Bacterial cell envelope peptidoglycan

Microbial Glycobiology: Structures, Relevance and Applications

Volumn , Issue , 2009, Pages 15-28

  Vollmer, Waldemar ^a   Born, Petra ^a  

^a NEWCASTLE UNIVERSITY   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 84907832721     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-374546-0.00002-X     Document Type: Chapter

References (98)

1. Abrams A. O-acetyl groups in the cell wall of Streptococcus faecalis. J. Biol. Chem. 1958, 230:949-959.
2. Aitken A., Stanier R.Y. Characetrization of peptidoglycan from cyanelles of Cyanophora paradoxa. J. Gen. Microbiol. 1979, 112:219-223.
3. Allen N.E., Hobbs J.N., Richardson J.M., Riggin R.M. Biosynthesis of modified peptidoglycan precursors by vancomycin-resistant Enterococcus faecium. FEMS Microbiol. Lett. 1992, 77:109-115.
4. Antignac A., Rousselle J.C., Namane A., Labigne A., Taha M.K., Boneca I.G. Detailed structural analysis of the peptidoglycan of the human pathogen Neisseria meningitidis. J. Biol. Chem. 2003, 278:31521-31528.
5. Araki Y., Nakatani T., Hayashi H., Ito E. Occurrence of non-N-substituted glucosamine residues in lysozyme-resistant peptidoglycan from Bacillus cereus cell walls. Biochem. Biophys. Res. Commun. 1971, 42:691-697.
6. Arthur M., Molinas C., Bugg T.D., Wright G.D., Walsh C.T., Courvalin P. Evidence for in vivo incorporation of d-lactate into peptidoglycan precursors of vancomycin-resistant enterococci. Antimicrob. Agents Chemother. 1992, 36:867-869.
7. Atrih A., Zollner P., Allmaier G., Foster S.J. Structural analysis of Bacillus subtilis 168 endospore peptidoglycan and its role during differentiation. J. Bacteriol. 1996, 178:6173-6183.
8. Atrih A., Bacher G., Allmaier G., Williamson M.P., Foster S.J. Analysis of peptidoglycan structure from vegetative cells of Bacillus subtilis 168 and role of PBP 5 in peptidoglycan maturation. J. Bacteriol. 1999, 181:3956-3966.
9. Azuma I., Thomas D.W., Adam A., et al. Occurrence of N-glycolylmuramic acid in bacterial cell walls. A preliminary survey. Biochim. Biophys. Acta 1970, 208:444-451.
10. Barnickel G., Labischinski H., Bradaczek H., Giesbrecht P. Conformational energy calculation on the peptide part of murein. Eur. J. Biochem. 1979, 95:157-165.
11. Barnickel G., Naumann D., Bradaczek H., Labischinski H., Giesbrecht P. Computer aided molecular modelling of the three-dimensional structure of bacterial peptidoglycan. The Target of Penicillin: The Murein Sacculus of Bacterial Cell Walls 1983, 61-66. de Gruyter, Berlin/New York. R. Hakenbeck, J.-V. Höltje, H. Labischinski (Eds.).
12. Barreteau H., Kova A., Boniface A., Sova M., Gobec S., Blanot D. Cytoplasmic steps of peptidoglycan biosynthesis. FEMS Microbiol. Rev. 2008, 32:168-207.
13. Bavoil P.M., Hsia R., Ojcius D.M. Closing in on Chlamydia and its intracellular bag of tricks. Microbiology 2000, 146:2723-2731.
14. fm, the d-aspartate ligase responsible for the addition of d-aspartic acid onto the peptidoglycan precursor of Enterococcus faecium. J. Biol. Chem. 2006, 281:11586-11594.
15. Bera A., Herbert S., Jakob A., Vollmer W., Götz F. Why are pathogenic staphylococci so lysozyme resistant? The peptidoglycan O-acetyltransferase OatA is the major determinant for lysozyme resistance of Staphylococcus aureus. Mol. Microbiol. 2005, 55:778-787.
16. Biarrotte-Sorin S., Maillard A.P., Delettre J., Sougakoff W., Arthur M., Mayer C. Crystal structures of Weissella viridescens FemX and its complex with UDP-MurNAc-pentapeptide: insights into FemABX family substrates recognition. Structure 2004, 12:257-267.
17. Boneca I.G., Huang Z.H., Gage D.A., Tomasz A. Characterization of Staphylococcus aureus cell wall glycan strands, evidence for a new ?-N-acetylglucosaminidase activity. J. Biol. Chem. 2000, 275:9910-9918.
18. Boneca I.G., Dussurget O., Cabanes D., et al. A critical role for peptidoglycan N-deacetylation in Listeria evasion from the host innate immune system. Proc. Natl. Acad. Sci. USA 2007, 104:997-1002.
19. Bouhss A., Josseaume N., Severin A., et al. Synthesis of the l-alanyl-l-alanine cross-bridge of Enterococcus faecalis peptidoglycan. J. Biol. Chem. 2002, 277:45935-45941.
20. Bouhss A., Trunkfield A.E., Bugg T.D.H., Mengin-Lecreulx D. The biosynthesis of peptidoglycan lipid-linked intermediates. FEMS Microbiol. Rev. 2008, 32:208-233.
21. Boulbitch A., Quinn B., Pink D. Elasticity of the rod-shaped gram-negative eubacteria. Phys. Rev. Lett. 2000, 85:5246-5249.
22. Braun V. Covalent lipoprotein from the outer membrane of Escherichia coli. Biochim. Biophys. Acta 1975, 415:335-377.
23. Brumfitt W., Wardlaw A.C., Park J.T. Development of lysozyme-resistance in Micrococcus lysodiekticus and its association with an increased O-acetyl content of the cell wall. Nature 1958, 181:1783-1784.
24. Chaput C., Labigne A., Boneca I.G. Characterization of Helicobacter pylori lytic transglycosylases Slt and MltD. J. Bacteriol. 2007, 189:422-429.
25. Chopra I., Storey C., Falla T.J., Pearce J.H. Antibiotics, peptidoglycan synthesis and genomics: the chlamydial anomaly revisited. Microbiology 1998, 144:2673-2678.
26. Costa K., Bacher G., Allmaier G., et al. The morphological transition of Helicobacter pylori cells from spiral to coccoid is preceded by a substantial modification of the cell wall. J. Bacteriol. 1999, 181:3710-3715.
27. Crisostomo M.I., Vollmer W., Kharat A.S., et al. Attenuation of penicillin resistance in a peptidoglycan O-acetyl transferase mutant of Streptococcus pneumoniae. Mol. Microbiol. 2006, 61:1497-1509.
28. Demchick P., Koch A.L. The permeability of the wall fabric of Escherichia coli and Bacillus subtilis. J. Bacteriol. 1996, 178:768-773.
29. Dmitriev B.A., Ehlers S., Rietschel E.T. Layered murein revisited: a fundamentally new concept of bacterial cell wall structure, biogenesis and function. Med. Microbiol. Immunol. (Berlin) 1999, 187:173-181.
30. Dmitriev B.A., Toukach F.V., Schaper K.J., Holst O., Rietschel E.T., Ehlers S. Tertiary structure of bacterial murein: the scaffold model. J. Bacteriol. 2003, 185:3458-3468.
31. Dmitriev B.A., Toukach F.V., Holst O., Rietschel E.T., Ehlers S. Tertiary structure of Staphylococcus aureus cell wall murein. J. Bacteriol. 2004, 186:7141-7148.
32. Dramsi S., Davison S., Magnet S., Arthur M. Surface proteins covalently attached to peptidoglycan: examples from both Gram-positive and Gram-negative bacteria. FEMS Microbiol. Rev. 2008, 32:307-320.
33. Draper P., Kandler O., Darbre A. Peptidoglycan and arabinogalactan of Mycobacterium leprae. J. Gen. Microbiol. 1987, 133:1187-1194.
34. Evtushenko L.I., Dorofeeva L.V., Krausova V.I., Gavrish E.Y., Yashina S.G., Takeuchi M. Okibacterium fritillariae gen. nov., sp. nov., a novel genus of the family Microbacteriaceae. Int. J. Syst. Evol. Microbiol. 2002, 52:987-993.
35. Ferain T., Hobbs J.N., Richardson J., et al. Knockout of the two ldh genes has a major impact on peptidoglycan precursor synthesis in Lactobacillus plantarum. J. Bacteriol. 1996, 178:5431-5437.
36. Fiedler F., Draxl R. Biochemical and immunochemical properties of the cell surface of Renibacterium salmoninarum. J. Bacteriol. 1986, 168:799-804.
37. Fiser A., Filipe S.R., Tomasz A. Cell wall branches, penicillin resistance and the secrets of the MurM protein. Trends Microbiol 2003, 11:547-553.
38. Garcia-Bustos J., Tomasz A. A biological price of antibiotic resistance: major changes in the peptidoglycan structure of penicillin-resistant pneumococci. Proc. Natl. Acad. Sci. USA 1990, 87:5415-5419.
39. Garcia-Bustos J.F., Chait B.T., Tomasz A. Altered peptidoglycan structure in a pneumococcal transformant resistant to penicillin. J. Bacteriol. 1988, 170:2143-2147.
40. Ghuysen J.M., Strominger J.L. Structure of the cell wall of Staphylococcus aureus, strain Copenhagen. Ii. Separation and structure of disaccharides. Biochemistry 1963, 2:1119-1125.
41. 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. Bi. Biochemistry 1968, 7:1450-1460.
42. Glauner B. Separation and quantification of muropeptides with high-performance liquid chromatography. Anal. Biochem. 1988, 172:451-464.
43. Glauner B., Höltje J.-V., Schwarz U. The composition of the murein of Escherichia coli. J. Biol. Chem. 1988, 263:10088-10095.
44. Harz H., Burgdorf K., Höltje J.-V. Isolation and separation of the glycan strands from murein of Escherichia coli by reversed-phase high-performance liquid chromatography. Anal. Biochem. 1990, 190:120-128.
45. Hirao T., Sato M., Shirahata A., Kamio Y. Covalent linkage of polyamines to peptidoglycan in Anaerovibrio lipolytica. J. Bacteriol. 2000, 182:1154-1157.
46. Höltje J.-V. Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli. Microbiol. Mol. Biol. Rev. 1998, 62:181-203.
47. Hughes R.C. Autolysis of Bacillus cereus cell walls and isolation of structural components. Biochem. J. 1971, 121:791-802.
48. Kamio Y., Itoh Y., Terawaki Y. Chemical structure of peptidoglycan in Selenomonas ruminantium: cadaverine links covalently to the d-glutamic acid residue of peptidoglycan. J. Bacteriol. 1981, 146:49-53.
49. Kamio Y., Itoh Y., Terawaki Y., Kusano T. Cadaverine is covalently linked to peptidoglycan in Selenomonas ruminantium. J. Bacteriol. 1981, 145:122-128.
50. Koch A.L. Bacterial Growth and Form 1995, Chapman & Hall, New York.
51. Koch A.L. Orientation of the peptidoglycan chains in the sacculus of Escherichia coli. Res. Microbiol. 1998, 149:689-701.
52. Labischinski H., Barnickel G., Naumann D., Keller P. Conformational and topological aspects of the three-dimensional architecture of bacterial peptidoglycan. Ann. Inst. Pasteur Microbiol. 1985, 136A:45-50.
53. Labischinski H., Goodell E.W., Goodell A., Hochberg M.L. Direct proof of a 'more-than-single-layered' peptidoglycan architecture of Escherichia coli W7: a neutron small-angle scattering study. J. Bacteriol. 1991, 173:751-756.
54. Li W.J., Chen H.H., Kim C.J., et al. Microbacterium halotolerans sp. nov., isolated from a saline soil in the west of China. Int. J. Syst. Evol. Microbiol. 2005, 55:67-70.
55. Machida M., Takechi K., Sato H., et al. Genes for the peptidoglycan synthesis pathway are essential for chloroplast division in moss. Proc. Natl. Acad. Sci. USA 2006, 103:6753-6758.
56. Magnet S., Arbeloa A., Mainardi J.L., et al. Specificity of l,d-transpeptidases from Gram-positive bacteria producing different peptidoglycan chemotypes. J. Biol. Chem. 2007, 282:13151-13159.
57. Magnet S., Bellais S., Dubost L., et al. Identification of the l,d-transpeptidases responsible for attachment of the Braun lipoprotein to Escherichia coli peptidoglycan. J. Bacteriol. 2007, 189:3927-3931.
58. Mahapatra S., Scherman H., Brennan P.J., Crick D.C. N-Glycolylation of the nucleotide precursors of peptidoglycan biosynthesis of Mycobacterium spp. is altered by drug treatment. J. Bacteriol. 2005, 187:2341-2347.
59. Mahapatra S., Yagi T., Belisle J.T., et al. Mycobacterial lipid II is composed of a complex mixture of modified muramyl and peptide moieties linked to decaprenyl phosphate. J. Bacteriol. 2005, 187:2747-2757.
60. Mainardi J.L., Legrand R., Arthur M., Schoot B., van Heijenoort J., Gutmann L. Novel mechanism of beta-lactam resistance due to bypass of dd-transpeptidation in Enterococcus faecium. J. Biol. Chem. 2000, 275:16490-16496.
61. Mainardi J.L., Fourgeaud M., Hugonnet J.E., et al. A novel peptidoglycan cross-linking enzyme for a beta-lactam-resistant transpeptidation pathway. J. Biol. Chem. 2005, 280:38146-38152.
62. Markiewicz Z., Glauner B., Schwarz U. Murein structure and lack of dd- and ld-carboxypeptidase activities in Caulobacter crescentus. J. Bacteriol. 1983, 156:649-655.
63. Martin H.H., Gmeiner J. Modification of peptidoglycan structure by penicillin action in cell walls of Proteus mirabilis. Eur. J. Biochem. 1979, 95:487-495.
64. Matsumoto A., Takahashi Y., Shinose M., Seino A., Iwai Y., Omura S. Longispora albida gen. nov., sp. nov., a novel genus of the family Micromonosporaceae. Int. J. Syst. Evol. Microbiol. 2003, 53:1553-1559.
65. Meroueh S.O., Bencze K.Z., Hesek D., et al. Three-dimensional structure of the bacterial cell wall peptidoglycan. Proc. Natl. Acad. Sci. USA 2006, 103:4404-4409.
66. Moulder J.W. Why is Chlamydia sensitive to penicillin in the absence of peptidoglycan?. Infect. Agents Dis. 1993, 2:87-99.
67. Neuhaus F.C., Baddiley J. A continuum of anionic charge: structures and functions of d-alanyl-teichoic acids in Gram-positive bacteria. Microbiol. Mol. Biol. Rev. 2003, 67:686-723.
68. Perkins H.R. The configuration of 2,6-diamino-3-hydroxypimelic acid in microbial cell walls. Biochem. J. 1969, 115:797-805.
69. Pfanzagl B., Zenker A., Pittenauer E., et al. Primary structure of cyanelle peptidoglycan of Cyanophora paradoxa: a prokaryotic cell wall as part of an organelle envelope. J. Bacteriol. 1996, 178:332-339.
70. Pfanzagl B., Allmaier G., Schmid E.R., de Pedro M.A., Loffelhardt W. N-acetylputrescine as a characteristic constituent of cyanelle peptidoglycan in glaucocystophyte algae. J. Bacteriol. 1996, 178:6994-6997.
71. Pisabarro A.G., de Pedro M.A., Vazquez D. Structural modifications in the peptidoglycan of Escherichia coli associated with changes in the state of growth of the culture. J. Bacteriol. 1985, 161:238-242.
72. Pittenauer E., Schmid E.R., Allmaier G., et al. Structural characterization of the cyanelle peptidoglycan of Cyanophora paradoxa by 252Cf plasma desorption mass spectrometry and fast atom bombardment/tandem mass spectrometry. Biol. Mass Spectrom. 1993, 22:524-536.
73. Popham D.L., Helin J., Costello C.E., Setlow P. Muramic lactam in peptidoglycan of Bacillus subtilis spores is required for spore outgrowth but not for spore dehydration or heat resistance. Proc. Natl. Acad. Sci. USA 1996, 93:15405-15410.
74. Quintela J.C., Caparros M., de Pedro M.A. Variability of peptidoglycan structural parameters in Gram-negative bacteria. FEMS Microbiol. Lett. 1995, 125:95-100.
75. Quintela J.C., Pittenauer E., Allmaier G., Aran V., de Pedro M.A. Structure of peptidoglycan from Thermus thermophilus HB8. J. Bacteriol 1995, 177:4947-4962.
76. Quintela J.C., Garcia-del Portillo F., Pittenauer E., Allmaier G., de Pedro M.A. Peptidoglycan fine structure of the radiotolerant bacterium Deinococcus radiodurans Sark. J. Bacteriol. 1999, 181:334-337.
77. Schleifer K.H., Kandler O. Peptidoglycan types of bacterial cell walls and their taxonomic implications. Bacteriol. Rev. 1972, 36:407-477.
78. Schleifer K.H., Plapp R., Kandler O. Identification of threo-3-hydroxyglutamic acid in the cell wall of Microbacterium lacticum. Biochem. Biophys. Res. Commun. 1967, 28:566-570.
79. Schneider T., Senn M.M., Berger-Bachi B., Tossi A., Sahl H.G., Wiedemann I. In vitro assembly of a complete, pentaglycine interpeptide bridge containing cell wall precursor (lipid II-Gly5) of Staphylococcus aureus. Mol. Microbiol. 2004, 53:675-685.
80. Shockman G.D., Thompson J.S., Conover M.J. Replacement of lysine by hydroxylysine and its effects on cell lysis in Streptococcus faecalis. J. Bacteriol. 1965, 90:575-588.
81. Sutcliffe I.C. Cell envelope composition and organisation in the genus Rhodococcus. Antonie van Leeuwenhoek 1998, 74:49-58.
82. Tipper D.J., Strominger J.L., Ensign J.C. Structure of the cell wall of Staphylococcus aureus, strain Copenhagen. VII. Mode of action of the bacteriolytic peptidase from Myxobacter and the isolation of intact cell wall polysaccharides. Biochemistry 1967, 6:906-920.
83. Ton-That H., Marraffini L.A., Schneewind O. Protein sorting to the cell wall envelope of Gram-positive bacteria. Biochim. Biophys. Acta 2004, 1694:269-278.
84. Tuomanen E., Schwartz J., Sande S., Light K., Gage D. Unusual composition of peptidoglycan in Bordetella pertussis. J. Biol. Chem. 1989, 264:11093-11098.
85. Uchida E., Aida K. Taxonomic significance of cell-wall acyl type in Corynebacterium-Mycobacterium-Nocardia group by a glycolate test. J. Gen. Appl. Microbiol. 1979, 25:169-183.
86. van den Bogaart G., Hermans N., Krasnikov V., Poolman B. Protein mobility and diffusive barriers in Escherichia coli: consequences of osmotic stress. Mol. Microbiol. 2007, 64:858-871.
87. Vollmer W. Structural variation in the glycan strands of bacterial peptidoglycan. FEMS Microbiol. Rev. 2008, 32:287-306.
88. Vollmer W., Höltje J.-V. The architecture of the murein (peptidoglycan) in Gram-negative bacteria: Vertical scaffold or horizontal layer(s)?. J. Bacteriol. 2004, 186:5978-5987.
89. Vollmer W., Tomasz A. The pgdA gene encodes for a peptidoglycan N-acetylglucosamine deacetylase in Streptococcus pneumoniae. J. Biol. Chem. 2000, 275:20496-20501.
90. Vollmer W., Tomasz A. Peptidoglycan N-acetylglucosamine deacetylase, a putative virulence factor in Streptococcus pneumoniae. Infect. Immun. 2002, 70:7176-7178.
91. Vollmer W., Blanot D., de Pedro M.A. Peptidoglycan structure and architecture. FEMS Microbiol. Rev. 2008, 32:149-167.
92. Vollmer W., Joris B., Charlier P., Foster S. Bacterial peptidoglycan (murein) hydrolases. FEMS Microbiol. Rev. 2008, 32:259-286.
93. Ward J.B. The chain length of the glycans in bacterial cell walls. Biochem. J. 1973, 133:395-398.
94. Warth A.D., Strominger J.L. Structure of the peptidoglycan from vegetative cell walls of Bacillus subtilis. Biochemistry 1971, 10:4349-4358.
95. Weadge J.T., Clarke A.J. Identification and characterization of O-acetylpeptidoglycan esterase: a novel enzyme discovered in Neisseria gonorrhoeae. Biochemistry 2006, 45:839-851.
96. Weidel W., Pelzer H. Bagshaped macromolecules - a new outlook on bacterial cell walls. Adv. Enzymol. 1964, 26:193-232.
97. Wietzerbin J., Das B.C., Petit J.F., Lederer E., Leyh-Bouille M., Ghuysen J.M. Occurrence of d-alanyl-(d)-meso-diaminopimelic acid and meso-diaminopimelyl-meso-diaminopimelic acid interpeptide linkages in the peptidoglycan of mycobacteria. Biochemistry 1974, 13:3471-3476.
98. Yao X., Jericho M., Pink D., Beveridge T. Thickness and elasticity of Gram-negative murein sacculi measured by atomic force microscopy. J. Bacteriol. 1999, 181:6865-6875.