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. 1994 Jun;62(6):2404–2408. doi: 10.1128/iai.62.6.2404-2408.1994

Plasmid regulation and temperature-sensitive behavior of the Yersinia pestis penicillin-binding proteins.

R C Ferreira 1, J T Park 1, L C Ferreira 1
PMCID: PMC186525  PMID: 8188365

Abstract

Six major bands corresponding to penicillin-binding proteins (PBPs) with molecular weights ranging from 43,000 to 97,000 were detected in cell envelopes of Yersinia pestis EV76 grown at 28 degrees C. When cells were transferred to 37 degrees C and incubated for extended periods of time, the amounts of all PBPs, except for PBP2, were gradually reduced in cell envelopes of a strain carrying a 75-kb virulence-associated plasmid (as measured by penicillin-binding capacity), whereas in a strain cured of the plasmid, all PBPs were stable. The results indicated that the stability and/or the expression of Y. pestis PBPs is affected by a temperature-inducible pathway associated with the virulence-associated plasmid.

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Selected References

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

  1. Abath F. G., de Almeida A. M., Ferreira L. C. Strain specific variation of outer membrane proteins of wild Yersinia pestis strains subjected to different growth temperatures. Mem Inst Oswaldo Cruz. 1990 Jan-Mar;85(1):107–111. doi: 10.1590/s0074-02761990000100018. [DOI] [PubMed] [Google Scholar]
  2. BRUBAKER R. R., SURGALLA M. J. THE EFFECT OF CA++ AND MG++ ON LYSIS, GROWTH, AND PRODUCTION OF VIRULENCE ANTIGENS BY PASTEURELLA PESTIS. J Infect Dis. 1964 Feb;114:13–25. doi: 10.1093/infdis/114.1.13. [DOI] [PubMed] [Google Scholar]
  3. Brubaker R. R. Growth of Pasteurella pseudotuberculosis in simulated intracellular and extracellular environments. J Infect Dis. 1967 Dec;117(5):403–417. doi: 10.1093/infdis/117.5.403. [DOI] [PubMed] [Google Scholar]
  4. Buchanan C. E., Sowell M. O. Synthesis of penicillin-binding protein 6 by stationary-phase Escherichia coli. J Bacteriol. 1982 Jul;151(1):491–494. doi: 10.1128/jb.151.1.491-494.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Buchanan C. E. Topographical distribution of penicillin-binding proteins in the Escherichia coli membrane. J Bacteriol. 1981 Mar;145(3):1293–1298. doi: 10.1128/jb.145.3.1293-1298.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Cornelis G. R., Biot T., Lambert de Rouvroit C., Michiels T., Mulder B., Sluiters C., Sory M. P., Van Bouchaute M., Vanooteghem J. C. The Yersinia yop regulon. Mol Microbiol. 1989 Oct;3(10):1455–1459. doi: 10.1111/j.1365-2958.1989.tb00129.x. [DOI] [PubMed] [Google Scholar]
  7. Dargis M., Gourde P., Beauchamp D., Foiry B., Jacques M., Malouin F. Modification in penicillin-binding proteins during in vivo development of genetic competence of Haemophilus influenzae is associated with a rapid change in the physiological state of cells. Infect Immun. 1992 Oct;60(10):4024–4031. doi: 10.1128/iai.60.10.4024-4031.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Darveau R. P., Charnetzky W. T., Hurlbert R. E. Outer membrane protein composition of Yersinia pestis at different growth stages and incubation temperatures. J Bacteriol. 1980 Aug;143(2):942–949. doi: 10.1128/jb.143.2.942-949.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Darveau R. P., Charnetzky W. T., Hurlbert R. F., Hancock R. E. Effects of growth temperature, 47-megadalton plasmid, and calcium deficiency on the outer membrane protein porin and lipopolysaccharide composition of Yersinia pestis EV76. Infect Immun. 1983 Dec;42(3):1092–1101. doi: 10.1128/iai.42.3.1092-1101.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Georgopapadakou N. H., Liu F. Y. Penicillin-binding proteins in bacteria. Antimicrob Agents Chemother. 1980 Jul;18(1):148–157. doi: 10.1128/aac.18.1.148. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. HIGUCHI K., KUPFERBERG L. L., SMITH J. L. Studies on the nutrition and physiology of Pasteurella pestis. III. Effects of calcium ions on the growth of virulent and avirulent strains of Pasteurella pestis. J Bacteriol. 1959 Mar;77(3):317–321. doi: 10.1128/jb.77.3.317-321.1959. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. 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]
  13. Malouin F., Bryan L. E. Haemophilus influenzae penicillin-binding proteins 1a and 3 possess distinct and opposite temperature-modulated penicillin-binding activities. Antimicrob Agents Chemother. 1988 Apr;32(4):498–502. doi: 10.1128/aac.32.4.498. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Malouin F., Parr T. R., Jr, Bryan L. E. Identification of a group of Haemophilus influenzae penicillin-binding proteins that may have complementary physiological roles. Antimicrob Agents Chemother. 1990 Feb;34(2):363–365. doi: 10.1128/aac.34.2.363. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Mehigh R. J., Braubaker R. R. Major stable peptides of Yersinia pestis synthesized during the low-calcium response. Infect Immun. 1993 Jan;61(1):13–22. doi: 10.1128/iai.61.1.13-22.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Nanninga N. Cell division and peptidoglycan assembly in Escherichia coli. Mol Microbiol. 1991 Apr;5(4):791–795. doi: 10.1111/j.1365-2958.1991.tb00751.x. [DOI] [PubMed] [Google Scholar]
  17. Pisabarro A. G., de Pedro M. A., Vázquez D. Structural modifications in the peptidoglycan of Escherichia coli associated with changes in the state of growth of the culture. J Bacteriol. 1985 Jan;161(1):238–242. doi: 10.1128/jb.161.1.238-242.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Pollack C., Straley S. C., Klempner M. S. Probing the phagolysosomal environment of human macrophages with a Ca2+-responsive operon fusion in Yersinia pestis. 1986 Aug 28-Sep 3Nature. 322(6082):834–836. doi: 10.1038/322834a0. [DOI] [PubMed] [Google Scholar]
  19. Portnoy D. A., Wolf-Watz H., Bolin I., Beeder A. B., Falkow S. Characterization of common virulence plasmids in Yersinia species and their role in the expression of outer membrane proteins. Infect Immun. 1984 Jan;43(1):108–114. doi: 10.1128/iai.43.1.108-114.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Sodeinde O. A., Subrahmanyam Y. V., Stark K., Quan T., Bao Y., Goguen J. D. A surface protease and the invasive character of plague. Science. 1992 Nov 6;258(5084):1004–1007. doi: 10.1126/science.1439793. [DOI] [PubMed] [Google Scholar]
  21. Spratt B. G., Cromie K. D. Penicillin-binding proteins of gram-negative bacteria. Rev Infect Dis. 1988 Jul-Aug;10(4):699–711. doi: 10.1093/clinids/10.4.699. [DOI] [PubMed] [Google Scholar]
  22. Spratt B. G. Properties of the penicillin-binding proteins of Escherichia coli K12,. Eur J Biochem. 1977 Jan;72(2):341–352. doi: 10.1111/j.1432-1033.1977.tb11258.x. [DOI] [PubMed] [Google Scholar]
  23. Straley S. C., Brubaker R. R. Cytoplasmic and membrane proteins of yersiniae cultivated under conditions simulating mammalian intracellular environment. Proc Natl Acad Sci U S A. 1981 Feb;78(2):1224–1228. doi: 10.1073/pnas.78.2.1224. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Straley S. C. The low-Ca2+ response virulence regulon of human-pathogenic Yersiniae. Microb Pathog. 1991 Feb;10(2):87–91. doi: 10.1016/0882-4010(91)90069-m. [DOI] [PubMed] [Google Scholar]
  25. Straley S. C. The plasmid-encoded outer-membrane proteins of Yersinia pestis. Rev Infect Dis. 1988 Jul-Aug;10 (Suppl 2):S323–S326. doi: 10.1093/cid/10.supplement_2.s323. [DOI] [PubMed] [Google Scholar]
  26. Tuomanen E., Cozens R. Changes in peptidoglycan composition and penicillin-binding proteins in slowly growing Escherichia coli. J Bacteriol. 1987 Nov;169(11):5308–5310. doi: 10.1128/jb.169.11.5308-5310.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Tuomanen E., Markiewicz Z., Tomasz A. Autolysis-resistant peptidoglycan of anomalous composition in amino-acid-starved Escherichia coli. J Bacteriol. 1988 Mar;170(3):1373–1376. doi: 10.1128/jb.170.3.1373-1376.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Zahorchak R. J., Brubaker R. R. Effect of exogenous nucleotides on Ca2+ dependence and V antigen synthesis in Yersinia pestis. Infect Immun. 1982 Dec;38(3):953–959. doi: 10.1128/iai.38.3.953-959.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]

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