Evidence map›Paper›PMID 35133176›Full record

ArticleScience (New York, N.Y.)2022

Structures of the Omicron spike trimer with ACE2 and an anti-Omicron antibody.

Wanchao Yin, Youwei Xu, Peiyu Xu, Xiaodan Cao, Canrong Wu, Chunyin Gu, Xinheng He, Xiaoxi Wang, Sijie Huang, Qingning Yuan and 16 more

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 182 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
182citing papers in PubMed, 1 pooled it
29.8field-weighted citation impact, top 1% 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

182 citing papers in PubMed, 1 synthesis or guideline pooled it, 299 citations in OpenAlex.

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

26 authors at 3 institutions in 1 country.

Wanchao Yin *The CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.ORCID 0000-0002-6889-4907
Youwei Xu *The CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.ORCID 0000-0001-8069-7511
Peiyu Xu *The CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.ORCID 0000-0003-3590-4037
Xiaodan Cao *Shanghai Jemincare Pharmaceuticals Co., Ltd., Shanghai 201203, China.ORCID 0000-0002-6458-4805
Canrong Wu *The CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.ORCID 0000-0002-2272-3838
Chunyin Gu *Shanghai Jemincare Pharmaceuticals Co., Ltd., Shanghai 201203, China.ORCID 0000-0001-8571-7411
Xinheng HeThe CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.ORCID 0000-0001-7813-5480
Xiaoxi WangThe CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.ORCID 0000-0002-4274-5698
Sijie HuangThe CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.ORCID 0000-0001-5653-0260
Qingning YuanThe Shanghai Advanced Electron Microscope Center, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
Kai WuThe Shanghai Advanced Electron Microscope Center, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
Wen HuThe Shanghai Advanced Electron Microscope Center, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
Zifu HuangState Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.ORCID 0000-0001-9436-4590
Jia LiuShanghai Jemincare Pharmaceuticals Co., Ltd., Shanghai 201203, China.
Zongda WangShanghai Jemincare Pharmaceuticals Co., Ltd., Shanghai 201203, China.ORCID 0000-0002-1662-2934
Fangfang JiaShanghai Jemincare Pharmaceuticals Co., Ltd., Shanghai 201203, China.
Kaiwen XiaShanghai Jemincare Pharmaceuticals Co., Ltd., Shanghai 201203, China.ORCID 0000-0002-1336-8790
Peipei LiuShanghai Jemincare Pharmaceuticals Co., Ltd., Shanghai 201203, China.
Xueping WangShanghai Jemincare Pharmaceuticals Co., Ltd., Shanghai 201203, China.ORCID 0000-0002-2564-8714
Bin SongImmunological Disease Research Center, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.ORCID 0000-0002-5327-5839
Jie ZhengImmunological Disease Research Center, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.ORCID 0000-0001-7932-5753
Hualiang JiangUniversity of Chinese Academy of Sciences, Beijing 100049, China.ORCID 0000-0003-0656-6315
Xi ChengUniversity of Chinese Academy of Sciences, Beijing 100049, China.ORCID 0000-0003-3081-3750
Yi JiangThe CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.ORCID 0000-0002-0723-1413
Su-Jun DengShanghai Jemincare Pharmaceuticals Co., Ltd., Shanghai 201203, China.ORCID 0000-0001-9266-0644
H Eric XuThe CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.ORCID 0000-0002-6829-8144
Chinese Academy of Sciences · CNShanghai Genon Biological Products (China) · CNShanghai Institute of Materia Medica · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) Omicron variant has become the dominant infective strain. We report the structures of the Omicron spike trimer on its own and in complex with angiotensin-converting enzyme 2 (ACE2) or an anti-Omicron antibody. Most Omicron mutations are located on the surface of the spike protein and change binding epitopes to many current antibodies. In the ACE2-binding site, compensating mutations strengthen receptor binding domain (RBD) binding to ACE2. Both the RBD and the apo form of the Omicron spike trimer are thermodynamically unstable. An unusual RBD-RBD interaction in the ACE2-spike complex supports the open conformation and further reinforces ACE2 binding to the spike trimer. A broad-spectrum therapeutic antibody, JMB2002, which has completed a phase 1 clinical trial, maintains neutralizing activity against Omicron. JMB2002 binds to RBD differently from other characterized antibodies and inhibits ACE2 binding.

Indexed as

Angiotensin-Converting Enzyme 2Antibodies, NeutralizingAntibodies, ViralBinding SitesCryoelectron MicroscopyEpitopesHumansImmunoglobulin Fab FragmentsModels, MolecularMutationProtein BindingProtein ConformationProtein DomainsProtein Interaction Domains and MotifsProtein MultimerizationProtein SubunitsACE2 protein, humanAngiotensin-Converting Enzyme 2Antibodies, NeutralizingAntibodies, ViralEpitopesImmunoglobulin Fab FragmentsJMB2002Protein SubunitsSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2

Identifiers

PMID35133176
PMCPMC8939775
OpenAlexW4210943449

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.