Peptidoglycan Biosynthesis in Neisseria Gonorrhoeae Strains Sensitive and Intrinsically Resistant to Beta-lactam Antibiotics

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 1983 Jan 1

PMID 6401284

Citations 13

Authors

T J Dougherty

Affiliations

Soon will be listed here.

Abstract

Treatment of penicillin-sensitive and intrinsically resistant Neisseria gonorrhoeae strains with their respective inhibitory concentrations of penicillin caused rapid cell death. When the peptidoglycan syntheses of these two strains were examined in the presence of penicillin, the sensitive strain continued to make this cell wall polymer for an extended time, whereas the resistant strain underwent a rapid and marked depression in synthesis. Examination of the labeled sodium dodecyl sulfate-insoluble peptidoglycan made in the presence of inhibitory concentrations of penicillin revealed further differences. The primary effect on the penicillin-sensitive gonococcus was a slight change in peptide cross-linking and a sharp decline in the degree of O-acetylation. In contrast, the resistant strain exhibited a substantial decline in cross-linking, with a very moderate change in O-acetylation. The degree of saturation of the individual penicillin-binding proteins (PBPs) was assessed under these conditions. PBP 2, which exhibits a reduced affinity for penicillin in the resistant strain, appeared to be related to O-acetylation, whereas PBP 1 was implicated in the transpeptidation reaction.

Citing Articles

Peptidoglycan O-Acetylation as a Virulence Factor: Its Effect on Lysozyme in the Innate Immune System.

Brott A, Clarke A Antibiotics (Basel). 2019; 8(3).

PMID: 31323733 PMC: 6783866. DOI: 10.3390/antibiotics8030094.

Mechanistic Pathways for Peptidoglycan O-Acetylation and De-O-Acetylation.

Sychantha D, Brott A, Jones C, Clarke A Front Microbiol. 2018; 9:2332.

PMID: 30327644 PMC: 6174289. DOI: 10.3389/fmicb.2018.02332.

Peptidoglycan O-acetylation is functionally related to cell wall biosynthesis and cell division in Streptococcus pneumoniae.

Bonnet J, Durmort C, Jacq M, Mortier-Barriere I, Campo N, VanNieuwenhze M Mol Microbiol. 2017; 106(5):832-846.

PMID: 28960579 PMC: 5696066. DOI: 10.1111/mmi.13849.

Postsynthetic Modification of Bacterial Peptidoglycan Using Bioorthogonal N-Acetylcysteamine Analogs and Peptidoglycan O-Acetyltransferase B.

Wang Y, Lazor K, DeMeester K, Liang H, Heiss T, Grimes C J Am Chem Soc. 2017; 139(39):13596-13599.

PMID: 28898061 PMC: 5837961. DOI: 10.1021/jacs.7b06820.

A putatively phase variable gene (dca) required for natural competence in Neisseria gonorrhoeae but not Neisseria meningitidis is located within the division cell wall (dcw) gene cluster.

Snyder L, Saunders N, Shafer W J Bacteriol. 2001; 183(4):1233-41.

PMID: 11157935 PMC: 94996. DOI: 10.1128/JB.183.4.1233-1241.2001.

References

Hash J, ROTHLAUF M . The N,O-diacetylmuramidase of Chalaropsis species. I. Purification and crystallization. J Biol Chem. 1967; 242(23):5586-90. View

Spratt B . Properties of the penicillin-binding proteins of Escherichia coli K12,. Eur J Biochem. 1977; 72(2):341-52. DOI: 10.1111/j.1432-1033.1977.tb11258.x. View

Iwaya M, Strominger J . Simultaneous deletion of D-alanine carboxypeptidase IB-C and penicillin-binding component IV in a mutant of Escherichia coli K12. Proc Natl Acad Sci U S A. 1977; 74(7):2980-4. PMC: 431372. DOI: 10.1073/pnas.74.7.2980. View

Wegener W, Hebeler B, Morse S . Cell envelope of Neisseria gonorrhoeae: relationship between autolysis in buffer and the hydrolysis of peptidoglycan. Infect Immun. 1977; 18(1):210-9. PMC: 421215. DOI: 10.1128/iai.18.1.210-219.1977. View

Wegener W, Hebeler B, Morse S . Cell envelope of Neisseria gonorrhoeae: penicillin enhancement of peptidoglycan hydrolysis. Infect Immun. 1977; 18(3):717-25. PMC: 421294. DOI: 10.1128/iai.18.3.717-725.1977. View

Suzuki H, Nishimura Y, Hirota Y . On the process of cellular division in Escherichia coli: a series of mutants of E. coli altered in the penicillin-binding proteins. Proc Natl Acad Sci U S A. 1978; 75(2):664-8. PMC: 411316. DOI: 10.1073/pnas.75.2.664. View

Matsuhashi M, Maruyama I, Takagaki Y, Tamaki S, Nishimura Y, Hirota Y . Isolation of a mutant of Escherichia coli lacking penicillin-sensitive D-alanine carboxypeptidase IA. Proc Natl Acad Sci U S A. 1978; 75(6):2631-5. PMC: 392616. DOI: 10.1073/pnas.75.6.2631. View

MARTIN H, Gmeiner J . Modification of peptidoglycan structure by penicillin action in cell walls of Proteus mirabilis. Eur J Biochem. 1979; 95(3):487-95. DOI: 10.1111/j.1432-1033.1979.tb12988.x. View

Brown C, Perkins H . In vitro synthesis of peptidoglycan by beta-lactam-sensitive and -resistant strains of Neisseria gonorrhoeae: effects of beta-lactam and other antibiotics. Antimicrob Agents Chemother. 1979; 16(1):28-36. PMC: 352782. DOI: 10.1128/AAC.16.1.28. View

10.

Sinha R, ROSENTHAL R . Release of soluble peptidoglycan from growing conococci: demonstration of anhydro-muramyl-containing fragments. Infect Immun. 1980; 29(3):914-25. PMC: 551218. DOI: 10.1128/iai.29.3.914-925.1980. View

11.

Dougherty T, Koller A, Tomasz A . Penicillin-binding proteins of penicillin-susceptible and intrinsically resistant Neisseria gonorrhoeae. Antimicrob Agents Chemother. 1980; 18(5):730-7. PMC: 284083. DOI: 10.1128/AAC.18.5.730. View

12.

Spratt B . Biochemical and genetical approaches to the mechanism of action of penicillin. Philos Trans R Soc Lond B Biol Sci. 1980; 289(1036):273-83. DOI: 10.1098/rstb.1980.0045. View

13.

Gmeiner J, Kroll H . Murein biosynthesis and O-acetylation of N-acetylmuramic acid during the cell-division cycle of Proteus mirabilis. Eur J Biochem. 1981; 117(1):171-7. DOI: 10.1111/j.1432-1033.1981.tb06317.x. View

14.

Blundell J, Perkins H . Effects of beta-lactam antibiotics on peptidoglycan synthesis in growing Neisseria gonorrhoeae, including changes in the degree of O-acetylation. J Bacteriol. 1981; 147(2):633-41. PMC: 216084. DOI: 10.1128/jb.147.2.633-641.1981. View

15.

Dougherty T, Koller A, Tomasz A . Competition of beta-lactam antibiotics for the penicillin-binding proteins of Neisseria gonorrhoeae. Antimicrob Agents Chemother. 1981; 20(1):109-14. PMC: 181641. DOI: 10.1128/AAC.20.1.109. View

16.

Sinha R, ROSENTHAL R . Effect of penicillin G on release of peptidoglycan fragments by Neisseria gonorrhoeae: characterization of extracellular products. Antimicrob Agents Chemother. 1981; 20(1):98-103. PMC: 181639. DOI: 10.1128/AAC.20.1.98. View

17.

Barbour A . Properties of penicillin-binding proteins in Neisseria gonorrhoeae. Antimicrob Agents Chemother. 1981; 19(2):316-22. PMC: 181418. DOI: 10.1128/AAC.19.2.316. View

18.

Goodell E, Fazio M, Tomasz A . Effect of benzylpenicillin on the synthesis and structure of the cell envelope of Neisseria gonorrhoeae. Antimicrob Agents Chemother. 1978; 13(3):514-26. PMC: 352274. DOI: 10.1128/AAC.13.3.514. View