Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2021 Dec 25;204(1):77.
doi: 10.1007/s00203-021-02727-3.

Molecular mechanisms for understanding the association between TMPRSS2 and beta coronaviruses SARS-CoV-2, SARS-CoV and MERS-CoV infection: scoping review

Affiliations
Review

Molecular mechanisms for understanding the association between TMPRSS2 and beta coronaviruses SARS-CoV-2, SARS-CoV and MERS-CoV infection: scoping review

María Juliana Chaves-Medina et al. Arch Microbiol. .

Abstract

The aim of this scoping review was to identify knowledge gaps and to describe the current state of the research on the association between TMPRSS2 and the essential beta coronaviruses (Beta-CoVs) infection and the molecular mechanisms for this association. We searched MEDLINE (OVID), EMBASE, and the Cochrane Central Register of Controlled Trials (CENTRAL). We included 13 studies. Evidence shows an essential role of TMPRSS2 in Spike protein activation, entry, and spread into host cells. Co-expression of TMPRSS2 with cell surface receptors (ACE2 or DPP4) increased virus entry. This serine protease is involved in the formation of large syncytia between infected cells. TMPRSS2 cleaved the Spike protein of SARS-CoV, SARS-CoV-2, and MERS-CoV, and increased virus propagation. Accumulating evidence suggests that TMPRSS2 is an essential protease for virus replication. We highlighted its critical molecular role in membrane fusion and the impact in viral mRNA replication, then promoting/driving pathogenesis and resistance.

Keywords: Betacoronavirus; Gene; MERS-CoV; SARS-CoV; SARS-CoV-2; TMPRSS2.

PubMed Disclaimer

Conflict of interest statement

The authors have no conflict of interest.

Figures

Fig. 1
Fig. 1
Flowchart of selected studies

Similar articles

Cited by

References

    1. Bilinska K, et al. Expression of the SARS-CoV-2 entry proteins, ACE2 and TMPRSS2, in cells of the olfactory epithelium: identification of cell types and trends with age. ACS Chem Neurosci. 2020;11(11):1555–1562. doi: 10.1021/acschemneuro.0c00210. - DOI - PMC - PubMed
    1. Glowacka I, et al. Evidence that TMPRSS2 activates the severe acute respiratory syndrome coronavirus spike protein for membrane fusion and reduces viral control by the humoral immune response. J Virol. 2011;85(9):4122–4134. doi: 10.1128/JVI.02232-10. - DOI - PMC - PubMed
    1. Heurich A, et al. TMPRSS2 and ADAM17 cleave ACE2 differentially and only proteolysis by TMPRSS2 augments entry driven by the severe acute respiratory syndrome coronavirus spike protein. J Virol. 2014;88(2):1293–1307. doi: 10.1128/JVI.02202-13. - DOI - PMC - PubMed
    1. Hoffmann M, et al. SARS-CoV-2 cell entry depends on ACE2 and TMPRSS2 and is blocked by a clinically proven protease inhibitor. Cell. 2020;181:1–10. doi: 10.1016/j.cell.2020.02.052. - DOI - PMC - PubMed
    1. Huang C, et al. ‘Clinical features of patients infected with 2019 novel coronavirus in Wuhan, China’. Lancet. 2020;395:497–506. doi: 10.1016/S0140-6736(20)30183-5. - DOI - PMC - PubMed

MeSH terms

Substances