Hepatitis C virus envelope glycoprotein E1
E1 is one of two subunits of the envelope
Structure
The E1 glycoprotein residues 192-383 in the
Function
The E1 protein helps the virus attach to the membrane of the targeted cell. In other envelope virus the E1 protein has a similar role in helping the virus get into the cell. As a heterodimer with E2 it has been discovered that it is essential for HCV entry.[7] When the heterodimer is formed the hepatitis C virus is then able to bind to the receptor of the cell. As a heterodimer the E1 protein alone with the E2 protein worked together to enter the cell. Also cleavage at the core-E1 junction is a prerequisite for SPP-catalyzed cleavage. This helps the virus relocate to the surface of lipid droplets. Once the virus gets to the surface of the lipid droplets it recruits the virus no-structural proteins and replication complex.[8] The SP-catalyzed cleavage at the core-E1 junction is required for the formation of infectious particles and for the release of any HCV particles. Also E1 has no function with budding at the ER membrane. It also had no effect on the intracellular formation of capsid-containing particles. Instead when E1 was not allowed to form this tended to facilitate the budding process.[citation needed]
Possible Vaccine
It has been shown that by blocking E1 we can prevent the formation of the
References
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- ^ Lavie, M.; Goffard, A.; Dubuisson, J. In Chapter 4 HCV Glycoproteins: Assembly of a Functional E1-E2 heterodimer; Norfolk: UK, 2006; .
- PMID 27933781.
- PMID 26811632.
- ^ Lavie, M.; Goffard, A.; Dubuisson, J. In Chapter 4 HCV Glycoproteins: Assembly of a Functional E1-E2 heterodimer; Norfolk: UK, 2006; .
- PMID 28437468.
- PMID 27933781.
- PMID 26811632.