Hi neo, my interpratation on this is that the virus Vpu protein holds a dual role.
The first is the viroporin function - whereby the protein forms a pore (ion channel) in the host cells plasma membrane whereby the virus can gain better acess into the host cell.
The second is that the Vpu protein antagonizes the host cell restriction factor tetherin. Tetherin is produced as a means to prevent viral access to the host cell. A tetherin antagonist therefore assists viral access to the host cell.
My take on this research is that it suggests that whilst BIT225 does prevent the virus viroporin formation, it has no such effect on the tetherin antagonist properties of Vpu.
Hence
"Our data provide support for the concept that tetherin antagonism and viroporin function are separable on the Vpu transmembrane and that viroporin function might be cell-type dependent. Further, this work contributes to the characterization of BIT225 as an inhibitor that specifically targets the viroporin function of Vpu."
I would value rgc68 opinion here.
bluebush
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