Identification of residues in the BST-2 TM domain important for antagonism by HIV-1 Vpu using a gain-of-function approach

Identification of residues in the BST-2 TM domain important for antagonism by HIV-1 Vpu using a gain-of-function approach

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The HIV-1 Vpu protein enhances the release of viral particles from the cell surface in a cell-type specific manner.In the absence of Vpu, nascent virions remain tethered to the cell surface in restricted cell types.Recently, the human host factor BST-2/CD317/tetherin was found to be responsible for the inhibition of virus release.

It was also reported that HIV-1 Vpu can target human BST-2 but eeboo coupons is unable to interfere with the function of murine or simian BST-2.We performed a gain-of-function study to determine which of the differences between human and rhesus BST-2 account for the differential sensitivity to Vpu.We transferred human BST-2 sequences into rhesus BST-2 and assessed the resulting chimeras for inhibition of HIV-1 virus release and sensitivity to Vpu.

We found that rhesus BST-2 carrying the transmembrane (TM) domain of human BST-2 is susceptible to HIV-1 Vpu.Finally, a single-amino-acid change in the rhesus BST-2 TM domain was sufficient to read more confer Vpu sensitivity.