Author: Fung, To Sing; Liu, Ding Xiang
Title: Post-translational modifications of coronavirus proteins: roles and function Document date: 2018_5_21
ID: 38c28tw1_41
Snippet: In animal isolates and early human isolates, the sgRNA8 of SARS-CoV encoded a single protein 8ab. However, in later human isolates during the peak of SARS-CoV epidemic, a 29-nt deletion in the center split ORF8 into two smaller ORFs, encoding proteins 8a and 8b respectively [166] . Whereas protein 8ab is co-translationally imported into the ER and is N-linked glycosylated at N81, protein 8b is synthesized in the cytosol and not modified [167] . B.....
Document: In animal isolates and early human isolates, the sgRNA8 of SARS-CoV encoded a single protein 8ab. However, in later human isolates during the peak of SARS-CoV epidemic, a 29-nt deletion in the center split ORF8 into two smaller ORFs, encoding proteins 8a and 8b respectively [166] . Whereas protein 8ab is co-translationally imported into the ER and is N-linked glycosylated at N81, protein 8b is synthesized in the cytosol and not modified [167] . Both proteins 8b and 8ab were shown to interact with mono-ubiquitin and polyubiquitin, and both were also modified by ubiquitination. However, whereas glycosylation at N81 stabilized protein 8ab and protected it from proteasomal degradation, protein 8b was highly unstable and underwent rapid proteasomal degradation [168] . The ubiquitinated 8b and 8ab may mediate rapid degradation of IRF3 and regulate host antiviral innate immunity [169] .
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