N-linked glycosylation of Gn (but not Gc) is important for Crimean Congo hemorrhagic fever virus glycoprotein localization and transport.

@article{Erickson2007NlinkedGO,
  title={N-linked glycosylation of Gn (but not Gc) is important for Crimean Congo hemorrhagic fever virus glycoprotein localization and transport.},
  author={Bobbie Rae Erickson and Varough M. Deyde and A. J. S{\'a}nchez and Martin J. Vincent and Stuart T Nichol},
  journal={Virology},
  year={2007},
  volume={361 2},
  pages={348-55}
}
The mature Gn glycoprotein of Crimean Congo hemorrhagic fever (CCHF) virus contains two predicted glycosylation sites (557N and 755N). Of these, N-glycans are added only at 557N, as evidenced by abrogation of Gn-glycosylation by mutation of 557N but not 755N site. Mutational block of Gn-glycosylation at 557N did not significantly affect Gn proteolytic processing but did result in mislocalization and retention of Gn and other proteins synthesized from the virus M segment ORF (GP160, GP85, GP38… CONTINUE READING

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