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TMPRSS2 and Other Host Factors in Influenza Virus and Coronavirus...
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TMPRSS2 and Other Host Factors in Influenza Virus and Coronavirus Infections

A special issue of Viruses (ISSN 1999-4915). This special issue belongs to the section "Human Virology and Viral Diseases".

Deadline for manuscript submissions: 31 January 2026 | Viewed by 5062

Special Issue Editors

Prof. Dr. Judy Wai Ping Yam

E-Mail Website
Guest Editor
Department of Pathology, Li Ka Shing Faculty of Medicine, The University of Hong Kong, Hong Kong
Interests: hepatocellular carcinoma; extracellular vesicles; tumor microenvironment
Dr. Sze Keong Tey

E-Mail Website
Guest Editor
Department of Surgery, Li Ka Shing Faculty of Medicine, The University of Hong Kong, Hong Kong
Interests: TMPRSS2; SARS-CoV-2; extracellular vesicles; tumor microenvironment; cancer metastasis; tumor biology

Special Issue Information

Dear Colleagues,

Since the early 21st century, epidemics and pandemics caused by highly contagious influenza viruses and coronaviruses have imposed a significant burden on global healthcare systems. In addition to the challenges posed by individual pathogens, co-infections involving SARS-CoV-2—the causative agent of the COVID-19 pandemic—together with influenza viruses and other respiratory pathogens have been reported, presenting an even greater threat to public health. Increasing evidence highlights the critical role of host factors, including various host proteins, immune responses, and genetic determinants, in influencing susceptibility to infections and disease severity. Among these, TMPRSS2 has emerged as a key host protein involved in the entry and activation of both influenza viruses and coronaviruses, notably facilitating SARS-CoV-2 cellular entry and priming viral glycoproteins of other respiratory viruses. While its physiological functions remain incompletely understood, TMPRSS2 represents a promising target for antiviral intervention.

This Special Issue aims to showcase the latest research on the role of TMPRSS2 and other host factors in influenza virus and coronavirus infections, offering new insights into mechanistic pathways, transmission dynamics, immune modulation, and epidemiology. We welcome the submission of original research articles, brief research reports, reviews, and communications addressing these important topics.

Prof. Dr. Judy Wai Ping Yam
Dr. Sze Keong Tey
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Viruses is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2600 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • TMPRSS2
  • host factors
  • influenza virus
  • coronavirus
  • viral infection
  • treatment of viral diseases

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Published Papers (2 papers)

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Research

23 pages, 3398 KiB  
Article
Unveiling the Role of TMPRSS2 in the Proteolytic Activation of Pandemic and Zoonotic Influenza Viruses and Coronaviruses in Human Airway Cells
by Marie Schwerdtner, Luna C. Schmacke, Julia Nave, Hannah Limburg, Torsten Steinmetzer, David A. Stein, Hong M. Moulton and Eva Böttcher-Friebertshäuser
Viruses 2024, 16(11), 1798; https://doi.org/10.3390/v16111798 - 20 Nov 2024
Cited by 2 | Viewed by 1710
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 [...] Read more.
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. Full article
(This article belongs to the Special Issue TMPRSS2 and Other Host Factors in Influenza Virus and Coronavirus Infections)
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16 pages, 6480 KiB  
Article
The Transmembrane Protease Serine 2 (TMPRSS2) Non-Protease Domains Regulating Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) Spike-Mediated Virus Entry
by Romano Strobelt, Julia Adler and Yosef Shaul
Viruses 2023, 15(10), 2124; https://doi.org/10.3390/v15102124 - 19 Oct 2023
Cited by 8 | Viewed by 2583
Abstract
The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) enters cells by binding to the angiotensin-converting enzyme 2 (hACE2) receptor. This process is aided by the transmembrane protease serine 2 (TMPRSS2), which enhances entry efficiency and infectiousness by cleaving the SARS-CoV-2 surface glycoprotein (Spike). [...] Read more.
The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) enters cells by binding to the angiotensin-converting enzyme 2 (hACE2) receptor. This process is aided by the transmembrane protease serine 2 (TMPRSS2), which enhances entry efficiency and infectiousness by cleaving the SARS-CoV-2 surface glycoprotein (Spike). The cleavage primes the Spike protein, promoting membrane fusion instead of receptor-mediated endocytosis. Despite the pivotal role played by TMPRSS2, our understanding of its non-protease distinct domains remains limited. In this report, we present evidence indicating the potential phosphorylation of a minimum of six tyrosine residues within the cytosolic tail (CT) of TMPRSS2. Via the use of TMPRSS2 CT phospho-mimetic mutants, we observed a reduction in TMPRSS2 protease activity, accompanied by a decrease in SARS-CoV-2 pseudovirus transduction, which was found to occur mainly via the endosomal pathway. We expanded our investigation beyond TMPRSS2 CT and discovered the involvement of other non-protease domains in regulating infection. Our co-immunoprecipitation experiments demonstrated a strong interaction between TMPRSS2 and Spike. We revealed a 21 amino acid long TMPRSS2-Spike-binding region (TSBR) within the TMPRSS2 scavenger receptor cysteine-rich (SRCR) domain that contributes to this interaction. Our study sheds light on novel functionalities associated with TMPRSS2’s cytosolic tail and SRCR region. Both of these regions have the capability to regulate SARS-CoV-2 entry pathways. These findings contribute to a deeper understanding of the complex interplay between viral entry and host factors, opening new avenues for potential therapeutic interventions. Full article
(This article belongs to the Special Issue TMPRSS2 and Other Host Factors in Influenza Virus and Coronavirus Infections)
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