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. 1988 Jul;85(14):5176–5180. doi: 10.1073/pnas.85.14.5176

Adhesion domain of human T11 (CD2) is encoded by a single exon.

N E Richardson 1, H C Chang 1, N R Brown 1, R E Hussey 1, P H Sayre 1, E L Reinherz 1
PMCID: PMC281711  PMID: 2455894

Abstract

The 50-kDa T11 (CD2) T-lymphocyte surface glycoprotein facilitates physical adhesion between T-lineage cells and their cognate cellular counterparts (cytotoxic T-lymphocytes-target cells, helper T lymphocytes-antigen-presenting cells, or thymocytes-thymic epithelium) as well as signaling through the antigen-specific T3-Ti receptor complex. To examine the relationship between the structure and function of the T11 molecule, we have utilized a baculoviral expression system to produce milligram quantities of the hydrophilic extracellular T11 segment. Enzyme cleavage, microsequencing, and HPLC analyses of the expressed protein in conjunction with genomic cloning information show that the domain involved in cellular adhesion is encoded by a single 321-base-pair exon.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bernard A., Gelin C., Raynal B., Pham D., Gosse C., Boumsell L. Phenomenon of human T cells rosetting with sheep erythrocytes analyzed with monoclonal antibodies. "Modulation" of a partially hidden epitope determining the conditions of interaction between T cells and erythrocytes. J Exp Med. 1982 May 1;155(5):1317–1333. doi: 10.1084/jem.155.5.1317. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Brain P., Gordon J., Willetts W. A. Rosette formation by peripheral lymphocytes. Clin Exp Immunol. 1970 May;6(5):681–688. [PMC free article] [PubMed] [Google Scholar]
  3. Clayton L. K., Ramachandran H., Pravtcheva D., Chen Y. F., Diamond D. J., Ruddle F. H., Reinherz E. L. The gene for T11 (CD2) maps to chromosome 1 in humans and to chromosome 3 in mice. J Immunol. 1988 May 15;140(10):3617–3621. [PubMed] [Google Scholar]
  4. Clayton L. K., Sayre P. H., Novotny J., Reinherz E. L. Murine and human T11 (CD2) cDNA sequences suggest a common signal transduction mechanism. Eur J Immunol. 1987 Sep;17(9):1367–1370. doi: 10.1002/eji.1830170922. [DOI] [PubMed] [Google Scholar]
  5. Coombs R. R., Gurner B. W., Wilson A. B., Holm G., Lindgren B. Rosette-formation between human lymphocytes and sheep red cells not involving immunoglobulin receptors. Int Arch Allergy Appl Immunol. 1970;39(5-6):658–663. doi: 10.1159/000230390. [DOI] [PubMed] [Google Scholar]
  6. Diamond D. J., Clayton L. K., Sayre P. H., Reinherz E. L. Exon-intron organization and sequence comparison of human and murine T11 (CD2) genes. Proc Natl Acad Sci U S A. 1988 Mar;85(5):1615–1619. doi: 10.1073/pnas.85.5.1615. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Dustin M. L., Sanders M. E., Shaw S., Springer T. A. Purified lymphocyte function-associated antigen 3 binds to CD2 and mediates T lymphocyte adhesion. J Exp Med. 1987 Mar 1;165(3):677–692. doi: 10.1084/jem.165.3.677. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Howard F. D., Ledbetter J. A., Wong J., Bieber C. P., Stinson E. B., Herzenberg L. A. A human T lymphocyte differentiation marker defined by monoclonal antibodies that block E-rosette formation. J Immunol. 1981 Jun;126(6):2117–2122. [PubMed] [Google Scholar]
  9. Hünig T., Mitnacht R., Tiefenthaler G., Köhler C., Miyasaka M. T11TS, the cell surface molecule binding to the "erythrocyte receptor" of T lymphocytes: cellular distribution, purification to homogeneity and biochemical properties. Eur J Immunol. 1986 Dec;16(12):1615–1621. doi: 10.1002/eji.1830161223. [DOI] [PubMed] [Google Scholar]
  10. Hünig T., Tiefenthaler G., Meyer zum Büschenfelde K. H., Meuer S. C. Alternative pathway activation of T cells by binding of CD2 to its cell-surface ligand. Nature. 1987 Mar 19;326(6110):298–301. doi: 10.1038/326298a0. [DOI] [PubMed] [Google Scholar]
  11. Kamoun M., Kadin M. E., Martin P. J., Nettleton J., Hansen J. A. A novel human T cell antigen preferentially expressed on mature T cells and shared by both well and poorly differentiated B cell leukemias and lymphomas. J Immunol. 1981 Sep;127(3):987–991. [PubMed] [Google Scholar]
  12. Lay W. H., Mendes N. F., Bianco C., Nussenzweig V. Binding of sheep red blood cells to a large population of human lymphocytes. Nature. 1971 Apr 23;230(5295):531–532. doi: 10.1038/230531a0. [DOI] [PubMed] [Google Scholar]
  13. Luescher B., Bron C. Biosynthesis of mouse Thy-1 antigen. J Immunol. 1985 Feb;134(2):1084–1089. [PubMed] [Google Scholar]
  14. Matsudaira P. Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J Biol Chem. 1987 Jul 25;262(21):10035–10038. [PubMed] [Google Scholar]
  15. Meuer S. C., Hussey R. E., Fabbi M., Fox D., Acuto O., Fitzgerald K. A., Hodgdon J. C., Protentis J. P., Schlossman S. F., Reinherz E. L. An alternative pathway of T-cell activation: a functional role for the 50 kd T11 sheep erythrocyte receptor protein. Cell. 1984 Apr;36(4):897–906. doi: 10.1016/0092-8674(84)90039-4. [DOI] [PubMed] [Google Scholar]
  16. Parkhouse R. M. Biosynthesis of J-chain in mouse IgA and IgM. Nat New Biol. 1972 Mar 1;236(61):9–11. doi: 10.1038/newbio236009a0. [DOI] [PubMed] [Google Scholar]
  17. Peterson A., Seed B. Monoclonal antibody and ligand binding sites of the T cell erythrocyte receptor (CD2). 1987 Oct 29-Nov 4Nature. 329(6142):842–846. doi: 10.1038/329842a0. [DOI] [PubMed] [Google Scholar]
  18. Sayre P. H., Chang H. C., Hussey R. E., Brown N. R., Richardson N. E., Spagnoli G., Clayton L. K., Reinherz E. L. Molecular cloning and expression of T11 cDNAs reveal a receptor-like structure on human T lymphocytes. Proc Natl Acad Sci U S A. 1987 May;84(9):2941–2945. doi: 10.1073/pnas.84.9.2941. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Seed B., Aruffo A. Molecular cloning of the CD2 antigen, the T-cell erythrocyte receptor, by a rapid immunoselection procedure. Proc Natl Acad Sci U S A. 1987 May;84(10):3365–3369. doi: 10.1073/pnas.84.10.3365. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Sewell W. A., Brown M. H., Dunne J., Owen M. J., Crumpton M. J. Molecular cloning of the human T-lymphocyte surface CD2 (T11) antigen. Proc Natl Acad Sci U S A. 1986 Nov;83(22):8718–8722. doi: 10.1073/pnas.83.22.8718. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Sewell W. A., Brown M. H., Owen M. J., Fink P. J., Kozak C. A., Crumpton M. J. The murine homologue of the T lymphocyte CD2 antigen: molecular cloning, chromosome assignment and cell surface expression. Eur J Immunol. 1987 Jul;17(7):1015–1020. doi: 10.1002/eji.1830170718. [DOI] [PubMed] [Google Scholar]
  22. Shaw S., Luce G. E., Quinones R., Gress R. E., Springer T. A., Sanders M. E. Two antigen-independent adhesion pathways used by human cytotoxic T-cell clones. Nature. 1986 Sep 18;323(6085):262–264. doi: 10.1038/323262a0. [DOI] [PubMed] [Google Scholar]
  23. Smith G. E., Ju G., Ericson B. L., Moschera J., Lahm H. W., Chizzonite R., Summers M. D. Modification and secretion of human interleukin 2 produced in insect cells by a baculovirus expression vector. Proc Natl Acad Sci U S A. 1985 Dec;82(24):8404–8408. doi: 10.1073/pnas.82.24.8404. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Verbi W., Greaves M. F., Schneider C., Koubek K., Janossy G., Stein H., Kung P., Goldstein G. Monoclonal antibodies OKT 11 and OKT 11A have pan-T reactivity and block sheep erythrocyte "receptors". Eur J Immunol. 1982 Jan;12(1):81–86. doi: 10.1002/eji.1830120115. [DOI] [PubMed] [Google Scholar]
  25. Vollger L. W., Tuck D. T., Springer T. A., Haynes B. F., Singer K. H. Thymocyte binding to human thymic epithelial cells is inhibited by monoclonal antibodies to CD-2 and LFA-3 antigens. J Immunol. 1987 Jan 15;138(2):358–363. [PubMed] [Google Scholar]
  26. Williams A. F., Barclay A. N., Clark S. J., Paterson D. J., Willis A. C. Similarities in sequences and cellular expression between rat CD2 and CD4 antigens. J Exp Med. 1987 Feb 1;165(2):368–380. doi: 10.1084/jem.165.2.368. [DOI] [PMC free article] [PubMed] [Google Scholar]

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