Author: Fung, To Sing; Liu, Ding Xiang
Title: Post-translational modifications of coronavirus proteins: roles and function Document date: 2018_5_21
ID: 38c28tw1_29
Snippet: One early study shows that the N protein of TGEV was cleaved at D359 during the late stage of infection, presumably by the activated caspase-6 and -7 during TGEV-induced apoptosis [136] . Similarly, the N protein of SARS-CoV was also cleaved at D400 and D403 by caspases during lytic infection in Vero E6 and A549 cells, but not during persistent infection in Caco-2 and N2a cells [137] . Cleavage of the SARS-CoV N protein was mediated by caspase-6 .....
Document: One early study shows that the N protein of TGEV was cleaved at D359 during the late stage of infection, presumably by the activated caspase-6 and -7 during TGEV-induced apoptosis [136] . Similarly, the N protein of SARS-CoV was also cleaved at D400 and D403 by caspases during lytic infection in Vero E6 and A549 cells, but not during persistent infection in Caco-2 and N2a cells [137] . Cleavage of the SARS-CoV N protein was mediated by caspase-6 and/or caspase-3, and was dependent on the nuclear localization of the N protein [137] . We have also observed cleavage of the IBV N protein during late stage IBV infection [138, 139] . Thus proteolytic cleavage of the N protein may be a common outcome associated with coronavirus-induced apoptosis in the infected cells, although the biological significance is not known. Presumably, coronavirus N protein may compete with other caspase substrates for cleavage, so as to promote cell survival in order to prolong the duration of virion release.
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