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Future Virol. Epub 2018 May 21. Post-translational modifications of coronavirus proteins: roles and function

tetano

Editor, Senior Moderator
Future Virol. 2018 Jun;13(6):405-430. doi: 10.2217/fvl-2018-0008. Epub 2018 May 21.
Post-translational modifications of coronavirus proteins: roles and function.


Fung TS[SUP]1,[/SUP][SUP]1[/SUP], Liu DX[SUP]1,[/SUP][SUP]2,[/SUP][SUP]1,[/SUP][SUP]2[/SUP].

Author information




Abstract

Post-translational modifications (PTMs) refer to the covalent modifications of polypeptides after they are synthesized, adding temporal and spatial regulation to modulate protein functions. Being obligate intracellular parasites, viruses rely on the protein synthesis machinery of host cells to support replication, and not surprisingly, many viral proteins are subjected to PTMs. Coronavirus (CoV) is a group of enveloped RNA viruses causing diseases in both human and animals. Many CoV proteins are modified by PTMs, including glycosylation and palmitoylation of the spike and envelope protein, N- or O-linked glycosylation of the membrane protein, phosphorylation and ADP-ribosylation of the nucleocapsid protein, and other PTMs on nonstructural and accessory proteins. In this review, we summarize the current knowledge on PTMs of CoV proteins, with an emphasis on their impact on viral replication and pathogenesis. The ability of some CoV proteins to interfere with PTMs of host proteins will also be discussed.
? 2018 Ding Xiang Liu.



KEYWORDS:

coronavirus; deubiquitination; glycosylation; innate immunity; pathogenesis; phosphorylation; post-translational modification; replication; ubiquitination; virus–host interaction


PMID:32201497PMCID:PMC7080180DOI:10.2217/fvl-2018-0008
 
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