ArticleFrontiers in immunology2024
Activation of the NLRP3 inflammasome by human adenovirus type 7 L4 100-kilodalton protein.
Article in Frontiers in immunology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 3 citations in OpenAlex.
- The 100 K protein of adenovirus: character, location, and function.Archives of virology · 2026Review
- Interpretable machine learning identifies a clinically inferred inflammasome-associated inflammatory injury phenotype in children with adenovirus pneumonia.Frontiers in cellular and infection microbiology · 2026Article
- High prevalence and pathogen-specific variations of co-infections in pediatric adenovirus pneumonia: a retrospective epidemiological analysis from Northern China.Italian journal of pediatrics · 2025Article
- Pyroptosis in Respiratory Virus Infections: A Narrative Review of Mechanisms, Pathophysiology, and Potential Therapeutic Interventions.Microorganisms · 2025Review
- Activation of pyroptosis impairs basal cell differentiation in the nasal epithelium in chronic rhinosinusitis with nasal polyps.Molecular medicine reports · 2025Article
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human adenovirus type 7 (HAdV-7) is a significant viral pathogen that causes respiratory infections in children. Currently, there are no specific antiviral drugs or vaccines for children targeting HAdV-7, and the mechanisms of its pathogenesis remain unclear. The NLRP3 inflammasome-driven inflammatory cascade plays a crucial role in the host's antiviral immunity. Our previous study demonstrated that HAdV-7 infection activates the NLRP3 inflammasome. Building upon this finding, our current study has identified the L4 100 kDa protein encoded by HAdV-7 as the primary viral component responsible for NLRP3 inflammasome activation. By utilizing techniques such as co-immunoprecipitation, we have confirmed that the 100 kDa protein interacts with the NLRP3 protein and facilitates the assembly of the NLRP3 inflammasome by binding specifically to the NACHT and LRR domains of NLRP3. These insights offer a deeper understanding of HAdV-7 pathogenesis and contribute to the development of novel antiviral therapies.
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