Mass spectrometric characterization of glycosylation of hepatitis C virus E2 envelope glycoprotein reveals extended microheterogeneity of N-glycans.

@article{Iacob2008MassSC,
  title={Mass spectrometric characterization of glycosylation of hepatitis C virus E2 envelope glycoprotein reveals extended microheterogeneity of N-glycans.},
  author={Roxana E. Iacob and Irina Perdivara and Michael Przybylski and Kenneth B. Tomer},
  journal={Journal of the American Society for Mass Spectrometry},
  year={2008},
  volume={19 3},
  pages={428-44}
}
Hepatitis C virus (HCV) causes acute and chronic liver disease in humans, including chronic hepatitis, cirrhosis, and hepatocellular carcinoma. The polyprotein encoded in the HCV genome is co- and post-translationally processed by host and viral peptidases, generating the structural proteins Core, E1, E2, and p7, and five nonstructural proteins. The two envelope proteins E1 and E2 are heavily glycosylated. Studying the glycan moieties attached to the envelope E2 glycoprotein is important… CONTINUE READING