Evidence map›Paper›PMID 32914439›Full record

ArticleThe EMBO journal2020

Structures of the SARS-CoV-2 nucleocapsid and their perspectives for drug design.

Ya Peng, Ning Du, Yuqing Lei, Sonam Dorje, Jianxun Qi, Tingrong Luo, George F Gao, Hao Song

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 198 papers.

0numbers the graph read from it
0cells of the map it votes in
198citing papers in PubMed
4.8field-weighted citation impact, top 3% of its field
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

198 citing papers in PubMed, 320 citations in OpenAlex.

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138 more citing papers are in PubMed but not listed here.

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

8 authors at 2 institutions in 1 country.

Ya PengLaboratory of Animal Infectious Diseases, College of Animal Sciences and Veterinary Medicine, Guangxi University, Nanning, China.
Ning DuResearch Network of Immunity and Health (RNIH), Beijing Institutes of Life Science, Chinese Academy of Sciences, Beijing, China.
Yuqing LeiCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China.
Sonam DorjeCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China.ORCID 0000-0002-1885-3007
Jianxun QiCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China.
Tingrong LuoLaboratory of Animal Infectious Diseases, College of Animal Sciences and Veterinary Medicine, Guangxi University, Nanning, China.
George F GaoCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China.ORCID 0000-0002-3869-615X
Hao SongResearch Network of Immunity and Health (RNIH), Beijing Institutes of Life Science, Chinese Academy of Sciences, Beijing, China.ORCID 0000-0002-2811-0370
Chinese Academy of Sciences · CNGuangxi University · CN

Funding

COVID-19 Emergency Project of CASExternal Cooperation Program of CAS 153211KYSB20160001Ministry of Science and Technology of the People's Republic of China (MOST) 2020YFC0845900National Natural Science Foundation of China (NSF) 81702015National Science and Technology Major Project 2018ZX10733403Youth Innovation Promotion Association of the Chinese Academy of Sciences (Youth Innovation Promotion Association CAS) 2017117
6 · The paper itself

Abstract

COVID-19, caused by SARS-CoV-2, has resulted in severe and unprecedented economic and social disruptions in the world. Nucleocapsid (N) protein, which is the major structural component of the virion and is involved in viral replication, assembly and immune regulation, plays key roles in the viral life cycle. Here, we solved the crystal structures of the N- and C-terminal domains (N-NTD and N-CTD) of SARS-CoV-2 N protein, at 1.8 and 1.5 Å resolution, respectively. Both structures show conserved features from other CoV N proteins. The binding sites targeted by small molecules against HCoV-OC43 and MERS-CoV, which inhibit viral infection by blocking the RNA-binding activity or normal oligomerization of N protein, are relatively conserved in our structure, indicating N protein is a promising drug target. In addition, certain areas of N-NTD and N-CTD display distinct charge distribution patterns in SARS-CoV-2, which may alter the RNA-binding modes. The specific antigenic characteristics are critical for developing specific immune-based rapid diagnostic tests. Our structural information can aid in the discovery and development of antiviral inhibitors against SARS-CoV-2 in the future.

Indexed as

Drug DesignAntiviral AgentsBetacoronavirusCoronavirus Nucleocapsid ProteinsCrystallography, X-RayDrug Delivery SystemsHumansModels, MolecularNucleocapsid ProteinsPhosphoproteinsProtein ConformationProtein DomainsRecombinant ProteinsSARS-CoV-2Antiviral AgentsCoronavirus Nucleocapsid Proteinsnucleocapsid phosphoprotein, SARS-CoV-2Nucleocapsid ProteinsPhosphoproteinsRecombinant Proteins2019-nCoVantiviralsdimerizationnucleocapsidRNA binding

Identifiers

PMID32914439
PMCPMC7560215
OpenAlexW3085912969

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.