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. 1985 Jul;163(1):69–74. doi: 10.1128/jb.163.1.69-74.1985

Analysis of Neisseria gonorrhoeae peptidoglycan by reverse-phase, high-pressure liquid chromatography.

T J Dougherty
PMCID: PMC219081  PMID: 3924898

Abstract

The muramidase digest of peptidoglycan from Neisseria gonorrhoeae was isolated and analyzed by the use of a reverse-phase, high-pressure liquid chromatography system. As was found previously in the case of Escherichia coli, gonococci peptidoglycan is also composed of a greater number of muropeptides than can be resolved with thin-layer chromatography systems. Preliminary classification of the muropeptide components into subclasses based on O-acetyl modification and degree of cross-linkage was achieved. Examination of a penicillin-susceptible strain and a highly resistant strain with two penicillin-binding protein alterations synthesized distinctly different peptidoglycan structures, as revealed by this technique.

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Selected References

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  1. 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]
  2. Dougherty T. J. Peptidoglycan biosynthesis in Neisseria gonorrhoeae strains sensitive and intrinsically resistant to beta-lactam antibiotics. J Bacteriol. 1983 Jan;153(1):429–435. doi: 10.1128/jb.153.1.429-435.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Ghuysen J. M., Bricas E., Lache M., Leyh-Bouille M. Structure of the cell walls of Micrococcus lysodeikticus. 3. Isolation of a new peptide dimer, N-alpha-[L-alanyl-gamma-(alpha-D-glutamylglycine)]-L-lysyl-D-alanyl-N-alpha-[L-alanyl-gamma-(alpha-D-glutamylglycine)]-L-lysyl-D-alanine. Biochemistry. 1968 Apr;7(4):1450–1460. doi: 10.1021/bi00844a030. [DOI] [PubMed] [Google Scholar]
  4. Goodell E. W., Fazio M., Tomasz A. Effect of benzylpenicillin on the synthesis and structure of the cell envelope of Neisseria gonorrhoeae. Antimicrob Agents Chemother. 1978 Mar;13(3):514–526. doi: 10.1128/aac.13.3.514. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Hebeler B. H., Wong W., Morse S. A., Young F. E. Cell envelope of Neisseria gonorrhoeae CS7: peptidoglycan protein complex. Infect Immun. 1979 Feb;23(2):353–359. doi: 10.1128/iai.23.2.353-359.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Hebeler B. H., Young F. E. Chemical composition and turnover of peptidoglycan in Neisseria gonorrhoeae. J Bacteriol. 1976 Jun;126(3):1180–1185. doi: 10.1128/jb.126.3.1180-1185.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Petersen B. H., Rosenthal R. S. Complement consumption gonococcal peptidoglycan. Infect Immun. 1982 Feb;35(2):442–448. doi: 10.1128/iai.35.2.442-448.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. 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]
  9. Rosenthal R. S., Folkening W. J., Miller D. R., Swim S. C. Resistance of O-acetylated gonococcal peptidoglycan to human peptidoglycan-degrading enzymes. Infect Immun. 1983 Jun;40(3):903–911. doi: 10.1128/iai.40.3.903-911.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Rosenthal R. S. Release of soluble peptidoglycan from growing gonococci: hexaminidase and amidase activities. Infect Immun. 1979 Jun;24(3):869–878. doi: 10.1128/iai.24.3.869-878.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Rosenthal R. S., Wright R. M., Sinha R. K. Extent of peptide cross-linking in the peptidoglycan of Neisseria gonorrhoeae. Infect Immun. 1980 Jun;28(3):867–875. doi: 10.1128/iai.28.3.867-875.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Schleifer K. H., Kandler O. Peptidoglycan types of bacterial cell walls and their taxonomic implications. Bacteriol Rev. 1972 Dec;36(4):407–477. doi: 10.1128/br.36.4.407-477.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Sinha R. K., Rosenthal R. S. Release of soluble peptidoglycan from growing conococci: demonstration of anhydro-muramyl-containing fragments. Infect Immun. 1980 Sep;29(3):914–925. doi: 10.1128/iai.29.3.914-925.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Spratt B. G. Escherichia coli resistance to beta-lactam antibiotics through a decrease in the affinity of a target for lethality. Nature. 1978 Aug 17;274(5672):713–715. doi: 10.1038/274713a0. [DOI] [PubMed] [Google Scholar]
  15. Spratt B. G. Penicillin-binding proteins and the future of beta-lactam antibiotics. The Seventh Fleming Lecture. J Gen Microbiol. 1983 May;129(5):1247–1260. doi: 10.1099/00221287-129-5-1247. [DOI] [PubMed] [Google Scholar]
  16. Swanson J. Studies on gonococcus infection. XII. Colony color and opacity varienats of gonococci. Infect Immun. 1978 Jan;19(1):320–331. doi: 10.1128/iai.19.1.320-331.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Wolf-Watz H., Elmros T., Normark S., Bloom G. D. Cell envelope of Neisseria gonorrhoeae: outer membrane and peptidoglycan composition of penicillin-sensitive and-resistant strains. Infect Immun. 1975 Jun;11(6):1332–1341. doi: 10.1128/iai.11.6.1332-1341.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]

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