Several carcinoembryonic antigens (CD66) serve as receptors for gonococcal opacity proteins

Journal of Experimental Medicine

Volumn 185, Issue 9, 1997, Pages 1557-1564

  Chen, Tie ^a   Grunert, Fritz ^b   Medina Marino, Andrew ^a   Gotschlich, Emil C ^a  

^a ROCKEFELLER UNIVERSITY   (United States)

^b UNIVERSITY OF FREIBURG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CARCINOEMBRYONIC ANTIGEN; HEPARAN SULFATE; SYNDECAN;

AMINO TERMINAL SEQUENCE; ANTIGEN EXPRESSION; ANTIGEN PRESENTATION; ARTICLE; CELL ADHESION; ENDOCYTOSIS; GENETIC TRANSFECTION; GONORRHEA; HUMAN; HUMAN CELL; INTERNALIZATION; MULTIGENE FAMILY; NEISSERIA GONORRHOEAE; OUTER MEMBRANE; PHAGOCYTOSIS; PRIORITY JOURNAL;

ANIMALS; ANTIGENS, BACTERIAL; ANTIGENS, CD; BACTERIAL ADHESION; CARCINOEMBRYONIC ANTIGEN; CHO CELLS; COLONIC NEOPLASMS; CRICETINAE; HELA CELLS; HEPARITIN SULFATE; HUMANS; MICROSCOPY, ELECTRON; NEISSERIA GONORRHOEAE; TUMOR CELLS, CULTURED;

EID: 0030924679     PISSN: 00221007     EISSN: None     Source Type: Journal    
DOI: 10.1084/jem.185.9.1557     Document Type: Article

References (74)

1. Ward, M.E., and P.J. Watt. 1972. Adherence of Neisseria gonorrhoeae to urethral mucosal cells: an electron-microscopic study of human gonorrhea. J. Infect. Dis. 126:601-605.
2. Wigfield, A.S. 1972. 27 years of uninterrupted contact tracing. Br. J. Vener. Dis. 48:37-50.
3. Swanson, J. 1973. Studies on gonococcus infection. IV. Pili: their role in attachment of gonococci to tissue culture cells. J. Exp. Med. 137:571-589.
4. Watt, P.J., and M.E. Ward. 1980. Adherence of Neisseria gonorrhoeae and other Neisseria species to mammalian cells. In Bacterial Adherence. Series B, 6th ed. E.H. Beachey, editor. Chapman & Hall, Ltd., New York. 253-288.
5. Swanson, J., K. Robbins, O. Barrera, D. Corwin, J. Boslego, J. Ciak, M. Blake, and J.M. Koomey. 1987. Gonococcal pilin variants in experimental gonorrhea. J. Exp. Med. 165:1344-1357.
6. Ward, M.E., P.J. Watt, and J.N. Robertson. 1974. The human fallopian tube: a laboratory model for gonococcal infection. J. Infect. Dis. 129:650-659.
7. McGee, Z.A., A.P. Johnson, and D. Taylor-Robinson. 1976. Human fallopian tubes in organ culture: preparation, maintenance, and quantitation of damage by pathogenic microorganisms. Infect. Immun. 13:608-618.
8. McGee, Z.A., G.L. Gorby, P.B. Wyrick, R. Hodinka, and L.H. Hoffman. 1988. Parasite-directed endocytosis. Rev. Inject. Dis. 10:S311-S316.
9. Gorby, G.L., and G.B. Shaefer. 1992. Effect of attachment factors (pili plus Opa) on Neisseria gonorrhoeae invasion of human fallopian tube tissue in vitro: quantitation by computerized image analysis. Microb. Pathog. 13:93-108.
10. Gorby, G., D. Simon, and R. Rest. 1994. Escherichia coli that express Neisseria gonorrhoeae opacity-associated proteins attach to and invade human fallopian tube epithelium. Ann. NY Acad. Sci. 730:286-289.
11. Swanson, J., O. Barrera, J. Sola, and J. Boslego. 1988. Expression of outer membrane protein II by gonococci in experimental gonorrhea. J. Exp. Med. 168:2121-2129.
12. Jerse, A.E., M.S. Cohen, P.M. Drown, L.G. Whicker, S.F. Isbey, H.S. Seifert, and J.G. Cannon. 1994. Multiple gonococcal opacity proteins are expressed during experimental urethral infection in the male. J. Exp. Med. 179:911-920.
13. Isberg, R., and J. Leong. 1990. Multiple beta 1 chain integrins are receptors for invasin, a protein that promotes bacterial penetration into mammalian cells. Cell. 60:861-871.
14. Mengaud, J., H. Ohayon, P. Gounon, R.-M. Mege, and P. Cossart. 1996. E-cadherin is the receptor for internalin, a surface protein required for entry of L. monocytogenes into epithelial cells. Cell. 84:923-932.
15. Wang, J., H. Schneider, and J. Griffiss. 1996. Neisseria gonorrhoeae must express the paraglobosyl LOS in order to invade human genitourinary epithelial cells. In Tenth International Pathogenic Neisseria Conference. Baltimore. 112-113.
16. Purachuri, D.K., H.S. Seifert, R.S. Ajioka, K.-A. Karlsson, and M. So. 1990. Identification and characterization of a Neisseria gonorrhoeae gene encoding a glycolipid-binding adhesin. Proc. Natl. Acad. Sci. USA. 87:333-337.
17. Stromberg, N., C. Deal, G. Nyberg, S. Normark, M. So, and K.-A. Karlsson. 1988. Identification of carbohydrate structures that are possible receptors for Neisseria gonorrhoeae. Proc. Natl. Acad. Sci. USA. 85:4902-4906.
18. Bessen, D., and E.C. Gotschlich. 1986. Interactions of gonococci with HeLa cells: attachment, detachment, replication, penetration, and the role of protein II. Infect. Immun. 54: 154-160.
19. Bhat, K.S., C.P. Gibbs, O. Barrera, S.G. Morrison, F. Jahnig, A. Stern, E.-M. Kupsch, T.F. Meyer, and J. Swanson. 1991. The opacity proteins of Neisseria gonorrhoeae strain MS11 are encoded by a family of 11 complete genes. Mol. Microbiol. 5: 1889-1901.
20. Weel, J.F.L., C.T.P. Hopman, and J.P.M. van Putten. 1991. In situ expression and localization of Neisseria gonorrhoeae opacity proteins in infected epithelial cells: apparent role of Opa proteins in cellular invasion. J. Exp. Med. 173:1395-1405.
21. Makino, S.-I., J.P.M. van Putten, and T.F. Meyer. 1991. Phase variation of the opacity outer membrane protein controls invasion of Neisseria gonorrhoeae into human epithelial cells. EMBO (Eur. Mol. Biol. Organ.) J. 10:1307-1315.
22. Kupsch, E.M., B. Knepper, T. Kuroki, I. Heuer, and T.F. Meyer. 1993. Variable opacity (Opa) outer membrane proteins account for cell tropisms displayed by Neisseria gonorrhoeae for human leukocytes and epithelial cells. EMBO (Eur. Mol. Biol. Organ.) J. 12:641-650.
23. Belland, R.J., T. Chen, J. Swanson, and S.H. Fischer. 1992. Human neutrophil response to recombinant neisserial Opa proteins. Mol. Microbiol. 6:1729-1737.
24. + gonococci to epithelial cells in vitro involves heparan sulfate. J. Exp. Med. 182:511-517.
25. van Putten, J., and S. Paul. 1995. Binding of syndecan-like cell surface proteoglycan receptors is required for Neisseria gonorrhoeae entry into human mucosal cells. EMBO (Eur. Mol. Biol. Organ.) J. 14:2144-2154.
26. Chen, T., and E. Gotschlich. 1996. CGM1a antigen of neutrophils, a receptor of gonococcal opacity proteins. Proc. Natl. Acad. Sci. USA. 93:14851-14856.
27. Virji, M., K. Makepeace, D.J.P. Ferguson, and M. Watt. 1996. Carcinoembryonic antigens (CD66) on epithelial cells and neutrophils are receptors for Opa proteins of pathogenic neisseriae. Mol. Microbiol. 22:941-950.
28. Virji, M., M. Watt, S. Barker, K. Makepeace, and R. Doyonnas. 1996. The N-domain of the human CD66a adhesion molecule is a target for Opa proteins of Neisseria meningitidis and Neisseria gonorrhoeae. Mol. Microbiol. 22:926-939.
29. Swanson, J., and O. Barrera. 1983. Immunological characteristics of gonococcal outer membrane protein II assessed by immunoprecipitation, immunoblotting, and coagglutination. J. Exp. Med. 157:1405-1420.
30. Swanson, J. 1991. Some effects of LOS and Opa on surface properties of gonococci. In Proceedings of the Seventh International Pathogenic Neisseria Conference. Walter de Gruyter & Co., Berlin. 391-396.
31. Nagel, G., F. Grunert, T. Kuijpers, S. Watt, J. Thompson, and W. Zimmermann. 1993. Genomic organization, splice variants and expression of CGM1, a CD66-related member of the carcinoembryonic antigen gene family. Eur. J. Biochem. 214:27-35.
32. Esko, J.D., T.E. Stewart, and W.H. Taylor. 1985. Animal cell mutants defective in glycosaminoglycan biosynthesis. Proc. Natl. Acad. Sci. USA. 82:3197-3201.
33. Esko, J., J. Weinke, W. Taylor, G. Ekborg, L. Roden, G. Anantharamaiah, and A. Gawish. 1987. Inhibition of chondroitin and heparan sulfate biosynthesis in Chinese hamster ovary cell mutants defective in galactosyltransferase I. J. Biol. Chem. 262:12189-12195.
34. Shieh, M., D. WuDunn, R. Montgomery, J. Esko, and P. Spear. 1992. Cell surface receptors for herpes simplex virus are heparan sulfate proteoglycans. J. Cell Biol. 116:1273-1281.
35. Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA. 76:4350-4354.
36. James, J.F., and J. Swanson. 1978. Color/opacity colony variants of Neisseria gonorrhoeae and their relationship to the menstrual cycle. In Immunobiology of Neisseria gonorrhoeae. G.F. Brooks, editor. American Society for Microbiology, Washington DC. 338-343.
37. James, J.F., and J. Swanson. 1978. Studies on gonococcus infection. XIII. Occurrence of color/opacity colonial variants in clinical cultures. Infect. Immun. 19:332-340.
38. Ison, C., and G. Brooks. 1991. Expression of protein II by clinical isolates of Neisseria gonorrhoeae. In Neisseriae 1990. M. Achtman, editor. Walter de Gruyter & Co., Berlin. 597-602.
39. Plummer, F., H. Chubb, J. Simonsen, M. Bosire, L. Slaney, N. Nagelkerke, I. Maclean, J. Ndinya-Achola, P. Waiyaki, and R. Brunham. 1994. Antibodies to opacity proteins (Opa) correlate with a reduced risk of gonococcal salpingitis. J. Clin. Invest. 93:1748-1755.
40. Gold, P., and S.O. Freedman. 1965. Demonstration of tumor-specific antigens in human colonic carcinomata by immunological tolerance and absorption techniques. J. Exp. Med. 121:439-462.
41. Von Kleist, S., G. Chavanel, and P. Burtin. 1972. Identification of an antigen from normal human tissue that cross-reacts with the carcinoembryonic antigen. Proc. Natl. Acad. Sci. USA. 69:2492-2494.
42. Mach, J.-P., and G. Pusztaszeri. 1972. Carcinoembryonic antigen (CEA): demonstration of a partial identity between CEA and a normal glycoprotein. Immunochemistry. 9:1031-1034.
43. Bordes, M., S. Knobel, and F. Martin. 1975. Carcinoembryonic antigen (CEA) and related antigens in blood cells and haematopoietic tissues. Eur. J. Cancer. 11:783-786.
44. Tynan, K., A. Olsen, B. Trask, P. de Jong, J. Thompson, W. Zimmermann, A. Carrano, and H. Mohrenweiser. 1992. Assembly and analysis of cosmid contigs in the CEA-gene family region of human chromosome 19. Nucleic Acids Res. 20: 1629-1636.
45. Thompson, J., W. Zimmermann, P. Osthus-Bugat, C. Schleussner, A. Eades-Perner, S. Barnert, S. Von Kleist, T. Willcocks, I. Craig, K. Tynan et al. 1992. Long-range chromosomal mapping of the carcinoembryonic antigen (CEA) gene family cluster. Genomics. 12:761-772.
46. Paxton, R., G. Mooser, H. Pande, T.D. Lee, and J.E. Shively. 1987. Sequence analysis of carcinoembryonic antigen: identification glycosylation sites and homology with the immunoglobulin supergene family. Proc. Natl. Acad. Sci. USA. 84:920-924.
47. Watt, S., J. Fawcett, S. Murdoch, A. Teixeira, S. Gschmeissner, N. Hajibagheri, and D. Simmons. 1994. CD66 identifies the biliary glycoprotein (BGP) adhesion molecule: cloning, expression, and adhesion functions of the BGPc splice variant. Blood. 84:200-210.
48. Oikawa, S., C. Inuzuka, M. Kuroki, F. Arakawa, Y. Matsuoka, G. Kosaki, and H. Nakazato. 1991. A specific heterotypic cell adhesion activity between members of carcinoembryonic antigen family. W272 and NCA, is mediated by N-domains. J. Biol. Chem. 266:7995-8001.
49. Tatarinov, Y.S., and V.N. Masyukevich. 1970. Immunological identification of a new β1-globulin in the blood serum of pregnant woman. Bull. Exp. Biol. Med. 69:66-68.
50. Oikawa, S., C. Inuzuka, G. Kosaki, and H. Nakazato. 1988. Exon-intron organization of a gene for pregnancy-specific beta 1-glycoprotein, a subfamily member of CEA family: implications for its characteristic repetitive domains and C-terminal sequences. Biochem. Biophys. Res. Commun. 156:68-77.
51. Oikawa, S., C. Inuzuka, M. Kuroki, Y. Matsuoka, G. Kosaki, and H. Nakazato. 1989. A pregnancy-specific beta 1-glycoprotein, a CEA gene family member, expressed in a human promyelocytic leukemia cell line, HL-60: structures of protein, mRNA and gene. Biochem. Biophys. Res. Commun. 163: 1021-1031.
52. Oikawa, S., M. Kuroki, Y. Matsuoka, G. Kosaki, and H. Nakazato. 1992. Homotypic and heterotypic Ca(++)-independent cell adhesion activities of biliary glycoprotein, a member of carcinoembryonic antigen family, expressed on CHO cell surface Biochem. Biophys. Res. Commun. 186:881-887.
53. Rojas, M., A. Fuks, and C. Stanners. 1990. Biliary glycoprotein a member of the immunoglobulin supergene family, functions in vitro as a Ca2(+)-dependent intercellular adhesion molecule. Cell Growth Differ. 1:527-533.
54. Benchimol, S., A. Fuks, S. Jothy, N. Beauchemin, K. Shirota, and C. Stanners. 1989. Carcinoembryonic antigen, a human tumor marker, functions as an intercellular adhesion molecule. Cell. 57:327-334.
55. Leusch, H., S. Hefta, Z. Drzeniek, K. Hummel, Z. Markos-Pusztai, and C. Wagener. 1990. Escherichia coli of human origin binds to carcinoembryonic antigen (CEA) and non-specific crossreacting antigen (NCA). FEBS Lett. 261:405-409.
56. Leusch, H., Z. Drzeniek, S. Hefta, Z. Markos-Pusztai, and C. Wagener 1991. The putative role of members of the CEA-gene family (CEA, NCA and BGP) as ligands for the bacterial colonization of different human epithelial tissues. Int. J. Med. Microbiol. 275:118-122.
57. Johnson, J., K. Skubitz, B. Nowicki, K. Jacques-Palaz, and R. Rakita. 1995. Nonlethal adherence to human neutrophils mediated by Dr antigen-specific adhesins of Escherichia coli. Infect. Immun. 63:309-316.
58. Pignatelli, M., H. Durbin, and W. Bodmer. 1990. Carcinoembryonic antigen functions as an accessory adhesion molecule mediating colon epithelial cell-collagen interactions. Proc. Natl. Acad. Sci. USA. 87:1541-1545.
59. Berling, B., F. Kolbinger, F. Grunert, J. Thompson, F. Brombacher, F. Buchegger, S. von Kleist, and W. Zimmermann. 1990. Cloning of a carcinoembryonic antigen gene family member expressed in leukocytes of chronic myeloid leukemia patients and bone marrow. Cancer Res. 50:6534-6539.
60. Skubitz, K.M., K. Micklem, and E. Van Der Schoot. 1995. CD66 and CD67 cluster workshop report. In Leucocyte Typing V. S.F. Schlossman, editor. Oxford University Press, Oxford. 889-899.
61. Keegan, A., and W. Paul. 1992. Multichain immune recognition receptors: similarities in structure and signaling pathways. Immunol. Today. 13:63-68.
62. Reth, M. 1995. The tyrosine activation motif as a target of protein tyrosine kinases and SH2 domains. Semin. Immunol. 7: 21-27.
63. Greenberg, S. 1995. Signal transduction of phagocytosis. Trends Cell Biol. 5:93-99.
64. Muta, T., T. Kurosaki, Z. Misulovin, M. Sanchez, M. Nussenzweig, and J. Ravetch. 1994. A 13-amino-acid motif in the cytoplasmic domain of Fc gamma RIIB modulates B-cell receptor signalling. Nature (Lond.). 368:70-73.
65. Daeron, M., S. Latour, O. Malbec, E. Espinosa, P. Pina, S. Pasmans, and W. Fridman. 1995. The same tyrosine-based inhibition motif, in the intracytoplasmic domain of Fc gamma RIIB regulates negatively BCR-, TCR-, and FcR-dependent cell activation. Immunity. 3:635-646.
66. Hefta, S., L. Hefta, T. Lee, R. Paxton, and J. Shively. 1988. Carcinoembryonic antigen is anchored to membranes by covalent attachment to a glycosylphosphatidylinositol moiety: identification of the ethanolamine linkage site. Proc. Natl. Acad. Sci. USA. 85:4648-4652.
67. Mayne, K., K. Pulford, M. Jones, K. Micklem, G. Nagel, C. van der Schoot, and D. Mason. 1993. Antibody By114 is selective for the 90 kD PI-linked component of the CD66 antigen: a new reagent for the study of paroxysmal nocturnal haemoglobinuria. Br. J. Haematol. 83:30-38.
68. Deckert, M., M. Ticchioni, and A. Bernard. 1996. Endocytosis of GPI-anchored proteins in human lymphocytes: role of glycolipid-based domains, actin cytoskeleton, and protein kinases. J. Cell Biol. 133:791-799.
69. McConville, M., and M. Ferguson. 1993. The structure, biosynthesis and function of glycosylated phosphatidylinositols in the parasitic protozoa and higher eukaryotes. Biochem. J. 294: 305-324.
70. Lisanti, M., Z. Tang, P. Scherer, E. Kubler, A. Koleske, and M. Sargiacomo. 1995. Caveolae, transmembrane signaling and cellular transformation. Mol. Membr. Biol. 12:121-124.
71. Falkow, S. 1991. Bacterial entry into eukaryotic cells. Cell. 65:1099-1102.
72. Shaw, J.H., and S. Falkow. 1988. Model for invasion of human tissue culture cells by Neisseria gonorrhoeae. Infect. Immun. 56:1625-1632.
73. Thompson, J., F. Grunert, and W. Zimmermann. 1991. Carcinoembryonic antigen gene family: molecular biology and clinical perspectives. J. Clin. Lab. Anal. 5:344-366.
74. Prall, F., P. Nollau, M. Neumaier, H. Haubeck, Z. Drzeniek, U. Helmchen, T. Loning, and C. Wagener. 1996. CD66a (BGP) an adhesion molecule of the carcinoembryonic antigen family, is expressed in epithelium, endothelium, and myeloid cells in a wide range of normal human tissues. J. Histochem. Cytochem. 44:35-41.