Evidence map›Paper›PMID 40157604›Full record

ArticleVirologica Sinica2025

The SARS-CoV-2 NSP4 T492I mutation promotes double-membrane vesicle formation to facilitate transmission.

Pei Wang, Buyun Tian, Ke Xiao, Wei Ji, Zonghong Li

Abstract read
In one paragraph

Article in Virologica Sinica, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Article
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

5 authors.

Pei WangThe First Affiliated Hospital of Guangzhou Medical University, Guangzhou National Laboratory Clinical Base, Guangzhou Medical University, Guangzhou, 510120, China; Guangzhou National Laboratory, Guangzhou, 510005, China.
Buyun TianThe First Affiliated Hospital of Guangzhou Medical University, Guangzhou National Laboratory Clinical Base, Guangzhou Medical University, Guangzhou, 510120, China; Guangzhou National Laboratory, Guangzhou, 510005, China.
Ke XiaoNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
Wei JiNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
Zonghong LiThe First Affiliated Hospital of Guangzhou Medical University, Guangzhou National Laboratory Clinical Base, Guangzhou Medical University, Guangzhou, 510120, China; Guangzhou National Laboratory, Guangzhou, 510005, China. Electronic address: li_zonghong@gzlab.ac.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The evolution of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has resulted in mutations not only in the spike protein, aiding immune evasion, but also in the NSP3/4/6 proteins, crucial for regulating double-membrane vesicle (DMV) formation. However, the functional consequences of these NSP3/4/6 mutations remain poorly understood. In this study, a systematic analysis was conducted to investigate the evolutionary patterns of NSP3/4/6 mutations and their impact on DMV formation. The findings revealed that the NSP4 T492I mutation, a prevalent mutation found in all Delta and Omicron sub-lineages, notably enhances DMV formation. Mechanistically, the NSP4 T492I mutation enhances its homodimerization, leading to an increase in the size of puncta induced by NSP3/4, and also augments endoplasmic reticulum (ER) membrane curvature, resulting in a higher DMV density per fluorescent puncta. This study underscores the significance of the NSP4 T492I mutation in modulating DMV formation, with potential implications for the transmission dynamics of SARS-CoV-2. It contributes valuable insights into how these mutations impact viral replication and pathogenesis.

Indexed as

COVID-19SARS-CoV-2Viral Nonstructural ProteinsAnimalsChlorocebus aethiopsEndoplasmic ReticulumHumansMutationVero CellsViral Nonstructural ProteinsDMVER membrane curvatureHomodimerizationNSP4 T492I mutationSARS-CoV-2Virus transmission

Identifiers

PMID40157604
PMCPMC12131028

What OpenQuestion holds

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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.