Frontline: Optimal T cell activation requires the engagement of CD6 and CD166
The T cell surface glycoprotein, CD6 binds CD166 in the first example of an interaction between a scavenger receptor cysteine-rich domain and an immunoglobulin-like domain. We report that in human these proteins interact with a KD =0.4-1.0 μM and Koff ≥0.4-0.63 s-1, typical of many leukocyte membran...
| Main Authors: | , , |
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| Format: | Journal article |
| Language: | English |
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2004
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| _version_ | 1826273097245786112 |
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| author | Hassan, N Barclay, N Brown, M |
| author_facet | Hassan, N Barclay, N Brown, M |
| author_sort | Hassan, N |
| collection | OXFORD |
| description | The T cell surface glycoprotein, CD6 binds CD166 in the first example of an interaction between a scavenger receptor cysteine-rich domain and an immunoglobulin-like domain. We report that in human these proteins interact with a KD =0.4-1.0 μM and Koff ≥0.4-0.63 s-1, typical of many leukocyte membrane protein interactions. CD166 also interacts in a homophilic manner but with around 100-fold lower affinity (KD =29-48 μM and Koff ≥ 5.3 s-1). At concentrations, that will block the CD6/CD166 interaction, soluble monomeric CD6 and CD166 inhibit antigen-specific human T cell responses. This is consistent with extracellular engagement between CD6 and CD166 being required for an optimal immune response. © 2004 Wiley-VCH Verlag GmbH and Co. KGaA. |
| first_indexed | 2024-03-06T22:22:59Z |
| format | Journal article |
| id | oxford-uuid:55b47e16-da25-4351-9555-506c2c426f7c |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T22:22:59Z |
| publishDate | 2004 |
| record_format | dspace |
| spelling | oxford-uuid:55b47e16-da25-4351-9555-506c2c426f7c2022-03-26T16:45:42ZFrontline: Optimal T cell activation requires the engagement of CD6 and CD166Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:55b47e16-da25-4351-9555-506c2c426f7cEnglishSymplectic Elements at Oxford2004Hassan, NBarclay, NBrown, MThe T cell surface glycoprotein, CD6 binds CD166 in the first example of an interaction between a scavenger receptor cysteine-rich domain and an immunoglobulin-like domain. We report that in human these proteins interact with a KD =0.4-1.0 μM and Koff ≥0.4-0.63 s-1, typical of many leukocyte membrane protein interactions. CD166 also interacts in a homophilic manner but with around 100-fold lower affinity (KD =29-48 μM and Koff ≥ 5.3 s-1). At concentrations, that will block the CD6/CD166 interaction, soluble monomeric CD6 and CD166 inhibit antigen-specific human T cell responses. This is consistent with extracellular engagement between CD6 and CD166 being required for an optimal immune response. © 2004 Wiley-VCH Verlag GmbH and Co. KGaA. |
| spellingShingle | Hassan, N Barclay, N Brown, M Frontline: Optimal T cell activation requires the engagement of CD6 and CD166 |
| title | Frontline: Optimal T cell activation requires the engagement of CD6 and CD166 |
| title_full | Frontline: Optimal T cell activation requires the engagement of CD6 and CD166 |
| title_fullStr | Frontline: Optimal T cell activation requires the engagement of CD6 and CD166 |
| title_full_unstemmed | Frontline: Optimal T cell activation requires the engagement of CD6 and CD166 |
| title_short | Frontline: Optimal T cell activation requires the engagement of CD6 and CD166 |
| title_sort | frontline optimal t cell activation requires the engagement of cd6 and cd166 |
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