Evidence map›Paper›PMID 40297833›Full record

ReviewScientifica2025

Exploring TMPRSS2 Drug Target to Combat Influenza and Coronavirus Infection.

Krishnaprasad Baby, Megh Pravin Vithalkar, Somasish Ghosh Dastidar, Chiranjay Mukhopadhyay, Rania Hamdy, Sameh S M Soliman, Yogendra Nayak

Abstract readReview
In one paragraph

Review in Scientifica, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Identification ofRSC medicinal chemistry · 2026
    Article
  5. Acute pulmonary inflammatory reaction in COVID-19 - histological and immunohistochemical study.Romanian journal of morphology and embryology = Revue roumaine de morphologie et embryologie
    Article
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

7 authors.

Krishnaprasad BabyDepartment of Pharmacology, Manipal College of Pharmaceutical Sciences, Manipal Academy of Higher Education, Manipal, Karnataka 576104, India.ORCID https://orcid.org/0000-0002-1753-2332
Megh Pravin VithalkarDepartment of Pharmacology, Manipal College of Pharmaceutical Sciences, Manipal Academy of Higher Education, Manipal, Karnataka 576104, India.ORCID https://orcid.org/0009-0001-0186-4906
Somasish Ghosh DastidarCentre for Molecular Neurosciences, Kasturba Medical College, Manipal Academy of Higher Education, Manipal, Karnataka 576104, India.ORCID https://orcid.org/0000-0003-4123-1801
Chiranjay MukhopadhyayManipal Institute of Virology, Manipal Academy of Higher Education, Manipal, Karnataka 576104, India.ORCID https://orcid.org/0000-0003-0402-1143
Rania HamdyResearch Institute for Science and Engineering (RISE), University of Sharjah, Sharjah 27272, UAE.ORCID https://orcid.org/0000-0002-4748-8790
Sameh S M SolimanResearch Institute for Medical and Health Sciences, University of Sharjah, P.O. Box 27272, Sharjah, UAE.ORCID https://orcid.org/0000-0002-7691-615X
Yogendra NayakDepartment of Pharmacology, Manipal College of Pharmaceutical Sciences, Manipal Academy of Higher Education, Manipal, Karnataka 576104, India.ORCID https://orcid.org/0000-0002-0508-1394

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Respiratory viral infections, including influenza and coronaviruses, present significant health risks worldwide. The recent COVID-19 pandemic highlights the urgent need for novel and effective antiviral agents. The host cell protease, transmembrane serine protease 2 (TMPRSS2), facilitates viral pathogenesis by playing a critical role in viral invasion and disease progression. This protease is coexpressed with the viral receptors of angiotensin-converting enzyme 2 (ACE2) for SARS-CoV-2 in the human respiratory tract and plays a significant role in activating viral proteins and spreading. TMPRSS2 activates the coronavirus spike (S) protein and permits membrane fusion and viral entry by cleaving the virus surface glycoproteins. It also activates the hemagglutinin (HA) protein, an enzyme necessary for the spread of influenza virus. TMPRSS2 inhibitors can reduce viral propagation and morbidity by blocking viral entry into respiratory cells and reducing viral spread, inflammation, and disease severity. This review examines the role of TMPRSS2 in viral replication and pathogenicity. It also offers potential avenues to develop targeted antivirals to inhibit TMPRSS2 function, suggesting a possible focus on targeted antiviral development. Ultimately, the review seeks to contribute to improving public health outcomes related to these viral infections.

Indexed as

antiviral therapycoronavirusCOVID-19 treatmenthost proteasesinfluenza virusprotease inhibitionpublic health strategiesSARS-CoV-2tTMPRSS2viral pathogenesis

Identifiers

PMID40297833
PMCPMC12037250

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.