Proteomics computational analyses suggest that hepatitis C virus E1 and pestivirus E2 envelope glycoproteins are truncated class II fusion proteins |
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Authors: | Garry Robert F Dash Srikanta |
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Affiliation: | Department of Microbiology and Immunology, Tulane University Health Sciences Center, New Orleans, LA 70112, USA. rfgarry@tulane.edu |
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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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Keywords: | Viral fusion proteins Hepatitis C virus envelope glycoproteins Pestivirus Proteomics Glycoprotein structure Virus evolution |
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