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 β sheet domains. Proteomics computational analyses suggest that hepatitis C virus (HCV) env...

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Veröffentlicht in:Virology (New York, N.Y.) N.Y.), 2003-03, Vol.307 (2), p.255-265
Hauptverfasser: Garry, Robert F, Dash, Srikanta
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Sprache:eng
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Zusammenfassung: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 β 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.
ISSN:0042-6822
1096-0341
DOI:10.1016/S0042-6822(02)00065-X