An IL-7 fusion protein that shows increased thymopoietic ability

SM Henson, R Snelgrove, T Hussell… - The Journal of …, 2005 - journals.aai.org
SM Henson, R Snelgrove, T Hussell, DJ Wells, R Aspinall
The Journal of Immunology, 2005journals.aai.org
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 …
Abstract
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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