Reviving lost binding sites: Exploring calcium‐binding site transitions between human and murine CD23
Immunoglobulin E (IgE) is a central regulatory and triggering molecule of allergic immune responses. IgE’s interaction with CD23 modulates both IgE production and functional activities.CD23 is a noncanonical immunoglobulin receptor, unrelated to receptors of other antibody isotypes. Human CD23 is a...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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Wiley
2021-07-01
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| Series: | FEBS Open Bio |
| Subjects: | |
| Online Access: | https://doi.org/10.1002/2211-5463.13214 |
| _version_ | 1818733294783561728 |
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| author | Veronica F. Ilkow Anna M. Davies Balvinder Dhaliwal Andrew J. Beavil Brian J. Sutton James M. McDonnell |
| author_facet | Veronica F. Ilkow Anna M. Davies Balvinder Dhaliwal Andrew J. Beavil Brian J. Sutton James M. McDonnell |
| author_sort | Veronica F. Ilkow |
| collection | DOAJ |
| description | Immunoglobulin E (IgE) is a central regulatory and triggering molecule of allergic immune responses. IgE’s interaction with CD23 modulates both IgE production and functional activities.CD23 is a noncanonical immunoglobulin receptor, unrelated to receptors of other antibody isotypes. Human CD23 is a calcium‐dependent (C‐type) lectin‐like domain that has apparently lost its carbohydrate‐binding capability. The calcium‐binding site classically required for carbohydrate binding in C‐type lectins is absent in human CD23 but is present in the murine molecule. To determine whether the absence of this calcium‐binding site affects the structure and function of human CD23, CD23 mutant proteins with increasingly “murine‐like” sequences were generated. Restoration of the calcium‐binding site was confirmed by NMR spectroscopy, and structures of mutant human CD23 proteins were determined by X‐ray crystallography, although no electron density for calcium was observed. This study offers insights into the evolutionary differences between murine and human CD23 and some of the functional differences between CD23 in different species. |
| first_indexed | 2024-12-17T23:47:11Z |
| format | Article |
| id | doaj.art-5fcdc2e1fa9d4377b70934cd23407cfe |
| institution | Directory Open Access Journal |
| issn | 2211-5463 |
| language | English |
| last_indexed | 2024-12-17T23:47:11Z |
| publishDate | 2021-07-01 |
| publisher | Wiley |
| record_format | Article |
| series | FEBS Open Bio |
| spelling | doaj.art-5fcdc2e1fa9d4377b70934cd23407cfe2022-12-21T21:28:16ZengWileyFEBS Open Bio2211-54632021-07-011171827184010.1002/2211-5463.13214Reviving lost binding sites: Exploring calcium‐binding site transitions between human and murine CD23Veronica F. Ilkow0Anna M. Davies1Balvinder Dhaliwal2Andrew J. Beavil3Brian J. Sutton4James M. McDonnell5Randall Centre for Cell & Molecular Biophysics King’s College London UKRandall Centre for Cell & Molecular Biophysics King’s College London UKRandall Centre for Cell & Molecular Biophysics King’s College London UKRandall Centre for Cell & Molecular Biophysics King’s College London UKRandall Centre for Cell & Molecular Biophysics King’s College London UKRandall Centre for Cell & Molecular Biophysics King’s College London UKImmunoglobulin E (IgE) is a central regulatory and triggering molecule of allergic immune responses. IgE’s interaction with CD23 modulates both IgE production and functional activities.CD23 is a noncanonical immunoglobulin receptor, unrelated to receptors of other antibody isotypes. Human CD23 is a calcium‐dependent (C‐type) lectin‐like domain that has apparently lost its carbohydrate‐binding capability. The calcium‐binding site classically required for carbohydrate binding in C‐type lectins is absent in human CD23 but is present in the murine molecule. To determine whether the absence of this calcium‐binding site affects the structure and function of human CD23, CD23 mutant proteins with increasingly “murine‐like” sequences were generated. Restoration of the calcium‐binding site was confirmed by NMR spectroscopy, and structures of mutant human CD23 proteins were determined by X‐ray crystallography, although no electron density for calcium was observed. This study offers insights into the evolutionary differences between murine and human CD23 and some of the functional differences between CD23 in different species.https://doi.org/10.1002/2211-5463.13214calciumCD23CTLDFcεRIIIgEimmunoglobulin E |
| spellingShingle | Veronica F. Ilkow Anna M. Davies Balvinder Dhaliwal Andrew J. Beavil Brian J. Sutton James M. McDonnell Reviving lost binding sites: Exploring calcium‐binding site transitions between human and murine CD23 FEBS Open Bio calcium CD23 CTLD FcεRII IgE immunoglobulin E |
| title | Reviving lost binding sites: Exploring calcium‐binding site transitions between human and murine CD23 |
| title_full | Reviving lost binding sites: Exploring calcium‐binding site transitions between human and murine CD23 |
| title_fullStr | Reviving lost binding sites: Exploring calcium‐binding site transitions between human and murine CD23 |
| title_full_unstemmed | Reviving lost binding sites: Exploring calcium‐binding site transitions between human and murine CD23 |
| title_short | Reviving lost binding sites: Exploring calcium‐binding site transitions between human and murine CD23 |
| title_sort | reviving lost binding sites exploring calcium binding site transitions between human and murine cd23 |
| topic | calcium CD23 CTLD FcεRII IgE immunoglobulin E |
| url | https://doi.org/10.1002/2211-5463.13214 |
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