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- W1679889097 endingPage "4046" @default.
- W1679889097 startingPage "3995" @default.
- W1679889097 abstract "In the 26 years since the discovery of Hepatitis C virus (HCV) a major global research effort has illuminated many aspects of the viral life cycle, facilitating the development of targeted antivirals. Recently, effective direct-acting antiviral (DAA) regimens with >90% cure rates have become available for treatment of chronic HCV infection in developed nations, representing a significant advance towards global eradication. However, the high cost of these treatments results in highly restricted access in developing nations, where the disease burden is greatest. Additionally, the largely asymptomatic nature of infection facilitates continued transmission in at risk groups and resource constrained settings due to limited surveillance. Consequently a prophylactic vaccine is much needed. The HCV envelope glycoproteins E1 and E2 are located on the surface of viral lipid envelope, facilitate viral entry and are the targets for host immunity, in addition to other functions. Unfortunately, the extreme global genetic and antigenic diversity exhibited by the HCV glycoproteins represents a significant obstacle to vaccine development. Here we review current knowledge of HCV envelope protein structure, integrating knowledge of genetic, antigenic and functional diversity to inform rational immunogen design." @default.
- W1679889097 created "2016-06-24" @default.
- W1679889097 creator A5027895154 @default.
- W1679889097 creator A5048573821 @default.
- W1679889097 creator A5052898175 @default.
- W1679889097 creator A5060383367 @default.
- W1679889097 creator A5076222298 @default.
- W1679889097 creator A5089379354 @default.
- W1679889097 creator A5091291837 @default.
- W1679889097 date "2015-07-17" @default.
- W1679889097 modified "2023-10-16" @default.
- W1679889097 title "Genetic Diversity Underlying the Envelope Glycoproteins of Hepatitis C Virus: Structural and Functional Consequences and the Implications for Vaccine Design" @default.
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