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 language | English (US) |
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Article number | 62 |
Journal | Viruses |
Volume | 8 |
Issue number | 3 |
DOIs | |
State | Published - Feb 26 2016 |
Keywords
- BST-2
- Glycosylation
- HBV
- HIV-1
ASJC Scopus subject areas
- Infectious Diseases
- Virology