Skip to main content
NCBI home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1993 Jun;175(11):3664–3668. doi: 10.1128/jb.175.11.3664-3668.1993

Characterization of a stress protein from group B Neisseria meningitidis.

G Arakere 1, M Kessel 1, N Nguyen 1, C E Frasch 1
PMCID: PMC204770  PMID: 8099073

Abstract

Increased levels of a 65-kDa stress protein (Msp65) were observed in group B Neisseria meningitidis grown under stationary-growth conditions. Electron microscopy showed two apposing rings of seven subunits, a structure typical of Escherichia coli GroEL. Msp65 was not found in either the periplasmic space or the outer membrane. Several important differences between the GroEL analogs of N. meningitidis and Neisseria gonorrhoeae are discussed.

Full text

PDF
3664

Images in this article

3665Image
on p.3665
3665Image
on p.3665
3665Image
on p.3665
3666Image
on p.3666

Selected References

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

  1. Ames G. F., Prody C., Kustu S. Simple, rapid, and quantitative release of periplasmic proteins by chloroform. J Bacteriol. 1984 Dec;160(3):1181–1183. doi: 10.1128/jb.160.3.1181-1183.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Banerjee-Bhatnagar N., Frasch C. E. Expression of Neisseria meningitidis iron-regulated outer membrane proteins, including a 70-kilodalton transferrin receptor, and their potential for use as vaccines. Infect Immun. 1990 Sep;58(9):2875–2881. doi: 10.1128/iai.58.9.2875-2881.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Black J. R., Dyer D. W., Thompson M. K., Sparling P. F. Human immune response to iron-repressible outer membrane proteins of Neisseria meningitidis. Infect Immun. 1986 Dec;54(3):710–713. doi: 10.1128/iai.54.3.710-713.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Burns D. L., Gould-Kostka J. L., Kessel M., Arciniega J. L. Purification and immunological characterization of a GroEL-like protein from Bordetella pertussis. Infect Immun. 1991 Apr;59(4):1417–1422. doi: 10.1128/iai.59.4.1417-1422.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Burton Z. F., Eisenberg D. A procedure for rapid isolation of both groE protein and glutamine synthetase from E coli. Arch Biochem Biophys. 1980 Dec;205(2):478–488. doi: 10.1016/0003-9861(80)90130-7. [DOI] [PubMed] [Google Scholar]
  6. Catlin B. W. Nutritional profiles of Neisseria gonorrhoeae, Neisseria meningitidis, and Neisseria lactamica in chemically defined media and the use of growth requirements for gonococcal typing. J Infect Dis. 1973 Aug;128(2):178–194. doi: 10.1093/infdis/128.2.178. [DOI] [PubMed] [Google Scholar]
  7. De Bruyn J., Bosmans R., Turneer M., Weckx M., Nyabenda J., Van Vooren J. P., Falmagne P., Wiker H. G., Harboe M. Purification, partial characterization, and identification of a skin-reactive protein antigen of Mycobacterium bovis BCG. Infect Immun. 1987 Jan;55(1):245–252. doi: 10.1128/iai.55.1.245-252.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Elias D., Reshef T., Birk O. S., van der Zee R., Walker M. D., Cohen I. R. Vaccination against autoimmune mouse diabetes with a T-cell epitope of the human 65-kDa heat shock protein. Proc Natl Acad Sci U S A. 1991 Apr 15;88(8):3088–3091. doi: 10.1073/pnas.88.8.3088. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Frasch C. E., Peppler M. S. Protection against group B Neisseria meningitidis disease: preparation of soluble protein and protein-polysaccharide immunogens. Infect Immun. 1982 Jul;37(1):271–280. doi: 10.1128/iai.37.1.271-280.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Hemmingsen S. M., Woolford C., van der Vies S. M., Tilly K., Dennis D. T., Georgopoulos C. P., Hendrix R. W., Ellis R. J. Homologous plant and bacterial proteins chaperone oligomeric protein assembly. Nature. 1988 May 26;333(6171):330–334. doi: 10.1038/333330a0. [DOI] [PubMed] [Google Scholar]
  11. Hohn T., Hohn B., Engel A., Wurtz M., Smith P. R. Isolation and characterization of the host protein groE involved in bacteriophage lambda assembly. J Mol Biol. 1979 Apr 15;129(3):359–373. doi: 10.1016/0022-2836(79)90501-1. [DOI] [PubMed] [Google Scholar]
  12. Houston L. S., Cook R. G., Norris S. J. Isolation and characterization of a Treponema pallidum major 60-kilodalton protein resembling the groEL protein of Escherichia coli. J Bacteriol. 1990 Jun;172(6):2862–2870. doi: 10.1128/jb.172.6.2862-2870.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Jindal S., Dudani A. K., Singh B., Harley C. B., Gupta R. S. Primary structure of a human mitochondrial protein homologous to the bacterial and plant chaperonins and to the 65-kilodalton mycobacterial antigen. Mol Cell Biol. 1989 May;9(5):2279–2283. doi: 10.1128/mcb.9.5.2279. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  15. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  16. Moos M., Jr, Nguyen N. Y., Liu T. Y. Reproducible high yield sequencing of proteins electrophoretically separated and transferred to an inert support. J Biol Chem. 1988 May 5;263(13):6005–6008. [PubMed] [Google Scholar]
  17. Morgan R. W., Christman M. F., Jacobson F. S., Storz G., Ames B. N. Hydrogen peroxide-inducible proteins in Salmonella typhimurium overlap with heat shock and other stress proteins. Proc Natl Acad Sci U S A. 1986 Nov;83(21):8059–8063. doi: 10.1073/pnas.83.21.8059. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Pannekoek Y., van Putten J. P., Dankert J. Identification and molecular analysis of a 63-kilodalton stress protein from Neisseria gonorrhoeae. J Bacteriol. 1992 Nov;174(21):6928–6937. doi: 10.1128/jb.174.21.6928-6937.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Rodden J. L., Scocca J. J. Purification and properties of cyclic phosphodiesterase: 3'-nucleotidase, a periplasmic enzyme of Haemophilus influenzae. Arch Biochem Biophys. 1972 Dec;153(2):837–844. doi: 10.1016/0003-9861(72)90406-7. [DOI] [PubMed] [Google Scholar]
  20. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Valentine R. C., Shapiro B. M., Stadtman E. R. Regulation of glutamine synthetase. XII. Electron microscopy of the enzyme from Escherichia coli. Biochemistry. 1968 Jun;7(6):2143–2152. doi: 10.1021/bi00846a017. [DOI] [PubMed] [Google Scholar]
  22. West S. E., Sparling P. F. Response of Neisseria gonorrhoeae to iron limitation: alterations in expression of membrane proteins without apparent siderophore production. Infect Immun. 1985 Feb;47(2):388–394. doi: 10.1128/iai.47.2.388-394.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Woods M. L., 2nd, Bonfiglioli R., McGee Z. A., Georgopoulos C. Synthesis of a select group of proteins by Neisseria gonorrhoeae in response to thermal stress. Infect Immun. 1990 Mar;58(3):719–725. doi: 10.1128/iai.58.3.719-725.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Yang X. D., Gasser J., Feige U. Prevention of adjuvant arthritis in rats by a nonapeptide from the 65-kD mycobacterial heat shock protein: specificity and mechanism. Clin Exp Immunol. 1992 Jan;87(1):99–104. doi: 10.1111/j.1365-2249.1992.tb06420.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Young R. A. Stress proteins and immunology. Annu Rev Immunol. 1990;8:401–420. doi: 10.1146/annurev.iy.08.040190.002153. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES