics computational analyses suggest that hepatitis C virus E1 and pestivirus E2 envelope glycoproteins are truncated class II fusion proteins

Virology. 2003 Mar 15;307(2):255-65. doi: 10.1016/s0042-6822(02)00065-x.

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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Classical Swine Fever Virus / chemistry*
  • Encephalitis Viruses, Tick-Borne / chemistry*
  • Genome, Viral
  • Molecular Sequence Data
  • Protein Structure, Secondary
  • Proteomics*
  • Sequence Alignment
  • Viral Envelope Proteins / chemistry*
  • Viral Fusion Proteins / chemistry*

Substances

  • E1 protein, Hepatitis C virus
  • Viral Envelope Proteins
  • Viral Fusion Proteins

Associated data

  • GENBANK/AF404756
  • SWISSPROT/P12823
  • SWISSPROT/P14336
  • SWISSPROT/P27958
  • SWISSPROT/P32886