Regulation of the phosphorylation of human pharyngeal cell proteins by group A streptococcal surface dehydrogenase: Signal transduction between streptococci and pharyngeal cells

Journal of Experimental Medicine

Volumn 186, Issue 10, 1997, Pages 1633-1643

  Pancholi, Vijaykumar ^a   Fischetti, Vincent A ^a  

^a ROCKEFELLER UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; GENISTEIN; IODINE 125; MONOCLONAL ANTIBODY; OXIDOREDUCTASE; PROTEIN KINASE INHIBITOR; STAUROSPORINE;

ARTICLE; BACTERIAL INFECTION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME PURIFICATION; GENETIC TRANSCRIPTION; HUMAN; HUMAN CELL; PHARYNGITIS; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; SIGNAL TRANSDUCTION; STREPTOCOCCUS GROUP A; STREPTOCOCCUS INFECTION;

AMINO ACID SEQUENCE; BACTERIAL ADHESION; BACTERIAL PROTEINS; CARCINOMA, SQUAMOUS CELL; CELL FRACTIONATION; CELL SURVIVAL; CYTOSOL; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASES; HISTONES; HUMANS; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; PHARYNGEAL NEOPLASMS; PHARYNX; PHOSPHOPROTEINS; PHOSPHORYLATION; RECEPTORS, CELL SURFACE; SIGNAL TRANSDUCTION; STREPTOCOCCUS PYOGENES; TUMOR CELLS, CULTURED;

EID: 0030661706     PISSN: 00221007     EISSN: None     Source Type: Journal    
DOI: 10.1084/jem.186.10.1633     Document Type: Article

References (43)

1. Johnson, D.R., D.L. Stevens, and E.L. Kaplan. 1992. Epidemiologic analysis of group A streptococcal serotypes associated with systemic infection, rheumatic fever, or uncomplicated pharyngitis. J. Infect. Dis. 166:374-382.
2. Stevens, D.L. 1995. Streptococcal toxic-shock syndrome: spectrum of disease, pathogenesis, and new concepts in treatment. Emerg. Infect. Dis. 1:69-78.
3. Falkow, S., R.R. Isberg, and D.A. Portnoy. 1992. The interaction of bacteria with mammalian cells. Annu. Rev. Cell Biol. 8:333-363.
4. Bliska, J.B., J.E. Galan, and S. Falkow. 1993. Signal transduction in the mammalian cell during bacterial attachment and entry. Cell. 73:903-920.
5. Ginocchio, C.C., S.B. Olmsted, C.L. Wells, and J.E. Galan. 1994. Contact with epithelial cells induces the formation of surface appendages on Salmonella typhimurium. Cell. 76:717-724.
6. Iseberg, R.R. 1991. Discrimination between intracellular up-take and surface adhesion of bacterial pathogens. Science (Wash. DC). 252:934-938.
7. Cossart, P., P. Bouquet, S. Normark, and R. Rappuoli. 1996. Cellular microbiology emerging. Science (Wash. DC). 271:315-316.
8. Finlay, B.B., and P. Cossart. 1997. Exploitation of mammalian host cell functions by bacterial pathogens. Science (Wash. DC). 276:718-725.
9. Kehoe, M.A. 1994. Cell-wall-associated proteins in gram-positive bacteria. In Bacterial Cell Wall. J.-M. Ghuysen and R. Hakenbeck, editors. Elsevier Science, Amsterdam. 217-261.
10. Pancholi, V., and V.A. Fischetti. 1992. A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate dehydrogenase with multiple binding activity. J. Exp. Med. 176:415-426.
11. Pancholi, V., and V.A. Fischetti. 1993. Glyceraldehyde-3-phosphate dehydrogenase on the surface of group A streptococci is also an ADP-ribosylating enzyme. Proc. Natl. Acad. Sci. USA. 90:8154-8158.
12. Kolberg, J., and K. Sletten. 1996. Monoclonal antibodies that recognize a common pneumococcal protein with similarities to streptococcal group A surface glyceraldehyde-3-phosphate dehydrogenase. Infect. Immun. 64:3544-3547.
13. Sirover, M. 1996. Emerging new functions of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in mammalian cells. Life Sci. 58:2271-2272.
14. Doucet, J.-P., and B.S. Tuana. 1991. Identification of low molecular weight GTP-binding proteins and their sites of interaction in subcellular fractions from skeletal muscle. J. Biol. Chem. 266:17631-17620.
15. Rosenshine, I., M.S. Donnenberg, J.B. Kaper, and B.B. Finlay. 1992. Signal transduction between enteropathogenic Escherichia coli (EPEC) and epithelial cells: EPEC induces tyrosine phosphorylation of host cell proteins to initiate cytoskeletal rearrangement and bacterial uptake. EMBO (Eur. Mol. Biol. Organ.) J. 11:3551-3560.
16. Galan, J.E., J. Pace, and M.J. Hayman. 1992. Involvement of the epidermal growth factor receptor in the invasion of cultured mammalian cells by Salmonella typhimurium. Nature (Lond.). 357:588-589.
17. Fischetti, V.A., K.F. Jones, B.N. Manjula, and J.R. Scott. 1984. Streptococcal M6 protein expressed in Escherichia coli. Localization, purification and comparison with streptococcal-derived M protein. J. Exp. Med. 159:1083-1095.
18. Matsudaira, P. 1987. Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 262:10035-10038.
19. Rubens, C.E., S. Smith, M. Hulse, E.Y. Chi, and G. van Belle. 1992. Respiratory epithelial cell invasion by group B streptococci. Inject. Immun. 60:5157-5163.
20. Fischetti, V.A. 1989. Streptococcal M protein: Molecular design and biological behavior. Clin. Microbiol. Rev. 2:285-314.
21. cdc2-kinase activity and histone H1 hyperphosphorylation, but is associated with enhanced histone H2A and H3 phosphorylation. EMBO (Eur. Mol. Biol. Organ.) J. 14:976-985.
22. Th'ng, J.P.M., G. Xiao-Wen, R.A. Swank, H.A. Crissman, and E. M. Bradbury. 1994. Inhibition of histone phosphorylation by staurosporine leads to chromosome decondensation. J. Biol. Chem. 269:9568-9573.
23. Paulson, J.R., and S.S. Taylor. 1982. Phosphorylation of histones 1 and 3 and nonhistone high mobiltiy group 14 by an endogenous kinase in HeLa metaphase chromosomes. J. Biol. Chem. 257:6064-6072.
24. Cano, E., C.A. Hazzalin, E. Kardalmou, R.S. Buckle, and L.C. Mahadevan. 1995. Neither ERK nor JNK/SAPK MAP kinase subtypes are essential for histone H3/HMG-14 phosphorylation or c-fos and C-jun induction. J. Cell Sci. 108: 3599-3609.
25. s6k containing a bifurcation to histone H3-HMG-like protein phosphorylation and c-fos-c-jun induction. Mol. Cell. Biol. 14:1066-1074.
26. Olins, D.E., and A.L. Olins. 1978. Nucleosomes: the structural quantum in chromosomes. Am. Sci. 66:704-711.
27. Schlessinger, J., and A. Ullrich. 1992. Growth factor signaling by receptor tyrosine kinases. Neuron. 9:383-391.
28. Laskey, R.A. 1983. Phosphorylation of nuclear proteins. Phil. Trans. R. Soc. Lond. B. Biol. Sci. 302:143-150.
29. Whitlock, Jr., D. Galeazzi, and H. Schulman. 1983. Acetylation and calcium-dependent phosphorylation of histone H3 in nuclei from butyrate-treated HeLa cells. J. Biol. Chem. 258:1299-1304.
30. Shibata, K., and K. Ajiro. 1993. Cell cycle-dependent suppressive effect of histone H1 on mitosis-specific H3 phosphorylation. J. Biol. Chem. 268:18431-18434.
31. Grunstein, M. 1992. Histones as regulators of genes. Sci. Am. 68-74.
32. Whitlock, Jr., R. Augustine, and H. Schulman. 1980. Calcium-dependent phosphorylation of histone H3 in butyrate-treated HeLa cells. Nature (Lond.). 287:74-76.
33. Mahadevan, L.C., A.C. Willis, and M.J. Barratt. 1991. Rapid histone H3 phosphorylation in response to growth factors, phorbol esters, okadaic acid, and protein synthesis inhibitors. Cell. 65:775-783.
34. Barratt, M.J., C.A. Hazzalin, E. Cano, and L.C. Mahadevan. 1994. Mitogen-stimulated phosphorylation of histone H3 is targeted to a small hyperacetylation-sensitive fraction. Proc. Natl. Acad. Sci. USA. 91:4781-4785.
35. Seger, R., and E.G. Krebs. 1995. The MAPK signaling cascade. FASEB (Fed. Am. Soc. Exp. Biol.) J. 9:726-735.
36. Robbins, D.J., E. Zhen, H. Owaki, C.A. Vanderbilt, D. Ebert, T.D. Geppert, and M.H. Cobb. 1993. Regulation of properties of extracellular signal-regulated protein kinases 1 and 2 in vitro. J. Biol. Chem. 268:5097-5106.
37. Goldschmidt-Clermont, P.J., J.W. Kim, L.M. Machesky, S.G. Rhee, and T.D. Pollard. 1991. Regulation of phospholipase C-gamma1 by profilin and tryrosine phosphorylation. Science (Wash. DC). 1231-1233.
38. Shariff, A., and E.J. Luna. 1992. Diacylglycerol-stimulated formation of actin nucleation sites at plasma membranes. Scieitce (Wash. DC). 256:245-247.
39. Goudot-Crozel, V., D. Caillol. M. Djabali, and A.J. Dessein. 1989. The major parasite surface antigen associated with human resistance to schistosomiasis is a 37-kD glyceraldehyde3P-dehydrogenase. J. Exp. Med. 170:2065-2080.
40. Fernandes, P.A., J.N. Keen, J.B.C. Findlay, and P. Moradas-Ferreira. 1992. A protein homologous to glyceraldehyde-3-phosphate dehydrogenase is induced in the cell wall of a flocculent Kluyveromyces marxianus. Biochim. Biophys. Acta 1159:67-73.
41. Hannaert, V., M. Blaauw, L. Kohl, S. Allert, F.R. Opperdoes, and P.A.M. Michels. 1992. Molecular analysis of the cytosolic and glycosomal glyceraldehyde-3-phosphate dehydrogenase in Leshmania mexicana. Mol. Biochem. Parasitol. 45:155-162.
42. Kendall, G., A.F. Wilderspin, F. Ashall, M.A. Miles, and J.M. Kelly. 1990. Trypanosoma cruzi glycosomal glyceraldehyde-3-phosphate dehydrogenase does not conform to the 'hot spot' topogenic signal model. EMBO (Eur. Mol. Biol. Organ.) J. 9: 2751-2758.
43. Gil-Navarro, I., M.L. Gil, M. Casanova, J.E. O'Connor, J.P. Martinez, and D. Gozalbo. 1997. The glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase of Candida albicans is a surface antigen. J. Bacteriol. 179:4992-4999.