Evidence map›Paper›PMID 37897633›Full record

ArticleMolecular neurobiology2024

SARS-CoV-2 Spike Protein S1 Domain Accelerates α-Synuclein Phosphorylation and Aggregation in Cellular Models of Synucleinopathy.

Jiannan Wang, Lijun Dai, Min Deng, Tingting Xiao, Zhaohui Zhang, Zhentao Zhang

Abstract read
PubMed Publisher
In one paragraph

Article in Molecular neurobiology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

13 citing papers in PubMed, 17 citations in OpenAlex.

  1. Human brain matters: Navigating the neuropathology of COVID-19.Brain pathology (Zurich, Switzerland) · 2026
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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

6 authors at 1 institution in 1 country.

Jiannan Wang *Department of Neurology, Renmin Hospital of Wuhan University, Wuhan, 430060, China.
Lijun Dai *Department of Neurology, Renmin Hospital of Wuhan University, Wuhan, 430060, China.
Min DengDepartment of Neurology, Renmin Hospital of Wuhan University, Wuhan, 430060, China.
Tingting XiaoDepartment of Neurology, Renmin Hospital of Wuhan University, Wuhan, 430060, China.
Zhaohui ZhangDepartment of Neurology, Renmin Hospital of Wuhan University, Wuhan, 430060, China.
Zhentao ZhangDepartment of Neurology, Renmin Hospital of Wuhan University, Wuhan, 430060, China. Zhentaozhang@whu.edu.cn.ORCID http://orcid.org/0000-0001-6708-1472
Wuhan University · CN

Funding

Foundation for Innovative Research Groups of Hubei Province of China 2022CFA026Jinan Science and Technology Bureau No. 202228022National Key Research and Development Program of China 2019YFE0115900National Natural Science Foundation of China No. 81901090National Natural Science Foundation of China No. 82271447
6 · The paper itself

Abstract

The 2019 novel coronavirus disease (COVID-19) is an infectious disease that began to spread globally since 2019. Some COVID-19 patients have neurological complications, such as olfactory disorders and movement disorders, which coincide with the symptoms of Parkinson's disease (PD). Increasing imaging and autopsy evidence supports that the density of dopaminergic neurons in the nigrostriatal pathway is damaged in some COVID-19 patients. However, the underlying mechanism that causes PD-like symptoms remains unclear. PD is an age-related neurodegenerative disease with Lewy bodies (LBs) as its histopathologic feature. The main component of LBs is abnormally aggregated α-synuclein (α-syn). The prion-like propagation of α-syn aggregates plays a key role in the onset and progression of PD. The spike protein (S protein) of SARS-CoV-2 is a heparin-binding protein that mediates the entry of the virus into host cells. Here we found that the S1 domain interacts with α-syn and promotes α-syn aggregation. The S1 domain induces mitochondrial dysfunction, oxidative stress, and cytotoxicity. The S1-seeded α-syn fibrils show enhanced seeding activity and induce synaptic damage and cytotoxicity. Thus, the S1 domain of SARS-CoV-2 promotes the aggregation of α-syn in the cellular model of synucleinopathy and may contribute to the pathogenesis of PD.

Indexed as

COVID-19Neurodegenerative DiseasesParkinson DiseaseSynucleinopathiesalpha-SynucleinHumansPhosphorylationSARS-CoV-2Spike Glycoprotein, Coronavirusalpha-SynucleinSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2COVID-19CytotoxicityLewy bodyParkinson’s diseaseVirus protein

Identifiers

PMID37897633
OpenAlexW4388002425

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.