Mutation of glycosylation sites in BST-2 leads to its accumulation at intracellular CD63-positive vesicles without affecting its antiviral activity against multivesicular body-targeted HIV-1 and hepatitis B virus

Zhu Han, Mingyu Lv, Ying Shi, Jinghua Yu, Junqi Niu, Xiao Fang Yu, Wenyan Zhang

Research output: Contribution to journalArticlepeer-review

Abstract

BST-2/tetherin blocks the release of various enveloped viruses including HIV-1 with a “physical tethering” model. The detailed contribution of N-linked glycosylation to this model is controversial. Here, we confirmed that mutation of glycosylation sites exerted an effect of post-translational mis-trafficking, leading to an accumulation of BST-2 at intracellular CD63-positive vesicles. BST-2 with this phenotype potently inhibited the release of multivesicular body-targeted HIV-1 and hepatitis B virus, without affecting the co-localization of BST-2 with EEA1 and LAMP1. These results suggest that N-linked glycosylation of human BST-2 is dispensable for intracellular virion retention and imply that this recently discovered intracellular tethering function may be evolutionarily distinguished from the canonical antiviral function of BST-2 by tethering nascent virions at the cell surface.

Original languageEnglish (US)
Article number62
JournalViruses
Volume8
Issue number3
DOIs
StatePublished - Feb 26 2016

Keywords

  • BST-2
  • Glycosylation
  • HBV
  • HIV-1

ASJC Scopus subject areas

  • Infectious Diseases
  • Virology

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