Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

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 K(D) =0.4-1.0 microM and K(off) > or =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 (K(D) =29-48 microM and K(off) > or = 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.

Original publication

DOI

10.1002/eji.200424856

Type

Journal article

Journal

Eur J Immunol

Publication Date

04/2004

Volume

34

Pages

930 - 940

Keywords

Activated-Leukocyte Cell Adhesion Molecule, Animals, Antigen Presentation, Antigen-Presenting Cells, Antigens, CD, Antigens, Differentiation, T-Lymphocyte, Flow Cytometry, Humans, Lymphocyte Activation, Polymerase Chain Reaction, Rats, T-Lymphocytes