An IL-7 Fusion Protein That Shows Increased Thymopoietic Ability
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The role of IL-7 during thymopoiesis has led to it being the focus of a number of therapeutic interventions. However, its small size and pleiotropic nature present problems for thymus-directed therapies. We have created a fusion molecule between the extracellular N-terminal domain of CCR9 and IL-7, which has the potential to overcome these difficulties. This novel fusion protein retains the thymopoietic activity of IL-7 and the ligand-binding ability of CCR9. As a thymopoietic agent, compared with IL-7, it shows an enhanced retention in the thymus, increased de novo T cell production, and increased thymic output. Old mice receiving the fusion protein show improved CD8 T cell responses and reduced viral load after infection with influenza virus compared with those receiving IL-7. This chimeric molecule offers a novel therapeutic strategy that may result in the production of an effective immunorestorative agent.
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The IL-7 fusion protein, IL-7 binding to the N-terminal extracellular domain of CCR9, could restore the thymus structure in elderly individuals.
“it was reported that the IL-7 fusion protein, that is, IL-7 binding to the N-terminal extracellular domain of CCR9, could restore the thymus structure in elderly individuals [173]”
From Immunosenescence: a key player in cancer development (2020) · cites this paper as [173]
IL-7 targeting the thymus of the elderly may restore the development of T cells in the elderly.
“IL-7 targeting the thymus of the elderly may also restore the development of T cells in the elderly.”
From Immunosenescence: a key player in cancer development (2020) · cites this paper as [173]
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Self-citation
- Authors
- Henson, S. M., Snelgrove, R., Hussell, T., Wells, D. J., & Aspinall, R.
- Affiliations
- Department of Immunology, Imperial College, Chelsea and Westminster Hospital , London ,
- Imperial College London (GB)
- Charing Cross Hospital (GB)
- Chelsea and Westminster Hospital (GB)
- Corresponding author
- Aspinall, Richard
- Venue
- The Journal of Immunology
- Publisher
- Oxford University Press (OUP)
- Published
- 2005-09
- Volume
- 175
- Issue
- 6
- Pages
- 4112-4118
- ISSN
- 0022-1767 (ISSN-L)
- 1550-6606
- OpenAlex
- W1856903046
- Cited by
- 55
- References
- 43
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 2 · 2022: 3 · 2021: 5 · 2020: 3 · 2019: 3 · 2018: 3 · 2017: 1 · 2016: 1 · 2013: 1 · 2012: 4
- FWCI
- 1.54
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Journal of Immunology (publishedVersion)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Research Explorer (The University of Manchester) (submittedVersion)
- Funders
- Directorate for Biological Sciences
- Biotechnology and Biological Sciences Research Council
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
- Life Sciences › Immunology and Microbiology › Immunology › Immunotherapy and Immune Responses
- Life Sciences › Immunology and Microbiology › Immunology › Immunotoxicology and immune responses
- Keywords
- IL-7, CCR9, fusion protein, thymopoiesis, T cell production, thymic output, CD8+ T cell responses, influenza, immunorestoration, ligand binding
- MeSH terms
- Animals, Influenza, Human, Mice, Inbred C57BL, Recombinant Fusion Proteins, T-Lymphocytes, Thymus Gland, Protein Engineering, Interleukin-7, CD8-Positive T-Lymphocytes, Viral Load, Receptors, Chemokine, Cell Proliferation, Mice, Receptors, CCR
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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