Evidence map›Paper›PMID 36071105›Full record

ArticleCommunications biology2022

Multiscale characterization reveals oligomerization dependent phase separation of primer-independent RNA polymerase nsp8 from SARS-CoV-2.

Jinxin Xu, Xin Jiang, Yulong Zhang, Yan Dong, Changli Ma, Hanqiu Jiang, Taisen Zuo, Rui Chen, Yubin Ke, He Cheng and 2 more

Abstract read
In one paragraph

Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

7 citing papers in PubMed.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors.

Jinxin Xu *State Key Laboratory of Respiratory Disease, Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou, 510530, China.
Xin Jiang *Neutron Science Platform, Songshan Lake Materials Laboratory, Dongguan, Guangdong, 523808, China.
Yulong ZhangState Key Laboratory of Respiratory Disease, Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou, 510530, China.
Yan DongState Key Laboratory of Respiratory Disease, Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou, 510530, China.
Changli MaSpallation Neutron Source Science Center, Dongguan, Guangdong, 523803, China.
Hanqiu JiangSpallation Neutron Source Science Center, Dongguan, Guangdong, 523803, China.ORCID 0000-0002-9061-4481
Taisen ZuoSpallation Neutron Source Science Center, Dongguan, Guangdong, 523803, China.
Rui ChenState Key Laboratory of Respiratory Disease, Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou, 510530, China.
Yubin KeSpallation Neutron Source Science Center, Dongguan, Guangdong, 523803, China.
He ChengSpallation Neutron Source Science Center, Dongguan, Guangdong, 523803, China.
Howard WangNeutron Science Platform, Songshan Lake Materials Laboratory, Dongguan, Guangdong, 523808, China. wangh@sslab.org.cn.ORCID 0000-0001-9905-4049
Jinsong LiuState Key Laboratory of Respiratory Disease, Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou, 510530, China. liu_jinsong@gibh.ac.cn.ORCID 0000-0003-2317-0558

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RNA replication and transcription machinery is an important drug target for fighting against coronavirus. Non-structure protein nsp8 was proposed harboring primase activity. However, the RNA primer synthesis mechanism of nsp8 is still largely unknown. Here, we purified dimer and tetramer forms of SARS-CoV-2 nsp8. Combined with dynamic light scattering, small-angle neutron scattering and thermo-stability analysis, we found that both dimer and tetramer become loosened and destabilized with decreasing salt concentration, and the dimer form is more stable than the tetramer form. Further investigation showed that nsp8 dimer and tetramer can undergo phase separation but exhibit different phase separation behaviors. Nsp8 dimer can form liquid-like droplets in the buffer with a low concentration of NaCl; phase separation of nsp8 tetramer depends on the assistance of RNA. Our findings on different phase separation behaviors of nsp8 dimer and tetramer may provide insight into the functional studies of nsp8 in coronavirus.

Indexed as

Coronavirus RNA-Dependent RNA PolymeraseSARS-CoV-2Viral Nonstructural ProteinsAmino Acid SequenceRNACoronavirus RNA-Dependent RNA PolymeraseNS8 protein, SARS-CoV-2RNAViral Nonstructural Proteins

Identifiers

PMID36071105
PMCPMC9451113

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.