Overexpression of SARS-CoV-2 protein ORF6 dislocates RAE1 and NUP98 from the nuclear pore complex.

Koki Kato, Dini Kurnia Ikliptikawati, Akiko Kobayashi, Hiroya Kondo, Keesiang Lim, Masaharu Hazawa, Richard W Wong

Biochemical and biophysical research communications 2021 Jan 15

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The novel human betacoronavirus SARS-CoV-2 has caused an unprecedented pandemic in the 21st century. Several studies have revealed interactions between SARS-CoV-2 viral proteins and host nucleoporins, yet their functions are largely unknown. Here, we demonstrate that the open-reading frame 6 (ORF6) of SARS-CoV-2 can directly manipulate localization and functions of nucleoporins. We found that ORF6 protein disrupted nuclear rim staining of nucleoporins RAE1 and NUP98. Consequently, this disruption caused aberrant nucleocytoplasmic trafficking and led to nuclear accumulation of mRNA transporters such as hnRNPA1. Ultimately, host cell nucleus size was reduced and cell growth was halted. Copyright © 2020 Elsevier Inc. All rights reserved.

Citation

Koki Kato, Dini Kurnia Ikliptikawati, Akiko Kobayashi, Hiroya Kondo, Keesiang Lim, Masaharu Hazawa, Richard W Wong. Overexpression of SARS-CoV-2 protein ORF6 dislocates RAE1 and NUP98 from the nuclear pore complex. Biochemical and biophysical research communications. 2021 Jan 15;536:59-66