The cell surface molecule recognized by the erythrocyte receptor of T lymphocytes. Identification and partial characterization using a monoclonal antibody

Journal of Experimental Medicine (Impact Factor: 12.52). 10/1985; 162(3):890-901. DOI: 10.1084/jem.162.3.890
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A monoclonal antibody (mAb) to sheep red blood cells (SRBC), termed L180/1, is described that completely blocks rosette formation between SRBC and human or sheep T lymphocytes. L180/1 precipitated a minor glycoprotein of about approximately 42,000 mol wt from surface-labeled SRBC. This glycoprotein was partially affinity purified and found to block E rosette formation and to compete with anti-T11 mAb for the E receptor. The molecule detected by mAb L180/1 thus appears to be recognized by the E receptor and was given the preliminary name, T11 target structure (T11TS). Since the mAb to sheep T11TS blocks the binding of SRBC to both human and sheep T cells, and mAb to T11 blocks the binding of red cells from human and sheep to the human E receptor, we concluded that analogous receptor-ligand (T11-T11TS) systems exist in man and sheep that are crossreactive over the species barrier. The possibility is discussed that the E receptor, which is known to be involved in T cell activation, and T11TS function as complementary cell interaction molecules in T cell responses.

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Available from: Thomas Hünig
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    • "The E-rosette-forming capacity has been reported in human and murine T cells of both gd and ab lineages, and porcine T cells of the ab and CD2 + gd lineages (Licence and Binns, 1984; Hunig, 1985; Kontny and Ryzewska, 1989; Binns, 1994). E-rosette formation is the result of the interaction between CD2 molecules on T cells and their targets on xenogeneic RBC (Hunig, 1985; Tiefenthaler et al., 1987). In contrast, porcine CD2 7 gd T cells do not have the E-rosette-forming capacity and thus are referred to as the non-classical T cells of pigs (Saalmuller et al., 1990; Binns et al., 1992; Binns, 1994). "
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    Full-text · Article · Jun 2006 · Animal Health Research Reviews
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    • "One of the first cell adhesion systems to be defined and reconstituted was based on the interaction of CD2 and CD58. Monoclonal antibody inhibition studies pointed to an adhesion mechanism based on the interaction of CD2 (also called T11, sheep red blood cell receptor and LFA-2) with CD58 (also called T11 target structure and LFA-3) (Hünig, 1985; Shaw et al., 1986; Vollger et al., 1987). CD2 –CD58 interactions were directly demonstrated using purified CD2 and purified CD58, the later reconstituted in supported planar bilayers (Dustin et al., 1987a; Selvaraj et al., 1987). "
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