Skip to main content
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1980 Aug;143(2):942–949. doi: 10.1128/jb.143.2.942-949.1980

Outer membrane protein composition of Yersinia pestis at different growth stages and incubation temperatures.

R P Darveau, W T Charnetzky, R E Hurlbert
PMCID: PMC294398  PMID: 7204338

Abstract

The protein composition of the outer membrane of Yersinia pestis grown at 26 and at 37 degrees C was examined. The outer membrane was isolated by isopycnic sucrose density centrifugation, and its degree of purity was determined with known inner and outer membrane components. Using two-dimensional gel electrophoresis, we identified a large number of heat-modifiable proteins in the outer membrane of cells grown at either incubation temperature. One-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis of heated preparations indicated five proteins in the outer membrane of 37 degrees C-grown cells not evident in 26 degrees C-grown cells. Differences in the protein composition of the outer membrane due to the stage of growth were evident at both 26 degrees C and 37 degrees C, although different changes were found at each temperature. When cell envelopes were examined for the presence of peptidoglycan-associated proteins, no differences were seen as a result of stage of growth. Envelopes from 26 degrees C-grown cells yielded two peptidoglycan-associated proteins, E and J. Cells grown at 37 degrees C, however, also contained an additional protein (F) which was not found in either the bound or free form 26 degrees C. The changes in outer membrane protein composition in response to incubation temperature may relate to known nutritional and antigenic changes which occur under the same conditions.

Full text

PDF
942

Images in this article

Selected References

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

  1. Alphen W. V., Lugtenberg B. Influence of osmolarity of the growth medium on the outer membrane protein pattern of Escherichia coli. J Bacteriol. 1977 Aug;131(2):623–630. doi: 10.1128/jb.131.2.623-630.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bradley S. G. Cellular and molecular mechanisms of action of bacterial endotoxins. Annu Rev Microbiol. 1979;33:67–94. doi: 10.1146/annurev.mi.33.100179.000435. [DOI] [PubMed] [Google Scholar]
  3. Brubaker R. R. The genus Yersinia: biochemistry and genetics of virulence. Curr Top Microbiol Immunol. 1972;57:111–158. doi: 10.1007/978-3-642-65297-4_4. [DOI] [PubMed] [Google Scholar]
  4. DiRienzo J. M., Nakamura K., Inouye M. The outer membrane proteins of Gram-negative bacteria: biosynthesis, assembly, and functions. Annu Rev Biochem. 1978;47:481–532. doi: 10.1146/annurev.bi.47.070178.002405. [DOI] [PubMed] [Google Scholar]
  5. Dröge W., Lehmann V., Lüderitz O., Westphal O. Structural investigations on the 2-keto-3-deoxyoctonate region of lipopolysaccharides. Eur J Biochem. 1970 May 1;14(1):175–184. doi: 10.1111/j.1432-1033.1970.tb00276.x. [DOI] [PubMed] [Google Scholar]
  6. Hancock R. E., Carey A. M. Outer membrane of Pseudomonas aeruginosa: heat- 2-mercaptoethanol-modifiable proteins. J Bacteriol. 1979 Dec;140(3):902–910. doi: 10.1128/jb.140.3.902-910.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Hui K. M., Hurlbert R. E. Modifiable chromatophore proteins in photosynthetic bacteria. J Bacteriol. 1979 Apr;138(1):207–217. doi: 10.1128/jb.138.1.207-217.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Koplow J., Goldfine H. Alterations in the outer membrane of the cell envelope of heptose-deficient mutants of Escherichia coli. J Bacteriol. 1974 Feb;117(2):527–543. doi: 10.1128/jb.117.2.527-543.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Kurland C. G. The requirements for specific sRNA binding by ribosomes. J Mol Biol. 1966 Jun;18(1):90–108. doi: 10.1016/s0022-2836(66)80079-7. [DOI] [PubMed] [Google Scholar]
  10. 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]
  11. 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]
  12. Lane B. C., Hurlbert R. E. Characterization of the cell wall and cell wall proteins of Chromatium vinosum. J Bacteriol. 1980 Mar;141(3):1386–1398. doi: 10.1128/jb.141.3.1386-1398.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Lugtenberg B., Bronstein H., van Selm N., Peters R. Peptidoglycan-associated outer membrane proteins in gammegatine bacteria. Biochim Biophys Acta. 1977 Mar 17;465(3):571–578. doi: 10.1016/0005-2736(77)90274-7. [DOI] [PubMed] [Google Scholar]
  14. Lugtenberg B., Peters R., Bernheimer H., Berendsen W. Influence of cultural conditions and mutations on the composition of the outer membrane proteins of Escherichia coli. Mol Gen Genet. 1976 Sep 23;147(3):251–262. doi: 10.1007/BF00582876. [DOI] [PubMed] [Google Scholar]
  15. Nakamura K., Mizushima S. Effects of heating in dodecyl sulfate solution on the conformation and electrophoretic mobility of isolated major outer membrane proteins from Escherichia coli K-12. J Biochem. 1976 Dec;80(6):1411–1422. doi: 10.1093/oxfordjournals.jbchem.a131414. [DOI] [PubMed] [Google Scholar]
  16. Osborn M. J., Gander J. E., Parisi E. Mechanism of assembly of the outer membrane of Salmonella typhimurium. Site of synthesis of lipopolysaccharide. J Biol Chem. 1972 Jun 25;247(12):3973–3986. [PubMed] [Google Scholar]
  17. Osborn M. J., Rick P. D., Lehmann V., Rupprecht E., Singh M. Structure and biogenesis of the cell envelope of gram-negative bacteria. Ann N Y Acad Sci. 1974 May 10;235(0):52–65. doi: 10.1111/j.1749-6632.1974.tb43256.x. [DOI] [PubMed] [Google Scholar]
  18. Paakkanen J., Gotschlich E. C., Mäkelä P. H. Protein K: a new major outer membrane protein found in encapsulated Escherichia coli. J Bacteriol. 1979 Sep;139(3):835–841. doi: 10.1128/jb.139.3.835-841.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Reithmeier R. A., Bragg P. D. Molecular characterization of a heat-modifiable protein from the outer membrane of Escherichia coli. Arch Biochem Biophys. 1977 Jan 30;178(2):527–534. doi: 10.1016/0003-9861(77)90223-5. [DOI] [PubMed] [Google Scholar]
  20. Rest R. F., Cooney M. H., Spitznagel J. K. Susceptibility of lipopolysaccharide mutants to the bactericidal action of human neutrophil lysosomal fractions. Infect Immun. 1977 Apr;16(1):145–151. doi: 10.1128/iai.16.1.145-151.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Rosenbusch J. P. Characterization of the major envelope protein from Escherichia coli. Regular arrangement on the peptidoglycan and unusual dodecyl sulfate binding. J Biol Chem. 1974 Dec 25;249(24):8019–8029. [PubMed] [Google Scholar]
  22. Schnaitman C. A. Outer membrane proteins of Escherichia coli. IV. Differences in outer membrane proteins due to strain and cultural differences. J Bacteriol. 1974 May;118(2):454–464. doi: 10.1128/jb.118.2.454-464.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Schweizer M., Hindennach I., Garten W., Henning U. Major proteins of the Escherichia coli outer cell envelope membrane. Interaction of protein II with lipopolysaccharide. Eur J Biochem. 1978 Jan 2;82(1):211–217. doi: 10.1111/j.1432-1033.1978.tb12013.x. [DOI] [PubMed] [Google Scholar]

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

RESOURCES