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Abstract
Tetherin (BST2/CD317/HM1.24) has emerged as a key host-cell ·defence molecule that acts by inhibiting the release and spread of diverse enveloped virions from infected cells. We analysed the biological features of canine tetherin and found it to be an unstable hydrophilic type I transmembrane protein with one transmembrane domain, no signal peptide, and multiple glycosylation and phosphorylation sites. Furthermore, the tissue expression profile of canine tetherin revealed that it was particularly abundant in immune organs. The canine tetherin gene contains an interferon response element sequence that can be regulated and expressed by canine IFN-α. A CCK-8 assay showed that canine tetherin was effective in helping mitigate cellular damage caused by canine influenza virus (CIV) infection. Additionally, we found that the overexpression of canine tetherin inhibited replication of the CIV and that interference with the canine tetherin gene enhanced CIV replication in cells. The impact of canine tetherin on CIV replication was mild. However, these results elucidate the role of the innate immune factor, canine tetherin, during CIV infection for the first time.
Highlights
In recent years, researchers have gradually discovered that humans and other mammals have various specific antiviral factors
EditSeq software analysis showed that the 567 nucleotides of the canine tetherin coding sequence (CDS) encode 188 amino acids whose total molecular weight is 20,626.84 daltons
The cytoplasmic tail,aapivotal transmembrane domain, an extracellular coiled-coil domain,ofand a C-terminal unique of tetherin consists oftoseveral domains, including an N-terminal anchor. bridge-like. All of these topology domains together allow tetherin effectively tether the viral membrane to the cytoplasmic tail, a[35]
Summary
Researchers have gradually discovered that humans and other mammals have various specific antiviral factors. In January 2008, the interferon-induced membrane protein tetherin ( known as CD317 or bone marrow stromal cell antigen 2 (BST2)) was identified by Neil. This protein can restrict the release of human immunodeficiency virus type 1 (HIV-1) particles from infected cells and can be counteracted by the HIV-1 protein Vpu [1]. Many researchers have conducted additional studies of tetherin and have found that it exerts broad antiviral effects by targeting virion components of various enveloped viruses. Canine influenza virus (CIV) belongs to the influenza A virus (IAV) family, which is composed of enveloped viruses. CIV H3N2 circulates and causes epidemics primarily in Asian countries including
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