Monoclonal antibody and ligand binding sites of the T cell erythrocyte receptor (CD2)

@article{Peterson1987MonoclonalAA,  title={Monoclonal antibody and ligand binding sites of the T cell erythrocyte receptor (CD2)},  author={Andrew S. Peterson and Brian Seed},  journal={Nature},  year={1987},  volume={329},  pages={842-846},  url={https://api.semanticscholar.org/CorpusID:4315968}}
Good agreement was observed between mutational lesions blocking LFA-3 binding and lesions blocking binding by activating antibodies, which supports the view that such antibodies induce T cell activation by mimicking the effect of LFA -3 binding.

134 Citations

Synergistic T cell activation via the physiological ligands for CD2 and the T cell receptor

The results suggest that the CD2/LFA-3 interaction not only plays a role in cell-cell adhesion but provides a stimulatory signal for T cell activation.

Structure and function of the erythrocyte receptor CD2 on human T lymphocytes: a review.

expression and biochemical analysis of a soluble extracellular domain CD2 molecule reveal that it expresses native CD2 epitopes and contains a stable 15kd NH2-terminal fragment corresponding to a single exon, suggesting that T cell-target adhesion mediated by CD2 and its ligand depends on multimeric attachment between an array of CD2 molecules and their cognate ligands.

Amino acid residues required for binding of lymphocyte function- associated antigen 3 (CD58) to its counter-receptor CD2

The data show that K30 and K34, in the predicted C-C' loop, and D84, inThe predicted F-G loop of LFA- 3, are involved in binding to CD2, suggesting that two complementary sites on one face of the first domain of each molecule bind to each other.

Structural and functional epitopes of the human adhesion receptor CD58 (LFA‐3)

Six structurally and/or functionally distinct epitopes on the CD58 molecule are described, found to be present in equal numbers on a wide range of CD58+ cells, none of them being differentially up‐regulated following cell activation or malignant transformation.

Specific interaction of lymphocyte function-associated antigen 3 with CD2 can inhibit T cell responses

It is demonstrated that a soluble, purified first domain-LFA-3/IgG1 fusion protein (LFA3TIP) interacts with CD2 and binds to the same CD2 epitope as purified multimeric or cell surface-expressed L FA-3, and is capable of inducing T cell unresponsiveness to secondary stimulation in allogeneic MLR.

Human cell-adhesion molecule CD2 binds CD58 (LFA-3) with a very low affinity and an extremely fast dissociation rate but does not bind CD48 or CD59.

CD2 is a T lymphocyte cell-adhesion molecule (CAM) belonging to the immunoglobulin superfamily (IgSF) which mediates transient adhesion of T cells to antigen-presenting cells and target cells.…

The CD2 ligand LFA-3 activates T cells but depends on the expression and function of the antigen receptor.

It is demonstrated that LFA-3 under appropriate conditions can activate T cells via the CD2 complex and that this activation requires not only the cell surface expression of the CD3/Ti complex but also a functional Ag receptor pathway.
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30 References

Alternative pathway activation of T cells by binding of CD2 to its cell-surface ligand

It is demonstrated that binding of this cell surface molecule, termed T11 target structure or T11TS, to CD2 (T11) induces reactivity in resting T cells to a mitogenic stimulus given by a mAb to the T113 determinant or by submitogenic concentrations of anti-T112+3 mAbs.

The T lymphocyte glycoprotein CD2 binds the cell surface ligand LFA-3

It is reported that purified CD2 binds to a cell-surface antigen known as lymphocyte function-associated anti-gen-3 (LFA-3) with high affinity, and can mediate adhesion of lymphoid cells via interaction with L FA-3, suggesting that CD2 can function in signalling as well as being an adhesion molecule.

Identification and functional characterization of two distinct epitopes on the human T cell surface protein Tp50.

The structural and functional domains of Tp50, the human T lymphocyte surface protein associated with the E rosette receptor, were probed with the use of two murine monoclonal antibodies to support the interpretation that the differences between the antibodies in their effects on E ro Sette formation and natural killer function stem from the fact that they bind to distinct epitopes of T p50.

A common pathway for T lymphocyte activation involving both the CD3-Ti complex and CD2 sheep erythrocyte receptor determinants.

It is demonstrated that anti-CD3 (SP34) induces epitopic modulation of the CD2 molecule, resulting in enhanced expression of theCD2, 9-1 epitope, suggesting that the T cell differentiation antigens CD3 and CD2 are jointly involved in antigen-specific T cell activation.

The ligand of the erythrocyte receptor of T lymphocytes: expression on white blood cells and possible involvement in T cell activation.

It is shown that T11 is also expressed on sheep white blood cells, notably on activated T lymphocytes, that are shown to actively synthesize this cell surface GP, and that the mixed lymphocyte reaction between outbred sheep is inhibited by mAb L180/1 at an early stage of the response.

Two antigen-independent adhesion pathways used by human cytotoxic T-cell clones

These studies suggest that CD2 on the effector interacts with LFA-3 as its ligand on targets, and the existence of distinct pathways is confirmed by the demonstration that L FA-1-dependent adhesion requires divalent cations and is temperature-sensitive whereas CD2- and LFA -3- dependent adhesion does not require divalentCations and was temperature-insensitive.

Thymocyte binding to human thymic epithelial cells is inhibited by monoclonal antibodies to CD-2 and LFA-3 antigens.

TE cell-thymocyte binding is blocked by antibodies to theCD-2 (T11) antigen on thymocytes and by an antibody to the LFA-3 antigen on TE cells, suggesting that a natural ligand for T cell activation via the CD-2 molecule is present on human thymic epithelial cells.

The murine homologue of the T lymphocyte CD2 antigen: molecular cloning, chromosome assignment and cell surface expression

Experiments with monoclonal antibodies against CD2 suggest that CD2 is the cell surface receptor for a natural ligand involved in T cell proliferation, and Clarification of the functional role of CD2 would be facilitated by the identification ofCD2 in the mouse.

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