Individual-Specific Repertoires of Immune Cells SRCR Receptors in the Purple Sea Urchin(S. Purpuratus)

  • Zeev Pancer
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 484)


Invertebrates comprise the vast majority of contemporary animal species, yet their immune system been poorly characterized, especially at the molecular level (Klein, 1995). Nevertheless, invertebrates possess elaborate mechanisms to identify and eliminate life-threatening pathogens (reviews by: Smith and Davidson, 1992; Sima, 1993; Smith and Davidson, 1994; Hoffmann et al., 1996; Medzhitov and Janeway, 1998). While the evolutionary elaboration of anti-pathogen responses in a hostile environment seems inevitable, the evolution of invertebrate and vertebrate individuality determining systems presents an evolutionary enigma. A basic function of the vertebrate immune system is to maintain a representative “image” of the cells and molecules of which individuals consist, and to mediate in the conflict between cooperation and competition among individual cells. The development and elaboration of such molecular and cellular surveillance systems might have accompanied the emergence of multicellular animals, along with the evolution of higher levels of molecular and cellular complexity.


Bacterial Artificial Chromosome Scavenger Receptor Activate Leukocyte Cell Adhesion Molecule Macrophage Scavenger Receptor Vertebrate Immune System 
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  1. Al-Sharif, W.Z., Sunyer, J.O., Lambris, J.D., and Smith, L.C. Sea urchin coelomocytes specifically express a homologue of the complement component C3. J. Immunol.160,2983–2997, 1998.PubMedGoogle Scholar
  2. Aruffo, A., G.S., Bowen, M.A., Patel, D.D., Hynes, B.F., Starling, G.C., Gebe, J.A. and Bajorath, J. CD6- ligand interactions: a paradigm for SRCR domain function? Immunol. Today18,498–504, 1997.PubMedCrossRefGoogle Scholar
  3. Aruffo, A., Melnick, M.B., Linsley, P.S. and Seed, B. The lymphocyte glycoprotein CD6 contains a repeated domain structure characteristic of a new family of cell surface and secreted proteins. J. Exp. Med.174,949–952, 1991.PubMedCrossRefGoogle Scholar
  4. Blumbach, B., Pancer, Z., Diehl-SeifertB.,Steffen, R., Münkner, J., Müller, I. and Müller, W.E.G. The putative sponge aggregation receptor: Isolation and characterization ofa molecule composed of scavenger receptor cysteine-rich domains and short consensus repeats. J. Cell Sei.111,2635–2644, 1998.Google Scholar
  5. Cheng, H., Bjerknes, M. and Chen, H. CRP-ductin: gene expressed in intestinal crypts and in pancreatic and hepatic ducts. Anat. Rec., 244, 327–343, 1996.Google Scholar
  6. Dangott, L.J., Jordan, J.E., Bellet, R.A. and Garbers, D.L. Cloning of the mRNA for the protein that crosslinks to the egg peptide speract. Proc. Natl. Acad. Sci. USA86,2128–2132, 1989.CrossRefGoogle Scholar
  7. Elomaa, O., Kangas, M., Sahlberg, C., Tuukkanen, J., Sormunen, R., Liakka, A., Thesleff, I., Kraal, G. and Tryggvason, K. Cloning of a novel bacteria-binding receptor structurally related to scavenger receptors and expressed in a subset of macrophages. Cell80,603–609, 1995.PubMedCrossRefGoogle Scholar
  8. Freeman, M., Ashkenas, J., Rees, D.J., Kingsley, D.M., Copeland, N.G., Jenkins, N.A. and Krieger, M. An ancient, highly conserved family of cysteine-rich protein domains revealed by cloning type I and type II murine macrophage scavenger receptors. Proc. Natl. Acad. Sei. USA87,8810–8814, 1990.CrossRefGoogle Scholar
  9. Friedman, J., Trahey, M. and Weissman, I. Cloning and characterization of cyclophilin C-associated protein: a candidate natural cellular ligand for cyclophilin C. Proc. Natl. Acad. Sci. USA90,6815–6819, 1993.CrossRefGoogle Scholar
  10. Gebe, J.A., Kiener, P.A., Ring, H.Z., Li, X., Francke, U. and Aruffo, A. Molecular cloning, mapping to human chromosome 1 q21-q23, and cell binding characteristics of SPa, a new member of the scavenger receptor cysteine-rich (SRCR) family of proteins. J. Biol. Chem., 272, 6151–58, 1997.PubMedCrossRefGoogle Scholar
  11. Goldberger, G., Bruns, G.A., Rits, M., Edge, M.D. and Kwiatkowski, D.J. Human complement factor I: analysis of eDNA-derived primary structure and assignment of its gene to chromosome 4. J. Biol. Chem., 262, 10065–10071, 1987.PubMedGoogle Scholar
  12. Hoffmann, J.A., Reichhart, J-M. and Hertru, C. Innate immunity in higher insects. Cur. Opinion Immunol.8,8–13, 1996.CrossRefGoogle Scholar
  13. Hohenester, E., Sasaki, T. and Timpl, R. Crystal structure of a scavenger receptor cysteine-rich domain sheds light on an ancient superfamily. Nature Struct. Biol.6,228–232, 1999PubMedCrossRefGoogle Scholar
  14. Kanan, J.H.C., Nayeem, N., Binns, R.M. and Chain, B.M. Mechanisms for variability in a member of the scavenger-receptor cysteine-rich superfamily. Immunogenetics46,276–82, 1997.PubMedCrossRefGoogle Scholar
  15. Kirkham, P.A., Takamatsu, H-H. and Parkhouse R.M.E. Growth arrest of gd T cells induced by monoclonal antibody against WCl correlates with activation of multiple tyrosinephosphatases and dephosphorylation of MAP kinases erk2. Eur. J. Immunol.27,717–725, 1997.PubMedCrossRefGoogle Scholar
  16. Klein, J. Ehrlich and Darwin: homochauvinism in immunology. Immunol. Cell Biol., 73, 103–108, 1995. Koths, K., Taylor, E., HalenbeckR.,Casipit, C. and Wang, A. Cloning and characterization of a human Mac-2-binding protein, a new member of the superfamily defined by the macrophage scavenger receptor cysteine-rich domain. J. Biol. Chem.268,14225–14249, 1993.Google Scholar
  17. Krieger, M. Molecular flypaper and arteriosclerosis: structure of the macrophage scavenger receptor. Trends Biochem. Sei., 17, 141–146, 1992.Google Scholar
  18. Law, S.K., Micklem, K.J., Shaw, J.M.,Zhang X.P., Dong, Y., Willis, A.C.and Mason, D.Y. Anew macrophage differentiation antigen which is a member of the scavenger receptor superfamily. Eur. J. Immunol.,23, 2320–2325,1993.PubMedCrossRefGoogle Scholar
  19. Mayer, W.E. and Tichy, H. A cDNA clone from the sea lampreyPetromyzon marinuscoding for a scavenger receptor Cys-rich (SRCR) domain protein. Gene,164,267–271, 1995.PubMedCrossRefGoogle Scholar
  20. O’Keeffe, M.A., Metcalfe, S.A., Cunningham, C.P. and Walker, I.D. Sheep CD4+ab T cells express novel members of the T19 multigene family. Immunogenetics49,45–55, 1999.PubMedCrossRefGoogle Scholar
  21. Pancer, Z., Münkner, J., Müller, I. and Müller, W.E.G. A novel member of an ancient superfamily: sponge(Geodia cydoniumPorifera) putative protein that features scavenger receptor cysteine-rich repeats. Gene,193, 211–218, 1997.PubMedCrossRefGoogle Scholar
  22. Pancer, Z., Rast, J.P. and Davidson E.H. Origins of immunity: transcription factors and homologues of effector genes of the vertebrate immune system expressed in sea urchin coelomocytes. Immunogenetics49,773–786, 1999.PubMedCrossRefGoogle Scholar
  23. Resnick, D., Pearson, A. and Krieger, M. The SRCR superfamily: a family reminiscent of the Ig superfamily. Trends Biochem. Sei.19,5–8, 1994.Google Scholar
  24. Sima, P. Evolution of immune reactions. Crit. Rev. Immunol.13,83–114, 1993.Google Scholar
  25. Smith, L.C., and Davidson, E.H. The echinoid immune system and the phylogenetic occurrence of immune mechanisms in deuterostomes. Immunol. Today13,356–361, 1992.Google Scholar
  26. Smith, L.C., and Davidson, E.H. () The echinoderm immune system. Ann. NY Acad. Sei.712,213–226, 1994.CrossRefGoogle Scholar
  27. Smith, L.C., Britten, R.J. and Davidson, E.H. SpCoel l: a sea urchin profilin gene expressed specifically in coelomocytes in response to injury. Mol. Biol. Cell3,403–414, 1992.Google Scholar
  28. Smith, L.C., Britten, R.J. and Davidson, E.H. Lipopolysaccharide activates the sea urchin immune system. Dev. Comp. Immunol.19,217–224, 1995.CrossRefGoogle Scholar
  29. Smith, L.C., Chang, L., Britten, R.J. and Davidson, E.H. Sea urchin genes expressed in activated coelomocytes are identified by expressed sequence tags. Immunology156,593–602, 1996.Google Scholar
  30. Smith, L.C., Shih, C-S. and Dachenhausen, S.G. Coelomocytes express SpBf, a homologue of factor B, the second component in the sea urchin complement system. J. Immunol., 161,6784–6793. 1998.PubMedGoogle Scholar
  31. Takamatsu, H-H., Kirkham, P.A. and Parkhouse R.M.E. A gd T cell specific surface receptor (WC I) signaling GO/G1 cell cycle arrest. Eur. J. Immunol.27,105–100, 1997.PubMedCrossRefGoogle Scholar
  32. Van de Velde, H., von HoegenI.,Luo, W., Parries, J.R. and Thielemans, K. The B-cell surface protein CD72/Lyb-2 is the ligand for CD5. Nature351,662–65, 1991.PubMedCrossRefGoogle Scholar
  33. Walker, I.D., Glew, M.D., O’Keeffe, M.A., Metclafe, S.A., Clevers, H.C., Wijngaard, P.L.J., Adams, T.E. and Hein, W.R. A novel multi-gene family of sheep T cells. Immunol.83,517–523, 1994.Google Scholar
  34. Whitney, G.S., Bowen, M.A., Neubauer, M. and Aruffo, A. Cloning and characterization of murine CD6. Mol. Immunol.32,89–92, 1994.Google Scholar
  35. Whitney, G.S., Starling, G.C., Bowen, M.A., ModrellB.,Siadak, A.W. and Aruffo, A. The membrane-proximal scavenger receptor cysteine-rich domain of CD6 contains the activated leukocyte cell adhesion molecule binding site. J. Biol. Chem.270,18187–18190, 1995.PubMedCrossRefGoogle Scholar
  36. Wijngaard, P.L., Metzelaar, M.J., MacHughN.D.,Morrison, W.I. and Clevers, H.C. Molecularcharacterization of the WC1 antigen expressed specifically on bovine CD4–CD8-gamma delta T lymphocytes. J. Immunol.149,3273–3277, 1992.PubMedGoogle Scholar
  37. Yu, Q., Reichert, M., Brousseau, T., Cleuter, Y., Burny, A. and Kettmann, R. Sequence of bovine CD5. Nucleic Acids Res.185296, 1990.PubMedCrossRefGoogle Scholar

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© Springer Science+Business Media New York 2001

Authors and Affiliations

  • Zeev Pancer
    • 1
  1. 1.Department of BiologyCalifornia Institute of TechnologyPasadena

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