CD2 (cluster of differentiation 2) is a cell adhesion molecule found on the surface of T cells and natural killer (NK) cells.
It has also been called T-cell surface antigen T11/Leu-5, LFA-2,[5] LFA-3 receptor, erythrocyte receptor and rosette receptor.[6]
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It interacts with other adhesion molecules, such as lymphocyte function-associated antigen-3 (LFA-3/CD58) in humans, or CD48 in rodents, which are expressed on the surfaces of other cells.[7]
In addition to its adhesive properties, CD2 also acts as a co-stimulatory molecule on T and NK cells.[8]
Diagnostic relevance
CD2 is a specific marker for T cells and NK cells, and can therefore be used in immunohistochemistry to identify the presence of such cells in tissue sections. The great majority of T cell lymphomas and leukaemias also express CD2, making it possible to use the presence of the antigen to distinguish these conditions from B cell neoplasms.[9]
Due to its structural characteristics, CD2 is a member of the immunoglobulin superfamily; it possesses two immunoglobulin-like domains in its extracellular portion.[8]
CD2 has been shown to interact with CD2BP2,[10] Lck[11] and PSTPIP1.[12]
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Yang JJ, Ye Y, Carroll A, Yang W, Lee HW (2001). "Structural biology of the cell adhesion protein CD2: alternatively folded states and structure-function relation". Curr Protein Pept Sci. 2 (1): 1–17. doi:10.2174/1389203013381251. PMID 12369898.
Leong, Anthony S-Y, Cooper, Kumarason, Leong, F Joel W-M (2003). Manual of Diagnostic Cytology (2 ed.). Greenwich Medical Media, Ltd. p. 61. ISBN 978-1-84110-100-2.
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- Rouleau M, Mollereau B, Bernard A, Metivier D, Rosenthal-Allieri MA, Charpentier B, Senik A (1997). "CD2 induced apoptosis of peripheral T cells". Transplant. Proc. 29 (5): 2377–8. doi:10.1016/S0041-1345(97)00410-7. PMID 9270771.
- Lüscher B (2001). "Function and regulation of the transcription factors of the Myc/Max/Mad network". Gene. 277 (1–2): 1–14. doi:10.1016/S0378-1119(01)00697-7. PMID 11602341.
- Yang JJ, Ye Y, Carroll A, Yang W, Lee HW (2002). "Structural biology of the cell adhesion protein CD2: alternatively folded states and structure-function relation". Curr. Protein Pept. Sci. 2 (1): 1–17. doi:10.2174/1389203013381251. PMID 12369898.
- Bell GM, Seaman WE, Niemi EC, Imboden JB (1992). "The OX-44 molecule couples to signaling pathways and is associated with CD2 on rat T lymphocytes and a natural killer cell line". J. Exp. Med. 175 (2): 527–36. doi:10.1084/jem.175.2.527. PMC 2119111. PMID 1346273.
- Marie-Cardine A, Maridonneau-Parini I, Ferrer M, Danielian S, Rothhut B, Fagard R, Dautry-Varsat A, Fischer S (1992). "The lymphocyte-specific tyrosine protein kinase p56lck is endocytosed in Jurkat cells stimulated via CD2". J. Immunol. 148 (12): 3879–84. doi:10.4049/jimmunol.148.12.3879. PMID 1351089.
- Luzzati AL, Giacomini E, Giordani L, Pugliese O, Viora M, Chersi A (1992). "The antigen-specific induction of normal human lymphocytes in vitro is down-regulated by a conserved HIV p24 epitope". Immunol. Lett. 33 (3): 307–14. doi:10.1016/0165-2478(92)90078-3. PMID 1385321.
- Ruegg CL, Strand M (1991). "A synthetic peptide with sequence identity to the transmembrane protein GP41 of HIV-1 inhibits distinct lymphocyte activation pathways dependent on protein kinase C and intracellular calcium influx". Cell. Immunol. 137 (1): 1–13. doi:10.1016/0008-8749(91)90051-C. PMID 1832084.
- Schraven B, Samstag Y, Altevogt P, Meuer SC (1990). "Association of CD2 and CD45 on human T lymphocytes". Nature. 345 (6270): 71–4. Bibcode:1990Natur.345...71S. doi:10.1038/345071a0. PMID 1970422. S2CID 23605689.
- Samelson LE, Fletcher MC, Ledbetter JA, June CH (1990). "Activation of tyrosine phosphorylation in human T cells via the CD2 pathway. Regulation by the CD45 tyrosine phosphatase". J. Immunol. 145 (8): 2448–54. doi:10.4049/jimmunol.145.8.2448. PMID 1976695.
- Luzzati AL, Pugliese O, Giacomini E, Giordani L, Quintieri F, Hraba T, Mach O, Krchnák V, Vágner J (1990). "Immunoregulatory effect of a synthetic peptide corresponding to a region of protein p24 of HIV". Folia Biol. (Praha). 36 (1): 71–7. PMID 2111780.
- Seed B, Aruffo A (1987). "Molecular cloning of the CD2 antigen, the T-cell erythrocyte receptor, by a rapid immunoselection procedure". Proc. Natl. Acad. Sci. U.S.A. 84 (10): 3365–9. Bibcode:1987PNAS...84.3365S. doi:10.1073/pnas.84.10.3365. PMC 304871. PMID 2437578.
- Peterson A, Seed B (1987). "Monoclonal antibody and ligand binding sites of the T cell erythrocyte receptor (CD2)". Nature. 329 (6142): 842–6. Bibcode:1987Natur.329..842P. doi:10.1038/329842a0. PMID 2444890. S2CID 4315968.
- Sayre PH, Chang HC, Hussey RE, Brown NR, Richardson NE, Spagnoli G, Clayton LK, Reinherz EL (1987). "Molecular cloning and expression of T11 cDNAs reveal a receptor-like structure on human T lymphocytes". Proc. Natl. Acad. Sci. U.S.A. 84 (9): 2941–5. Bibcode:1987PNAS...84.2941S. doi:10.1073/pnas.84.9.2941. PMC 304776. PMID 2883656.
- Diamond DJ, Clayton LK, Sayre PH, Reinherz EL (1988). "Exon-intron organization and sequence comparison of human and murine T11 (CD2) genes". Proc. Natl. Acad. Sci. U.S.A. 85 (5): 1615–9. Bibcode:1988PNAS...85.1615D. doi:10.1073/pnas.85.5.1615. PMC 279824. PMID 2894031.
- Lang G, Wotton D, Owen MJ, Sewell WA, Brown MH, Mason DY, Crumpton MJ, Kioussis D (1988). "The structure of the human CD2 gene and its expression in transgenic mice". EMBO J. 7 (6): 1675–82. doi:10.1002/j.1460-2075.1988.tb02995.x. PMC 457152. PMID 2901953.
- Leca G, Boumsell L, Fabbi M, Reinherz EL, Kanellopoulos JM (1986). "The sheep erythrocyte receptor and both alpha and beta chains of the human T-lymphocyte antigen receptor bind the mitogenic lectin (phytohaemagglutinin) from Phaseolus vulgaris". Scand. J. Immunol. 23 (5): 535–44. doi:10.1111/j.1365-3083.1986.tb01985.x. PMID 3085210. S2CID 84246845.
- Sewell WA, Brown MH, Dunne J, Owen MJ, Crumpton MJ (1986). "Molecular cloning of the human T-lymphocyte surface CD2 (T11) antigen". Proc. Natl. Acad. Sci. U.S.A. 83 (22): 8718–22. Bibcode:1986PNAS...83.8718S. doi:10.1073/pnas.83.22.8718. PMC 387002. PMID 3490670.