Selected article for: "amino acid and hydrophobic domain"
Author: Bederka, Lydia H.; Bonhomme, Cyrille J.; Ling, Emily L.; Buchmeier, Michael J.
Title: Arenavirus Stable Signal Peptide Is the Keystone Subunit for Glycoprotein Complex Organization
  • Document date: 2014_10_28
    • ID: wbh06gzb_19
    Snippet: Given that the arenavirus signal peptide is an essential component of the glycoprotein complex, our goal was to dissect this subunit's role in glycoprotein maturation. SSP was not degraded upon translocation into the secretory pathway but rather was retained and trafficked with the rest of the glycoprotein complex to the plasma membrane for viral packaging and egress. The requirement for SSP packaging within virions demonstrates two critical role.....
    Document: Given that the arenavirus signal peptide is an essential component of the glycoprotein complex, our goal was to dissect this subunit's role in glycoprotein maturation. SSP was not degraded upon translocation into the secretory pathway but rather was retained and trafficked with the rest of the glycoprotein complex to the plasma membrane for viral packaging and egress. The requirement for SSP packaging within virions demonstrates two critical roles for this 58-amino-acid peptide. First, SSP acts as the leader protein for ER exit and GPC processing within the Golgi stacks, as deletion of either hydrophobic domain inhibits downstream GPC processing (29, 34) . Second, SSP is an important structural component within virions alongside the spike GP1 and transmembrane GP2 subunits.

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