Abstract
Human Tetherin/BST-2 has recently been identified as a cellular antiviral factor that blocks the release of various enveloped viruses. In this study, we cloned a cDNA fragment encoding a feline homolog of Tetherin/BST-2 and characterized the protein product. The degree of amino acid sequence identity between human Tetherin/BST-2 and the feline homolog was 44.4%. Similar to human Tetherin/BST-2, the expression of feline Tetherin/BST-2 mRNA was inducible by type I interferon (IFN). Exogenous expression of feline Tetherin/BST-2 efficiently inhibited the release of feline endogenous retrovirus RD-114. The extracellular domain of feline Tetherin/BST-2 has two putative N-linked glycosylation sites, N79 and N119. Complete loss of N-linked glycosylation by introduction of mutations into both sites resulted in almost complete abolition of its antiviral activity. In addition, feline Tetherin/BST-2 was insensitive to antagonism by HIV-1 Vpu, although the antiviral activity of human Tetherin/BST-2 was antagonized by HIV-1 Vpu. Our data suggest that feline Tetherin/BST-2 functions as a part of IFN-induced innate immunity against virus infection and that the induction of feline Tetherin/BST-2 in vivo may be effective as a novel antiviral strategy for viral infection.
Highlights
Human Tetherin/BST-2 was first identified as a cellular restriction factor that blocks the release of HIV-1 in the absence of the viral accessory protein, Vpu [1]
We identified feline Tetherin/BST-2 and demonstrated the antiviral activity of feline Tetherin/BST-2
It has been reported that the antiviral activity of Tetherin/BST-2 require the structural features such as an N-terminal transmembrane region, a C-terminal glycophosphatidyl inositol (GPI) anchor, and a proper
Summary
Human Tetherin/BST-2 ( referred to as CD317 or HM1.24) was first identified as a cellular restriction factor that blocks the release of HIV-1 in the absence of the viral accessory protein, Vpu [1]. The extracellular domain of Tetherin/BST-2 has two putative N-linked glycosylation sites, which are highly conserved at the same positions among human, rhesus monkey, dog, pig, rat, and mouse, and orthologs have been identified that are glycosylated heterogeneously [8,9]. We showed that N-linked glycosylation is dispensable for the antiviral activity of human Tetherin/BST-2 against Lassa and Marburg viruses [6]. There are conflicting data regarding the role of Nlinked glycosylation on the antiviral activity of human Tetherin/
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