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Tetherin antagonism by V proteins is a common trait among the genus Rubulavirus

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Abstract

Tetherin (BST-2/CD317/HM1.24) is an anti-viral factor that restricts the budding of several enveloped viruses. Most of these viruses have evolved to encode tetherin antagonists. Our previous study demonstrated that the growth of human parainfluenza virus type 2 (hPIV-2), a member of the genus Rubulavirus in the family Paramyxoviridae, was inhibited by tetherin, and its V protein decreases the amount of cell surface tetherin by the interaction. In the present study, we investigated whether tetherin inhibits the growth of other rubulaviruses including PIV-5, mumps virus (MuV), simian virus 41, and hPIV-4, and whether their V proteins act as tetherin antagonists. Plaque assay demonstrated that the growth of PIV-5 and MuV was inhibited by tetherin. Flow cytometry and immunoblot analyses revealed that the infection of PIV-5 and MuV caused reduction of cell surface tetherin without affecting total amount of tetherin. Immunoprecipitation analysis showed that all V proteins of rubulaviruses tested bound to tetherin. These results suggest that tetherin antagonism by V proteins is common among the genus Rubulavirus.

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Acknowledgements

We thank Drs Klaus Strebel and Amy Andrew for anti-Bst2 via the NIH AIDS Research and Reference Reagent Program.

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Correspondence to Machiko Nishio.

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Ohta, K., Matsumoto, Y., Ito, M. et al. Tetherin antagonism by V proteins is a common trait among the genus Rubulavirus . Med Microbiol Immunol 206, 319–326 (2017). https://doi.org/10.1007/s00430-017-0509-y

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  • DOI: https://doi.org/10.1007/s00430-017-0509-y

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