Evidence map›Paper›PMID 39599912›Full record

ArticleViruses2024

Unveiling the Role of TMPRSS2 in the Proteolytic Activation of Pandemic and Zoonotic Influenza Viruses and Coronaviruses in Human Airway Cells.

Marie Schwerdtner, Luna C Schmacke, Julia Nave, Hannah Limburg, Torsten Steinmetzer, David A Stein, Hong M Moulton, Eva Böttcher-Friebertshäuser

Abstract read
In one paragraph

Article in Viruses, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
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

8 authors.

Marie SchwerdtnerInstitute of Virology, Philipps-University Marburg, 35043 Marburg, Germany.
Luna C SchmackeInstitute of Pharmaceutical Chemistry, Philipps-University Marburg, 35037 Marburg, Germany.
Julia NaveInstitute of Virology, Philipps-University Marburg, 35043 Marburg, Germany.
Hannah LimburgInstitute of Virology, Philipps-University Marburg, 35043 Marburg, Germany.
Torsten SteinmetzerInstitute of Pharmaceutical Chemistry, Philipps-University Marburg, 35037 Marburg, Germany.ORCID 0000-0001-6523-4754
David A SteinDepartment of Biomedical Sciences, Carlson College of Veterinary Medicine, Oregon State University, Corvallis, OR 97331, USA.ORCID 0000-0002-5446-5167
Hong M MoultonDepartment of Biomedical Sciences, Carlson College of Veterinary Medicine, Oregon State University, Corvallis, OR 97331, USA.
Eva Böttcher-FriebertshäuserInstitute of Virology, Philipps-University Marburg, 35043 Marburg, Germany.ORCID 0000-0002-0007-8110

Funding

Deutsche Forschungsgemeinschaft SFB1021State of Hesse PandemienetzwerkState of Hesse LOEWE CoroPan
6 · The paper itself

Abstract

The zoonotic transmission of influenza A viruses (IAVs) and coronaviruses (CoVs) may result in severe disease. Cleavage of the surface glycoproteins hemagglutinin (HA) and spike protein (S), respectively, is essential for viral infectivity. The transmembrane serine protease 2 (TMPRSS2) is crucial for cleaving IAV HAs containing monobasic cleavage sites and severe acute respiratory syndrome (SARS)-CoV-2 S in human airway cells. Here, we analysed and compared the TMPRSS2-dependency of SARS-CoV, Middle East respiratory syndrome (MERS)-CoV, the 1918 pandemic H1N1 IAV and IAV H12, H13 and H17 subtypes in human airway cells. We used the peptide-conjugated morpholino oligomer (PPMO) T-ex5 to knockdown the expression of active TMPRSS2 and determine the impact on virus activation and replication in Calu-3 cells. The activation of H1N1/1918 and H13 relied on TMPRSS2, whereas recombinant IAVs carrying H12 or H17 were not affected by TMPRSS2 knockdown. MERS-CoV replication was strongly suppressed in T-ex5 treated cells, while SARS-CoV was less dependent on TMPRSS2. Our data underline the importance of TMPRSS2 for certain (potentially) pandemic respiratory viruses, including H1N1/1918 and MERS-CoV, in human airways, further suggesting a promising drug target. However, our findings also highlight that IAVs and CoVs differ in TMPRSS2 dependency and that other proteases are involved in virus activation.

Indexed as

SARS-CoV-2Serine EndopeptidasesAnimalsCell LineCoronavirusHemagglutinin Glycoproteins, Influenza VirusHumansInfluenza A virusInfluenza A Virus, H1N1 SubtypeInfluenza, HumanMiddle East Respiratory Syndrome CoronavirusProteolysisSevere acute respiratory syndrome-related coronavirusSpike Glycoprotein, CoronavirusVirus ReplicationHemagglutinin Glycoproteins, Influenza VirusSerine EndopeptidasesSpike Glycoprotein, CoronavirusTMPRSS2 protein, humancoronavirusinfluenza A virusMERS-CoVproteolytic activationSARS-CoVTMPRSS2

Identifiers

PMID39599912
PMCPMC11599139

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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.