Evidence map›Paper›PMID 40556423›Full record

ArticleJournal of medical virology2025

TMEM106B Supports Viral Entry and Syncytia Formation Mediated by the Spike Proteins From Omicron BA.2.86 and JN.1.

Yuanyuan Wang, Hui Sun, Yuxin Liu, Yanjun Song, Weitong Wang, Guoli Li, Jie Zhang, Yuanyuan Zhang, Danying Chen, Xuesen Zhao

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of medical virology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

10 authors.

Yuanyuan WangNational Key Laboratory of Intelligent Tracking and Forecasting for Infectious Diseases, Beijing Ditan Hospital, Capital Medical University, Beijing, China.
Hui SunNational Key Laboratory of Intelligent Tracking and Forecasting for Infectious Diseases, Beijing Ditan Hospital, Capital Medical University, Beijing, China.
Yuxin LiuNational Key Laboratory of Intelligent Tracking and Forecasting for Infectious Diseases, Beijing Ditan Hospital, Capital Medical University, Beijing, China.
Yanjun SongNational Key Laboratory of Intelligent Tracking and Forecasting for Infectious Diseases, Beijing Ditan Hospital, Capital Medical University, Beijing, China.
Weitong WangNational Key Laboratory of Intelligent Tracking and Forecasting for Infectious Diseases, Beijing Ditan Hospital, Capital Medical University, Beijing, China.
Guoli LiNational Key Laboratory of Intelligent Tracking and Forecasting for Infectious Diseases, Beijing Ditan Hospital, Capital Medical University, Beijing, China.
Jie ZhangNational Key Laboratory of Intelligent Tracking and Forecasting for Infectious Diseases, Beijing Ditan Hospital, Capital Medical University, Beijing, China.
Yuanyuan ZhangNational Key Laboratory of Intelligent Tracking and Forecasting for Infectious Diseases, Beijing Ditan Hospital, Capital Medical University, Beijing, China.
Danying ChenNational Key Laboratory of Intelligent Tracking and Forecasting for Infectious Diseases, Beijing Ditan Hospital, Capital Medical University, Beijing, China.
Xuesen ZhaoNational Key Laboratory of Intelligent Tracking and Forecasting for Infectious Diseases, Beijing Ditan Hospital, Capital Medical University, Beijing, China.ORCID 0000-0003-1286-5733

Funding

This study was supported by the National Key Research and Development Program (2023YFC2306000) and the National Key Research and Development Program (2023YFC3043502).
6 · The paper itself

Abstract

Transmembrane protein 106B (TMEM106B) has been identified as a functional receptor facilitating ACE2-independent SARS-CoV-2 entry. However, its role in supporting a broad range of SARS-CoV-2 variants, including the emerging Omicron BA.2.86 and JN.1 subvariants, remains to be determined. To address this question, we generated 293- and A549-derived TMEM106B knockout cell lines and assessed their ability to support viral entry for various SARS-CoV-2 variants (D614G, E484D, Omicron BA.1, BA.2, XBB.1.5, BA.2.86, and JN.1) using pseudoviral infection systems. We also examined the role of transmembrane protease serine 2 (TMPRSS2) and other type II transmembrane serine proteases (TTSP) in viral entry and syncytium formation. Our results showed that TMEM106B knockout significantly reduced viral entry across all tested variants. Additionally, overexpression of TMPRSS2, TMPRSS11F and TMPRSS13 in TMEM106B-expressing cells enhanced viral entry and syncytium formation, including BA.2.86 and JN.1 variants. Importantly, we identified two single-nucleotide polymorphisms (SNPs) that result in G2A and N151S variant, respectively, affects TMEM106B receptor function, indicating that selected genetic polymorphisms of TMEM106B gene may impact cell susceptibility to SARS-CoV-2 infection. These findings highlight TMEM106B as a functional receptor for SARS-CoV-2 across different variants, including the latest Omicron subvariants, and provide new insights for the therapeutic interventions targeting viral entry.

Indexed as

COVID-19Giant CellsMembrane ProteinsSARS-CoV-2Spike Glycoprotein, CoronavirusVirus InternalizationA549 CellsAngiotensin-Converting Enzyme 2HEK293 CellsHumansReceptors, VirusSerine EndopeptidasesAngiotensin-Converting Enzyme 2Membrane ProteinsReceptors, VirusSerine EndopeptidasesSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2TMPRSS2 protein, humanSARS‐CoV‐2SNPsyncytia formationTMEM106BTTSPs

Identifiers

PMID40556423
PMCPMC12188148

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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.