MRC OX-2 antigen: a lymphoid/neuronal membrane glycoprotein with a structure like a single immunoglobulin light chain.

Clark, M.J.; Gagnon, Jean; Williams, Alan F.; Barclay, A. Neil

doi:10.1002/j.1460-2075.1985.tb02324.x

Cited by 155 publications

(62 citation statements)

References 30 publications

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“…Consistent with this are data showing that cell-cell contact leads to down-regulation of myeloid cells through CD200R [5] and targeting the CD200R with Fc fusion proteins and antibodies can ameliorate autoimmune diseases [6,7]. CD200 and CD200R both contain two IgSF domains like many surface proteins at the leukocyte cell surface [2,8,9]. In T cells these proteins often interact with other proteins with two IgSF domains in an end-to-end topology.…”

Section: Introductionmentioning

confidence: 52%

The CD200 and CD200 receptor cell surface proteins interact through their N‐terminal immunoglobulin‐like domains

Hatherley

Barclay

2004

Eur J Immunol

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CD200 (OX2) is a broadly distributed cell surface glycoprotein that interacts with a receptor on myeloid cells (CD200R) involved in regulation of macrophage function. Both CD200 and CD200R contain two Ig superfamily domains like many other leukocyte membrane proteins. Site‐directed mutagenesis of CD200R showed that, like CD200, it interacted through its N‐terminal domain. This indicated that the cell‐cell interaction spans four Ig superfamily domains and this distance is similar to many interactions found between T cells and antigen‐presenting cells. This suggests that this topology is also important in interactions of CD200 on a variety of cells with CD200R on myeloid cells, and comparable contact sites may be important mediating regulation in other cell‐cell interactions. The mutagenesis showed that the binding involved the predicted GFCC′ face of its N‐terminal domain, like that of CD200, suggesting that the interaction evolved from a homotypic interaction.

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Section: Introductionmentioning

confidence: 52%

The CD200 and CD200 receptor cell surface proteins interact through their N‐terminal immunoglobulin‐like domains

Hatherley

Barclay

2004

Eur J Immunol

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“…The widely expressed glycoprotein CD200 is closely related structurally to the T cell costimulatory molecules CD80 and CD86 and is genetically linked to them on human chromosome 3 and mouse chromosome 16 (7,8). Structurally, CD200 contains two Ig superfamily (IgSF) domains in a typical V/C2 arrangement (9).…”

Section: Yeloid Cells (Ie Macrophages Dendritic Cells (Dc)mentioning

confidence: 99%

Regulation of Myeloid Cell Function through the CD200 Receptor

Jenmalm¹,

Cherwinski²,

Bowman³

et al. 2006

The Journal of Immunology

204

172

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Myeloid cells play pivotal roles in chronic inflammatory diseases through their broad proinflammatory, destructive, and remodeling capacities. CD200 is widely expressed on a variety of cell types, while the recently identified CD200R is expressed on myeloid cells and T cells. CD200 deletion in vivo results in myeloid cell dysregulation and enhanced susceptibility to autoimmune inflammation, suggesting that the CD200-CD200R interaction is involved in immune suppression. We demonstrate in this study that CD200R agonists suppress mouse and human myeloid cell function in vitro, and also define a dose relationship between receptor expression and cellular inhibition. IFN-γ- and IL-17-stimulated cytokine secretion from mouse peritoneal macrophages was inhibited by CD200R engagement. Inhibitory effects were not universal, as LPS-stimulated responses were unaffected. Inhibition of U937 cell cytokine production correlated with CD200R expression levels, and inhibition was only observed in low CD200R expressing cells, if the CD200R agonists were further cross-linked. Tetanus toxoid-induced human PBMC IL-5 and IL-13 secretion was inhibited by CD200R agonists. This inhibition was dependent upon cross-linking the CD200R on monocytes, but not on cross-linking the CD200R on CD4+ T cells. In all, we provide direct evidence that the CD200-CD200R interaction controls monocyte/macrophage function in both murine and human systems, further supporting the potential clinical application of CD200R agonists for the treatment of chronic inflammatory diseases.

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“…One recently characterized interaction is that between the CD200 (OX2) membrane protein, which is expressed on a variety of cells, including activated T cells, B cells, follicular dendritic cells, neurons, and vascular endothelium (2,7,28,41,43), and its receptor (CD200R), which is restricted mainly to myeloid cells (42,44). CD200 contains two extracellular immunoglobulin superfamily (IgSF) domains, a hydrophobic transmembrane sequence and a short cytoplasmic region that is devoid of any known signaling motifs (3,12). CD200R also contains two extracellular IgSF domains but differs in that it has a substantial cytoplasmic region that contains tyrosine-based motifs that can be phosphorylated, suggesting that it is capable of signaling events within myeloid cells (44).…”

mentioning

confidence: 99%

Human Herpesvirus 8 K14 Protein Mimics CD200 in Down-Regulating Macrophage Activation through CD200 Receptor

Foster-Cuevas

Wright

Puklavec

et al. 2004

J Virol

110

140

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Many viral proteins limit host immune defenses, and their genes often originate from their hosts. CD200 (OX2) is a broadly distributed cell surface glycoprotein that interacts with a receptor on myeloid cells (CD200R) that is implicated in locally preventing macrophage activation. Distant, but recognizable, homologues of CD200 have been identified in many herpesviruses and poxviruses. Here, we show that the product of the K14 open reading frame from human herpesvirus 8 (Kaposi's sarcoma-associated herpesvirus) interacts with human CD200R and is expressed at the surfaces of infected cells solely during the lytic cycle. Despite sharing only 40% primary sequence identity, K14 and CD200 interacted with CD200R with an almost identical and low affinity (K D ‫؍‬ 0.5 M), in contrast to other characterized viral homologue interactions. Cells expressing CD200 or K14 on the cell surface were able to inhibit secretion by activated macrophages of proinflammatory cytokines such as tumor necrosis factor alpha, an effect that could be specifically relieved by addition of monoclonal antibodies and soluble monomeric CD200 protein. We conclude that CD200 delivers local down-modulatory signals to myeloid cells through direct cell-cell contact and that the K14 viral homologue closely mimics this.

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MRC OX-2 antigen: a lymphoid/neuronal membrane glycoprotein with a structure like a single immunoglobulin light chain.

Cited by 155 publications

References 30 publications

The CD200 and CD200 receptor cell surface proteins interact through their N‐terminal immunoglobulin‐like domains

The CD200 and CD200 receptor cell surface proteins interact through their N‐terminal immunoglobulin‐like domains

Regulation of Myeloid Cell Function through the CD200 Receptor

Human Herpesvirus 8 K14 Protein Mimics CD200 in Down-Regulating Macrophage Activation through CD200 Receptor

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