ArticlePloS one2015
TMPRSS2 Isoform 1 Activates Respiratory Viruses and Is Expressed in Viral Target Cells.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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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.
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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.
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Who cites it
27 citing papers in PubMed, 65 citations in OpenAlex.
- Expression ofBiomedical reports · 2025Article
- Computational screening combined with well-tempered metadynamics simulations identifies potential TMPRSS2 inhibitors.Scientific reports · 2024Article
- TMPRSS2 isoform 1 downregulation by G-quadruplex stabilization induces SARS-CoV-2 replication arrest.BMC biology · 2024Article
- Article
- Unravelling the Role of P300 and TMPRSS2 in Prostate Cancer: A Literature Review.International journal of molecular sciences · 2023Review
- Interaction of copper potential metallodrugs with TMPRSS2: A comparative study of docking tools and its implications on COVID-19.Frontiers in chemistry · 2023Article
- Molecular mechanisms involved in anosmia induced by SARS-CoV-2, with a focus on the transmembrane serine protease TMPRSS2.Archives of virology · 2022Review
- Identification of cap-dependent endonuclease inhibitors with broad-spectrum activity against bunyaviruses.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The Transmembrane Protease TMPRSS2 as a Therapeutic Target for COVID-19 Treatment.International journal of molecular sciences · 2022Review
- Host factors: Implications in immunopathogenesis of COVID-19.Pathology, research and practice · 2021Review
- Article
- Overcoming Culture Restriction for SARS-CoV-2 in Human Cells Facilitates the Screening of Compounds Inhibiting Viral Replication.Antimicrobial agents and chemotherapy · 2021Article
- The Immunological Role of the Placenta in SARS-CoV-2 Infection-Viral Transmission, Immune Regulation, and Lactoferrin Activity.International journal of molecular sciences · 2021Review
- Protective Role of aGenes · 2021Article
- Term Human Placental Trophoblasts Express SARS-CoV-2 Entry Factors ACE2, TMPRSS2, and Furin.mSphere · 2021Article
- Host Sex Steroids Interact With Virus Infection: New Insights Into Sex Disparity in Infectious Diseases.Frontiers in microbiology · 2021Review
- An updated review of the association of host genetic factors with susceptibility and resistance to COVID-19.Journal of cellular physiology · 2021Review
- Contributions of human ACE2 and TMPRSS2 in determining host-pathogen interaction of COVID-19.Journal of genetics · 2021Review
- Serine Protease Inhibitors to Treat Lung Inflammatory Diseases.Advances in experimental medicine and biology · 2021Review
- Extracellular vesicles containing ACE2 efficiently prevent infection by SARS-CoV-2 Spike protein-containing virus.Journal of extracellular vesicles · 2020Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cellular protease TMPRSS2 cleaves and activates the influenza virus hemagglutinin (HA) and TMPRSS2 expression is essential for viral spread and pathogenesis in mice. Moreover, severe acute respiratory syndrome coronavirus (SARS-CoV) and other respiratory viruses are activated by TMPRSS2. However, previous studies on viral activation by TMPRSS2 focused on a 492 amino acids comprising form of the protein (isoform 2) while other TMPRSS2 isoforms, generated upon alternative splicing of the tmprss2 mRNA, have not been characterized. Here, we show that the mRNA encoding a TMPRSS2 isoform with an extended N-terminal cytoplasmic domain (isoform 1) is expressed in lung-derived cell lines and tissues. Moreover, we demonstrate that TMPRSS2 isoform 1 colocalizes with HA and cleaves and activates HA. Finally, we show that isoform 1 activates the SARS-CoV spike protein for cathepsin L-independent entry into target cells. Our results indicate that TMPRSS2 isoform 1 is expressed in viral target cells and might contribute to viral activation in the host.
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Registered trials
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.