Human T cells that have been conditioned by the proteolytic activity of the major dust mite allergen Der p 1 trigger enhanced immunoglobulin E synthesis by B cells

Ghaemmaghami, A. M.; Shakib, F.

Abstract

Background: We have previously demonstrated that the proteolytic activity of Der p 1 selectively cleaves human CD25, the 55 kDa α subunit of the IL-2 receptor. As a result of cleavage of surface CD25, peripheral blood T cells produce less IFN-γ and more IL-4, thereby leading to progressive polarization of the T cells towards a Th2 cytokine profile. Therefore, these observations underline the potential role of the proteolytic activity of Der p 1 in creating a microenvironment conducive for IgE synthesis. Objective: To study the effect of T cells that have been conditioned by the proteolytic activity of Der p 1 on IgE synthesis by B cells. Methods: We have examined this concept in experiments whereby T cells that have becn exposed to either proteolytically active or inactive Der p 1 were cocultured with autologous B cells and IgE antibody synthesis was monitored. Results: Here we demonstrate for the first time that coculturing T cells that have been in contact with proteolytically active Der p 1 with autologous B cells leads to augmentation of IgE antibody responses. Conclusions: The proteolytic activity of Der p 1 conditions human T cells, which then become empowered to trigger enhanced IgE synthesis by B cells.

Citation

Ghaemmaghami, A. M., & Shakib, F. (2002). Human T cells that have been conditioned by the proteolytic activity of the major dust mite allergen Der p 1 trigger enhanced immunoglobulin E synthesis by B cells. Clinical and Experimental Allergy, 32(5), 728-732. https://doi.org/10.1046/j.1365-2222.2002.01374.x

• Journal Article Type: Article
• Acceptance Date: Dec 20, 2021
• Online Publication Date: May 2, 2002
• Publication Date: 2002-05
• Deposit Date: Jan 3, 2023
• Journal: Clinical and Experimental Allergy
• Print ISSN: 0954-7894
• Electronic ISSN: 1365-2222
• Publisher: Wiley
• Peer Reviewed: Peer Reviewed
• Volume: 32
• Issue: 5
• Pages: 728-732
• DOI: https://doi.org/10.1046/j.1365-2222.2002.01374.x
• Public URL: https://nottingham-repository.worktribe.com/output/3097657
• Publisher URL: https://onlinelibrary.wiley.com/doi/abs/10.1046/j.1365-2222.2002.01374.x