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. 1987 Nov;169(11):5298–5300. doi: 10.1128/jb.169.11.5298-5300.1987

Identification of Treponema pallidum penicillin-binding proteins.

T M Cunningham 1, J N Miller 1, M A Lovett 1
PMCID: PMC213939  PMID: 3312170

Abstract

Penicillin-binding proteins of 180, 89, 80, 68, 61, 41, and 38 kilodaltons were identified in Treponema pallidum (Nichols) by their covalent binding of [35S]benzylpenicillin. Penicillin-binding proteins are localized in the plasma membranes of many bacterial species and may serve as useful markers for determining plasma membrane intactness in T. pallidum fractionation studies.

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Selected References

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

  1. Alderete J. F., Baseman J. B. Surface characterization of virulent Treponema pallidum. Infect Immun. 1980 Dec;30(3):814–823. doi: 10.1128/iai.30.3.814-823.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Barbour A. G., Todd W. J., Stoenner H. G. Action of penicillin on Borrelia hermsii. Antimicrob Agents Chemother. 1982 May;21(5):823–829. doi: 10.1128/aac.21.5.823. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Blanco D. R., Radolf J. D., Lovett M. A., Miller J. N. The antigenic interrelationship between the endoflagella of Treponema phagedenis biotype Reiter and Treponema pallidum Nichols strain. I. Treponemicidal activity of cross-reactive endoflagellar antibodies against T. pallidum. J Immunol. 1986 Nov 1;137(9):2973–2979. [PubMed] [Google Scholar]
  4. Dougherty T. J. Involvement of a change in penicillin target and peptidoglycan structure in low-level resistance to beta-lactam antibiotics in Neisseria gonorrhoeae. Antimicrob Agents Chemother. 1985 Jul;28(1):90–95. doi: 10.1128/aac.28.1.90. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Dougherty T. J., Koller A. E., Tomasz A. Penicillin-binding proteins of penicillin-susceptible and intrinsically resistant Neisseria gonorrhoeae. Antimicrob Agents Chemother. 1980 Nov;18(5):730–737. doi: 10.1128/aac.18.5.730. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Fehniger T. E., Radolf J. D., Walfield A. M., Cunningham T. M., Miller J. N., Lovett M. A. Native surface association of a recombinant 38-kilodalton Treponema pallidum antigen isolated from the Escherichia coli outer membrane. Infect Immun. 1986 May;52(2):586–593. doi: 10.1128/iai.52.2.586-593.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Hanff P. A., Norris S. J., Lovett M. A., Miller J. N. Purification of Treponema pallidum, Nichols strain, by Percoll density gradient centrifugation. Sex Transm Dis. 1984 Oct-Dec;11(4):275–286. doi: 10.1097/00007435-198410000-00003. [DOI] [PubMed] [Google Scholar]
  8. 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]
  9. MILLER J. N., WHANG S. J., FAZZAN F. P. STUDIES ON IMMUNITY IN EXPERIMENTAL SYPHILIS. I. IMMUNOLOGIC RESPONSE OF RABBITS IMMUNIZED WITH REITER PROTEIN ANTIGEN AND CHALLENGED WITH VIRULENT TREPONEMA PALLIDUM. Br J Vener Dis. 1963 Sep;39:195–198. doi: 10.1136/sti.39.3.195. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. NELL E. E. Comparative sensitivity of treponemes of syphilis, yaws, and bejel to penicillin in vitro, with observations on factors affecting its treponemicidal action. Am J Syph Gonorrhea Vener Dis. 1954 Mar;38(2):92–106. [PubMed] [Google Scholar]
  11. Peterson K. M., Baseman J. B., Alderete J. F. Treponema pallidum receptor binding proteins interact with fibronectin. J Exp Med. 1983 Jun 1;157(6):1958–1970. doi: 10.1084/jem.157.6.1958. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Radolf J. D., Fehniger T. E., Silverblatt F. J., Miller J. N., Lovett M. A. The surface of virulent Treponema pallidum: resistance to antibody binding in the absence of complement and surface association of recombinant antigen 4D. Infect Immun. 1986 May;52(2):579–585. doi: 10.1128/iai.52.2.579-585.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. 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]
  14. Stamm L. V., Bassford P. J., Jr Cellular and extracellular protein antigens of Treponema pallidum synthesized during in vitro incubation of freshly extracted organisms. Infect Immun. 1985 Mar;47(3):799–807. doi: 10.1128/iai.47.3.799-807.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Thomas D. D., Baseman J. B., Alderete J. F. Fibronectin mediates Treponema pallidum cytadherence through recognition of fibronectin cell-binding domain. J Exp Med. 1985 Mar 1;161(3):514–525. doi: 10.1084/jem.161.3.514. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Tomasz A. Penicillin-binding proteins and the antibacterial effectiveness of beta-lactam antibiotics. Rev Infect Dis. 1986 Jul-Aug;8 (Suppl 3):S260–S278. doi: 10.1093/clinids/8.supplement_3.s260. [DOI] [PubMed] [Google Scholar]
  17. Tomasz A. Penicillin-binding proteins in bacteria. Ann Intern Med. 1982 Apr;96(4):502–504. doi: 10.7326/0003-4819-96-4-502. [DOI] [PubMed] [Google Scholar]

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