Demonstration of a second ligand for the low affinity receptor for immunoglobulin E (CD23) using recombinant CD23 reconstituted into fluorescent liposomes.

Pochon, Sibylle; Graber, Pierre; Yeager, Mark; Jansen, Kathrin U.; Bernard, Alain K.; Aubry, Jean‐Pierre; Bonnefoy, Jean‐Yves

doi:10.1084/jem.176.2.389

Cited by 68 publications

(23 citation statements)

References 34 publications

(31 reference statements)

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“…One potential explanation is that the interaction with alternate ligands such as CD21 (37), CD11 (38), or CD47-vitronectin (39) is both not temperature sensitive and is triggering the observed IgE regulation. Alternatively, the multipoint interaction when both the CD23 and surface IgE are membrane bound may make a lower affinity interaction sufficient for triggering.…”

Section: Discussionmentioning

confidence: 99%

Temperature Effect on IgE Binding to CD23 Versus FcεRI

Chen

Kilmon

et al. 2003

The Journal of Immunology

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A chimeric soluble CD23, consisting of the extracellular domain of mouse CD23 and a modified leucine zipper (lz-CD23), has been shown to inhibit IgE binding to the FcεRI. A similar human CD23 construct was also shown to inhibit binding of human IgE to human FcεRI. In both systems, the inhibition was found to be temperature dependent; a 10-fold molar excess of lz-CD23 gave 90–98% inhibition at 4°C, dropping to 20–30% inhibition at 37°C. Surface plasmon resonance analysis of lz-CD23 binding to an IgE-coated sensor chip suggested that the effective concentration of lz-CD23 was lower at the higher temperatures. Analysis of 125I-IgE binding to CD23+-Chinese hamster ovary cells also indicated that increased temperature resulted in a lower percentage of IgE capable of interacting with CD23. In contrast, IgE interacts more effectively with FcεRI+-rat basophilic leukemia cells at 37°C compared with 4°C. The results support the concept that the open and closed IgE structures found by crystallography interact differently with the two IgE receptors and suggest that temperature influences the relative percentage of IgE in the respective structural forms. Changes in CD23 oligomerization also plays a role in the decreased binding seen at physiological temperatures.

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Section: Discussionmentioning

confidence: 99%

Temperature Effect on IgE Binding to CD23 Versus FcεRI

Chen

Kilmon

et al. 2003

The Journal of Immunology

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“…Known ligands to CD21 include the lowaffinity receptor for IgE (CD23), the EBV envelope glycoprotein gp350, and the complement factor C3d (25). It was shown that exosomes released from B cells and macrophages contain C3 fragments (26), but because heat-inactivated FCS was used in all of our cell cultures, C3d is unlikely to make a difference.…”

Section: Gp350 On Lcl1 Exosomes Mediates the Binding To B Cellsmentioning

confidence: 99%

Exosomes Containing Glycoprotein 350 Released by EBV-Transformed B Cells Selectively Target B Cells through CD21 and Block EBV Infection In Vitro

Vallhov

Gutzeit

Johansson

et al. 2011

The Journal of Immunology

122

113

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Exosomes are nano-sized membrane vesicles released from a wide variety of cells, formed in endosomes by inward budding of the endosomal limiting membrane. They have immune stimulatory-, inhibitory-, or tolerance-inducing effects, depending on their cellular origin, which is why they are investigated for use in vaccine and immune therapeutic strategies. In this study, we explored whether exosomes of different origins and functions can selectively target different immune cells in human peripheral blood. Flow cytometry, confocal laser scanning microscopy, and multispectral imaging flow cytometry (ImageStream) revealed that exosomes derived from human monocyte-derived dendritic cells and breast milk preferably associated with monocytes. In contrast, exosomes from an EBV-transformed B cell line (LCL1) preferentially targeted B cells. This was not observed for an EBV− B cell line (BJAB). Electron microscopy, size-distribution analysis (NanoSight), and a cord blood transformation assay excluded the presence of virions in our LCL1 exosome preparations. The interaction between LCL1-derived exosomes and peripheral blood B cells could be blocked efficiently by anti-CD21 or anti-gp350, indicating an interaction between CD21 on B cells and the EBV glycoprotein gp350 on exosomes. The targeting of LCL1-derived exosomes through gp350–CD21 interaction strongly inhibited EBV infection in B cells isolated from umbilical cord blood, suggesting a protective role for exosomes in regulating EBV infection. Our finding also suggests that exosome-based vaccines can be engineered for specific B cell targeting by inducing gp350 expression.

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“…9,16 However, the fact that inhibition with the sugars was much more profound and also affected proliferation suggests that their action may not be confined strictly to CD23/CD21 but that they can also interfere with other molecular interactions. In contrast to the apparent complexity of signals involved in regulating differentiation and IgE synthesis, induction of proliferation and aggregation seems to be more simple.…”

Section: Cd40 Antibodies and B-cell Differentiation 293mentioning

confidence: 99%

CD40 antibodies defining distinct epitopes display qualitative differences in their induction of B‐cell differentiation

Björck

Paulie

1996

Immunology

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SUMMARYIgE production can be obtained in vitro by stimulating B lymphocytes with CD40 antibodies and interleukin-4 (IL-4). This stimulation also results in homotypic aggregation and cell proliferation. We have shown previously that IgE synthesis may be dependent on additional signals provided by the close cellular contact. Thus inhibition of the aggregation by lymphocyte function-associated antigen-1 (LFA-1) antibodies leads to a decrease in IgE production. In the present study we show that the inhibitory effect of LFA-1 antibodies is critically dependent on the CD40 antibody used for stimulation. Thus, while previously using the monoclonal antibody (mAb) S2C6, IgE production induced by the CD40 antibody mAb89 was generally higher and could be enhanced more than fivefold in the presence of LFA-1 antibodies. Similarly, the addition of the CD23 mAb MHM6, which blocked aggregation to a similar degree as the LFA-1 antibodies, inhibited S2C6-induced IgE production but enhanced that induced by mAb89. In contrast to these opposing effects on IgE synthesis, proliferation induced by the two CD40 antibodies was affected similarly by the blocking antibodies. As the interaction between CD23 and CD21 has been suggested to involve recognition of carbohydrate structures on CD21 by the lectin-like domain on CD23, we also tested the effect of some different sugars on IgE synthesis and proliferation. Addition of fucose-1-phosphate to anti-CD40 and IL-4-stimulated B cells completely inhibited IgE synthesis and proliferation. Inhibtion was also seen with mannose-6-phosphate but not with glucose-1-phosphate. In contrast to the MHM6 antibody, the effect of the sugars was similar irrespective of the CD40 antibody used for stimulation. The study shows that different antibodies to CD40 may give rise to qualitatively distinct signals depending on the epitope recognized.

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Demonstration of a second ligand for the low affinity receptor for immunoglobulin E (CD23) using recombinant CD23 reconstituted into fluorescent liposomes.

Cited by 68 publications

References 34 publications

Temperature Effect on IgE Binding to CD23 Versus FcεRI

Temperature Effect on IgE Binding to CD23 Versus FcεRI

Exosomes Containing Glycoprotein 350 Released by EBV-Transformed B Cells Selectively Target B Cells through CD21 and Block EBV Infection In Vitro

CD40 antibodies defining distinct epitopes display qualitative differences in their induction of B‐cell differentiation

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