【摘 要】
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A key to tackling the coronavirus disease 2019 (COVID-19) pandemic is to understand how severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) manages to outsmart host antiviral defense mecha-nisms.Stress granules (SGs),which are assembled during vi
【机 构】
：
School of Pharmacy,Shanghai University of Traditional Chinese Medicine,Shanghai 201203,China;School
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A key to tackling the coronavirus disease 2019 (COVID-19) pandemic is to understand how severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) manages to outsmart host antiviral defense mecha-nisms.Stress granules (SGs),which are assembled during viral infection and function to sequester host and viral mRNAs and proteins,are part of the antiviral responses.Here,we show that the SARS-CoV-2 nucleocapsid (N) protein,an RNA binding protein essential for viral production,interacted with Ras-GTPase-activating protein SH3-domain-binding protein (G3BP) and disrupted SG assembly,both of which require intrinsically disordered region1 (IDR1) in N protein.The N protein partitioned into SGs through liquid-liquid phase separation with G3BP,and blocked the interaction of G3BP1 with other SG-related proteins.Moreover,the N protein domains important for phase separation with G3BP and SG disassembly were required for SARS-CoV-2 viral production.We propose that N protein-mediated SG disassembly is crucial for SARS-CoV-2 oroduction.
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