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 |
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Format: | Artikel |
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. |
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ISSN: | 0042-6822 1096-0341 |
DOI: | 10.1016/S0042-6822(02)00065-X |