Related Experiment Video

Updated: Aug 8, 2026

Development of an in vitro model system for studying the interaction of Equus caballus IgE with its high-affinity receptor FcεRI
07:31

Development of an in vitro model system for studying the interaction of Equus caballus IgE with its high-affinity receptor FcεRI

Published on: November 1, 2014

IgE receptor on human eosinophils (FcERII). Comparison with B cell CD23 and association with an adhesion molecule

C Grangette1, V Gruart, M A Ouaissi

  • 1Centre d'Immunologie et de Biologie Parasitaire, Institut Pasteur Lille, France.

Journal of Immunology (Baltimore, Md. : 1950)
|December 1, 1989
PubMed

Insights

Researchers characterized IgE Fc receptors (FcERII) on eosinophils and B cells, finding a shared fibronectin-like sequence crucial for IgE binding and cell adhesion. This discovery impacts understanding of immune cell interactions and potential therapeutic targets.

Area of Science:

  • Immunology
  • Cell Biology
  • Molecular Biology

Background:

  • The IgE Fc receptor (FcERII), also known as CD23, plays a role in immune responses.
  • FcERII is found on various immune cells, including B cells and eosinophils.
  • The precise function and structural characteristics of FcERII on eosinophils are not fully understood.

Purpose of the Study:

  • To characterize and compare the IgE Fc receptor (FcERII) on human eosinophils with that on B cells (CD23).
  • To investigate the structural and functional similarities between eosinophil and B cell FcERII.
  • To explore the role of a potential cell attachment sequence in FcERII function.

Main Methods:

  • Characterization of FcERII using monoclonal antibodies (mAbs) BB10 (anti-eosinophil FcERII) and 135 (anti-CD23).
  • Immunoprecipitation and Western blotting to determine molecular weight and IgE binding.
  • Flow microfluorometry to assess antibody binding to eosinophils and B cells.
  • Inhibition assays using synthetic peptides (RGDS, SDGR) and polyclonal antibodies to study cell adhesion and cytotoxicity.

Main Results:

  • Both eosinophil and B cell FcERII share a major component of 45,000-50,000 Mr, recognized by mAbs BB10 and 135.
  • Human myeloma IgE binds to the FcERII molecule immunoprecipitated by BB10.
  • A fibronectin (Fn)-like sequence containing the L-arginine-L-glycyl-L-aspartyl (RGD) cell attachment domain is present in both eosinophil and B cell FcERII.
  • The RGD and SDGR peptides inhibited the binding of BB10 and anti-Fn mAbs to eosinophils and B cells.
  • IgE-dependent eosinophil cytotoxicity against parasite targets was significantly inhibited by mAbs and peptides targeting the RGD sequence.

Conclusions:

  • Human eosinophil FcERII shares structural and functional similarities with B cell FcERII (CD23).
  • A conserved RGD cell attachment sequence is integral to FcERII structure and function, particularly in IgE-mediated eosinophil cytotoxicity.
  • This RGD sequence may play a role in eosinophil and B cell adhesion and potentially B cell growth.

More Related Videos

Basophil Activation Test for Allergy Diagnosis07:22

Basophil Activation Test for Allergy Diagnosis

Published on: May 31, 2021

Three-Dimensional Cell Culture Models to Investigate the Epithelial Barrier in Eosinophilic Esophagitis03:23

Three-Dimensional Cell Culture Models to Investigate the Epithelial Barrier in Eosinophilic Esophagitis

Published on: May 10, 2024

Related Concept Videos

Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR activation may...
Integrins01:10

Integrins

Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
Adherens Junctions01:24

Adherens Junctions

Strong contact points between adjacent cells anchor them to each other, forming tissues. Such anchoring junctions are of two types –  adherens junctions and desmosomes. Adherens junctions are abundant in tissues such as  epithelium and endothelium, forming a continuous zone of adhesion called the adhesion belt. In other tissues, such as  heart muscle, they appear as clusters, linking the cells to produce coordinated heart muscle contraction.
Adherens Junctions are Dynamic
The endothelial cells...
Selectins01:25

Selectins

Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain, which...
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
Role of Ephrin-Eph Signalling in Intestinal Stem Cell Renewal01:22

Role of Ephrin-Eph Signalling in Intestinal Stem Cell Renewal

Erythropoietin-producing hepatocellular carcinoma receptor (Eph) and its ligand, Eph receptor-interacting protein (Ephrin) were first discovered in the human carcinoma cell line, hence the name. Ephrin-Eph interaction guides cells to reach their appropriate location in adult tissues. They also play an essential role in the immune system by helping in immune cell migration, adhesion, and activation. Based on their structure and function, Eph is divided into two classes — EphA and EphB.