Abstract
BackgroundTetherin (also known as BST-2, CD317, and HM1.24) is an interferon- induced protein that blocks the release of a variety of enveloped viruses, such as retroviruses, filoviruses and herpesviruses. However, the relationship between tetherin and foamy viruses has not been clearly demonstrated.ResultsIn this study, we found that tetherin of human, simian, bovine or canine origin inhibits the production of infectious prototypic foamy virus (PFV). The inhibition of PFV by human tetherin is counteracted by human immunodeficiency virus type 1 (HIV-1) Vpu. Furthermore, we generated human tetherin transmembrane domain deletion mutant (delTM), glycosyl phosphatidylinositol (GPI) anchor deletion mutant (delGPI), and dimerization and glycosylation deficient mutants. Compared with wild type tetherin, the delTM and delGPI mutants only moderately inhibited PFV production. In contrast, the dimerization and glycosylation deficient mutants inhibit PFV production as efficiently as the wild type tetherin.ConclusionsThese results demonstrate that tetherin inhibits the release and infectivity of PFV, and this inhibition is antagonized by HIV-1 Vpu. Both the transmembrane domain and the GPI anchor of tetherin are important for the inhibition of PFV, whereas the dimerization and the glycosylation of tetherin are dispensable.
Highlights
Tetherin is an interferon- induced protein that blocks the release of a variety of enveloped viruses, such as retroviruses, filoviruses and herpesviruses
To determine whether the antiviral activity of tetherin against prototypic foamy virus (PFV) is antagonized by Vpu, human immunodeficiency virus (HIV)-1 Vpu was coexpressed with pcPFV and human tetherin
These data suggest that human tetherin inhibits the release of PFV and this inhibition is overcome by Human immunodeficiency virus type 1 (HIV-1) Vpu
Summary
Tetherin ( known as BST-2, CD317, and HM1.24) is an interferon- induced protein that blocks the release of a variety of enveloped viruses, such as retroviruses, filoviruses and herpesviruses. Human immunodeficiency virus type 1 (HIV-1) Vpu and K5 of Kaposi’s sarcoma-associated herpesvirus (KSHV) cause the degradation and cell surface downregulation of Tetherin is a 30-36 kDa type II transmembrane protein. It consists of four domains, an N-terminal cytoplasmic tail (CT), a single transmembrane domain (TM), an extracellular coiled-coil domain and a C-terminal glycosyl phosphatidylinositol (GPI) anchor [22,23,24,25]. The three cysteine residues at positions 53, 63 and 91 in the extracellular domain are involved in disulfide bond-linked dimerization of tetherin [22,24]
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