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TitleModular characterization of SARS-CoV-2 nucleocapsid protein domain functions in nucleocapsid-like assembly.
Journal, issue, pagesMol Biomed, Vol. 4, Issue 1, Page 16, Year 2023
Publish dateMay 22, 2023
AuthorsYan Wang / Xiaobin Ling / Chong Zhang / Jian Zou / Bingnan Luo / Yongbo Luo / Xinyu Jia / Guowen Jia / Minghua Zhang / Junchao Hu / Ting Liu / Yuanfeiyi Wang / Kefeng Lu / Dan Li / Jinbiao Ma / Cong Liu / Zhaoming Su /
PubMed AbstractSARS-CoV-2 and its variants, with the Omicron subvariant XBB currently prevailing the global infections, continue to pose threats on public health worldwide. This non-segmented positive-stranded RNA ...SARS-CoV-2 and its variants, with the Omicron subvariant XBB currently prevailing the global infections, continue to pose threats on public health worldwide. This non-segmented positive-stranded RNA virus encodes the multi-functional nucleocapsid protein (N) that plays key roles in viral infection, replication, genome packaging and budding. N protein consists of two structural domains, NTD and CTD, and three intrinsically disordered regions (IDRs) including the N, the serine/arginine rich motif (SR), and the C. Previous studies revealed functions of N protein in RNA binding, oligomerization, and liquid-liquid phase separation (LLPS), however, characterizations of individual domains and their dissected contributions to N protein functions remain incomplete. In particular, little is known about N protein assembly that may play essential roles in viral replication and genome packing. Here, we present a modular approach to dissect functional roles of individual domains in SARS-CoV-2 N protein that reveals inhibitory or augmented modulations of protein assembly and LLPS in the presence of viral RNAs. Intriguingly, full-length N protein (N) assembles into ring-like architecture whereas the truncated SR-CTD-C (N) promotes filamentous assembly. Moreover, LLPS droplets of N and N are significantly enlarged in the presence of viral RNAs, and we observed filamentous structures in the N droplets using correlative light and electron microscopy (CLEM), suggesting that the formation of LLPS droplets may promote higher-order assembly of N protein for transcription, replication and packaging. Together this study expands our understanding of the multiple functions of N protein in SARS-CoV-2.
External linksMol Biomed / PubMed:37211575 / PubMed Central
MethodsEM (single particle)
Resolution20.0 Å
Structure data

EMDB-35527: SARS-CoV-2,N protein
Method: EM (single particle) / Resolution: 20.0 Å

EMDB-35528: SARS-CoV-2 NFL and N182-419 protein assembly under low and high salt conditions
Method: EM (single particle) / Resolution: 20.0 Å

Source
  • Severe acute respiratory syndrome coronavirus 2

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