Topology of hepatitis C virus envelope glycoproteins

@article{Opdebeeck2003TopologyOH,
  title={Topology of hepatitis C virus envelope glycoproteins},
  author={Anne Op de beeck and Jean Dubuisson},
  journal={Reviews in Medical Virology},
  year={2003},
  volume={13}
}
Hepatitis C virus encodes two envelope glycoproteins, E1 and E2, that are released from a polyprotein precursor after cleavage by host signal peptidase(s). These proteins contain a large N‐terminal ectodomain and a C‐terminal transmembrane domain, and they assemble as a noncovalent heterodimer. The transmembrane domains of hepatitis C virus envelope glycoproteins have been shown to be multifunctional: (1) they are membrane anchors, (2) they bear ER retention signals, (3) they contain a signal… 
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TLDR
The results reveal that NS4A is important for late stages of the HCV lifecycle and suggest that the interaction betweenNS4A and E1 may regulate the incorporation of viral RNA into the virion for the formation of infectious HCV particles.
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The results indicate that the HCV E1 and E2 glycoproteins have separable functional properties and that the presence of these two envelope glyCoproteins on VSV/HCV pseudotype particles increases infectious titer.
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TLDR
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References

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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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