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...

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Veröffentlicht in:European journal of immunology 2004-04, Vol.34 (4), p.930-940
Hauptverfasser: Hassan, Namir J., Barclay, A. Neil, Brown, Marion H.
Format: Artikel
Sprache:eng
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Zusammenfassung: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.
ISSN:0014-2980
1521-4141
DOI:10.1002/eji.200424856