Functional relationship between high-affinity E receptor and CD2-11.3 epitope

• Published in: Immunology Vol. 77; no. 2; pp. 196 - 200
• Main Authors: KONTNY, E, RYZEWSKA, A
• Format: Journal Article
• Language: English
• Published: Oxford Blackwell 01-10-1992
• Subjects: Antigens, Differentiation, T-Lymphocyte - immunology; Biological and medical sciences; CD2 Antigens; Cells, Cultured; Epitopes - immunology; Erythrocytes - immunology; Fundamental and applied biological sciences. Psychology; Fundamental immunology; Humans; Immunobiology; Lymphocyte Activation - immunology; Lymphoid cells: ontogeny, maturation, markers, receptors, circulation and recirculation; Phytohemagglutinins - immunology; Receptors, IgE - immunology; Receptors, Immunologic - immunology; Rosette Formation; T-Lymphocytes - immunology; Human; Antigenic determinant; Ligand; Rosette test; Red blood cell; Biological marker; Adhesion; Vertebrata; Mammalia; T-Lymphocyte; Sheep; Artiodactyla; Ungulata; Biological receptor
• ISSN: 0019-2805; 1365-2567

The expression of both high-affinity E receptor (EhR) to sheep erythrocytes and CD2-11.3 epitope on activated human T lymphocytes suggests that these two structures may be functionally identical or closely associated. Therefore the aim of the present work was to determine if the CD2-11.3 epitope is involved in the early E rosette formation. The ability of normal and phytohaemagglutin (PHA)-activated human T lymphocytes to express the CD2-11.3 epitope and to form early E rosettes (T cells with EhR) was studied simultaneously. The partial divergence of CD2-11.3 expression on T lymphocytes from the ability of these cells to form early E (Ee) rosettes was found. The results indicated that the expression of CD2-11.3 epitope alone is insufficient to form the Ee rosettes by activated T lymphocytes, yet it may facilitate this phenomenon in the presence of EhR. The above data clearly show that the CD2-11.3 epitope is functionally closely associated although not identical to EhR. Accordingly, it seems that these two structures may co-adhere to the appropriate ligand. Thus it is possible that the CD2-11.3 epitope, as well as its established role in activation signalling, may also act as a co-adhesion molecule.