Author: Fung, To Sing; Liu, Ding Xiang
Title: Post-translational modifications of coronavirus proteins: roles and function Document date: 2018_5_21
ID: 38c28tw1_20
Snippet: O-linked glycosylation is not essential for the assembly of MHV virions, as mutations that abolished the normal O-linked glycosylation site did not inhibit the budding of infectious virions [103] or growth kinetics in cell culture [104] . However, it was found that recombinant MHV containing N-linked glycosylated M protein induced a higher level of type I interferon compared with the wild-type MHV with O-linked glycosylated M protein, whereas MHV.....
Document: O-linked glycosylation is not essential for the assembly of MHV virions, as mutations that abolished the normal O-linked glycosylation site did not inhibit the budding of infectious virions [103] or growth kinetics in cell culture [104] . However, it was found that recombinant MHV containing N-linked glycosylated M protein induced a higher level of type I interferon compared with the wild-type MHV with O-linked glycosylated M protein, whereas MHV with nonglycosylated M protein was a poor interferon inducer in cell culture [104] . The in vitro interferongenic capacity also correlated with the abilities of these viruses to replicate in the liver of infected mice, suggesting that glycosylation status of M protein might affect the induction of innate immune response by MHV infection [104] .
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