Proteomics computational analyses suggest that hepatitis C virus E1 and pestivirus E2 envelope glycoproteins are truncated class II fusion proteins.
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.
Garry
Robert F
RF
Department of Microbiology and Immunology, Tulane University Health Sciences Center, New Orleans, LA 70112, USA. rfgarry@tulane.edu
Dash
Srikanta
S
D000595:Amino Acid Sequence; D006692:Classical Swine Fever Virus / Q000737:chemistry*; D004669:Encephalitis Viruses, Tick-Borne / Q000737:chemistry*; D016679:Genome, Viral; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D040901:Proteomics; D016415:Sequence Alignment; D014759:Viral Envelope Proteins / Q000737:chemistry*; D014760:Viral Fusion Proteins / Q000737:chemistry*
C087035:E1 protein, Hepatitis C virus; D014759:Viral Envelope Proteins; D014760:Viral Fusion Proteins