Modification of Peptidoglycan Structure by Penicillin Action in Cell Walls of <i>Proteus mirabilis</i>

Martin, Hans Herbert; Gmeiner, Jobst

doi:10.1111/j.1432-1033.1979.tb12988.x

Cited by 68 publications

(57 citation statements)

References 28 publications

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“…The mass fractions v) found for each oligomer permitted the calculation of the cross-linking index CI for each peptidoglycan by using an expanded version of the theoretical equation of Martin and Gmeiner [19], viz:…”

Section: Fractionation Of Muramidase-digested Non-teichoic-acid-linkementioning

confidence: 99%

Peptidoglycan cross‐linking in Staphylococcus aureus

Snowden¹,

Perkins

1990

European Journal of Biochemistry

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The peptidoglycan of Staphylococcus aureus contains relatively short glycan chains and is highly cross-linked via its peptide chains. The material from wild-type (strain H) and mutants H28, H4B and MR-1 was freed from the teichoic-acid-linked component and then hydrolysed by Chalaropsis muramidase to yield disacchariderepeating units of the glycan with attached peptides either non-cross-linked (monomer) or joined to similar units by one (dimer), two (trimer) or more (oligomer) peptide cross links. The resulting fragments were separated by high-resolution HPLC so that distinguishable components as large as nonamer could be identified. Extrapolation showed that, in S. aureus H, H28 and MR-1, oligomers at least as large as eicosamer formed part of the smooth distribution of oligomer fragments, whereas in strain H4B (PBP4-) the maximum size was around dodecamer. The oligomer distribution profile was related to the polymerization theories of Flory, which allow a distinction to be made between a monomer addition model, whereby each oligomer can only be synthesized by the addition of a single monomer unit to its next lower homologue, and a random addition model, in which an oligomer can be formed by linkage of any combination of its constituent smaller units. In S. aureus close approximation to the random addition model for oligomer synthesis and hence for peptidoglycan cross-linking was observed, both in PBP4' and PBP4-mutants. The implications for secondary cross-linking in S. aureus cell wall formation are inescapable, although the possibility of an endopeptidase/transpeptidase providing later modification of the peptidoglycan is not completely ruled out.Peptidoglycan (murein) is the major structural and stressbearing polymer of the cell walls of most prokaryotes [l]. It is composed of glycan chains of repeating N-acetylglucosaminyl-P-(I -4)-N-acetylmuramic acid (disaccharide) units substituted at the muramic acid carboxyl group with short, specific peptides [I]. The peptidoglycan network (murein sacculus [2]) is formed by the cross-linking of adjacent glycan chains via peptide linkages between the initial primary chains attached to the muramic acid. In Staphylococcus aureus the primary peptide chain has the sequence L-Ala-D-Glu(L-Lys-DAla-D-Ala) and before polymerisation of the glycan chain the &-amino group of L-lysine becomes substituted with a glycine pentapeptide [3]. Cross-links are then formed by a transpeptidase reaction, in which a terminal malanine is lost from one primary chain and the sub-terminal D-alanine becomes linked to the free amino group of a pentaglycine bridge [4]. The degree of cross-linking (CI), i.e. the number of such links achieved in practice divided by the total number possible, often expressed as a percentage (100 CI), varies greatly among bacterial species; thus in Escherichia coli and Neisseria gonorrhoeae the value is 30-40%, whereas in S. aureus it is exceptionally high at about 70-80% [4]. A value of 75% corresponds to an average degree of peptide polymerisation (Xn) of 4, since 2,...

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Section: Fractionation Of Muramidase-digested Non-teichoic-acid-linkementioning

confidence: 99%

Peptidoglycan cross‐linking in Staphylococcus aureus

Snowden¹,

Perkins

1990

European Journal of Biochemistry

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“…Baselines for all peaks were then adjusted manually. The percentage of cross-linking was calculated as previously described (Martin & Gmeiner, 1979;Glauner, 1988), except for the cell cycle analysis in which only the peak areas of significant peaks -tri, tetra, tetra-tetra, tetra-tri and tetra-tetra-tetra -were used.…”

Section: Preparation Of Labelled Peptidoglycan Fragments For Hplc Anamentioning

confidence: 99%

Peptidoglycan synthesis in Salmonella typhimurium 2616

Gally¹,

Cooper

1993

Journal of General Microbiology

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HPLC analysis of peptidoglycan synthesis in Salmonella typhimurium strain 2616 has revealed that : (i) there is observable variation in the composition, but no signifkant variation in the overall degree of cross-linking, of newly synthesized peptidoglycan during the division cycle; (ii) the types of muropeptide that constitute peptidoglycan do not vary over a wide range of growth rates; and (iii) the composition and maturation kinetics of S. typhimurium peptidoglycan are, as expected, similar to those of Escherichia coli. We propose a unitary model of peptidoglycan synthesis, with single-strand incorporation occurring at both side wall and polar sites.

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“…The extent of cross-linking (33%) is typical of most Gram-negative bacteria [l]. Thus, the peptidoglycan of P. mirabilis is characteristic of the Enterobacteriaceae but for one notable and significant difference, the presence of extensive 0-acetylation [2]. Peptidoglycan 0-acetylation occurs at the 6-hydroxyl group of MurNAc residues producing the corresponding N,O-diacetylmuramyl derivatives, and this modification confers resistance to the hydrolytic action of many muramidases, including hen egg-white lysozyme (HEWL) and human lysozymes [3 -61.…”

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confidence: 99%

Dependence of lysozyme‐catalysed solubilization of Proteus mirabilis peptidoglycan on the extent of O‐acetylation

Dupont

Clarke

1991

European Journal of Biochemistry

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The degree of peptidoglycan 0-acetylation in 14 strains of Proteus mirabilis has been accurately determined by a procedure which employs the quantitation of mild-base-released acetic acid by HPLC, and the estimation of peptidoglycan concentration by cation-exchange amino acid analysis. The /3-~-N,6-O-diacetylmuramyl content of all isolated and purified peptidoglycans was ranged 20-52.8%, relative to the total muramic acid concentration. Each of the 0-acetylated peptidoglycans was found to be resistant to solubilization by both human and hen eggwhite lysozymes and for hen egg-white lysozyme, the extent of this resistance was dependent upon the degree of 0-acetylation. The steady-state parameters, K, and V, for the hen-egg-white-lysozyme-catalysed solubilization of various peptidoglycan preparations were determined at pH 6.61 and 25°C. Values of K , for the different peptidoglycan samples were found to increase with increasing 0-acetylation, whereas with V no such relationship appeared to exist. An increase in the overall change in the standard Gibbs free energy of activation [d(dG*)], a consequence of increasing 0-acetylation, was observed, and is shown to result from the weaker affinity of the enzyme for the modified substrates.Peptidoglycan is a heteropolymer of distinct composition and structure, associated uniquely with eubacterial cell walls. Proteus mirabilis peptidoglycan is comprised of equimolar amounts of GlcNAc, N-acetylmuramic acid (MurNAc), Lalanine, D-glutamic acid, L-meso-diaminopimelic acid and Dalanine. The cross-linking of neighbouring peptides is direct (chemotype Aly) and involves the meso-diaminopimelic acid and D-alanyl residues. The extent of cross-linking (33%) is typical of most Gram-negative bacteria [l]. Thus, the peptidoglycan of P. mirabilis is characteristic of the Enterobacteriaceae but for one notable and significant difference, the presence of extensive 0-acetylation [2]. Peptidoglycan 0-acetylation occurs at the 6-hydroxyl group of MurNAc residues producing the corresponding N,O-diacetylmuramyl derivatives, and this modification confers resistance to the hydrolytic action of many muramidases, including hen egg-white lysozyme (HEWL) and human lysozymes [3 -61.The phenomenon of peptidoglycan 0-acetylation was first observed independently by two different groups of researchers over 30 years ago [7, 81, and its role in conferring lysozyme resistance was demonstrated soon after [6]. Since then, 0-acetylation of peptidoglycan has been observed in a diverse group of bacteria which includes some important pathogens, both Gram positive (e.g. Staphylococcus aureus [9, 101) and Gram negative (e. g. Neisseria gonorrhoeae [3] and P. mirabilis strains of N . gonorrhoeae and characterized by 34-52% 0-acetylation, was shown to be resistant to hydrolysis by HEWL to the extent of 34-59% [12]. On the other hand, O-acetyldeficient peptidoglycan, isolated from N . gonorrhoea RD5 was completely solubilized and degraded to low-molecular-mass fragments. In the study, resistance was defined as the percen...

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Modification of Peptidoglycan Structure by Penicillin Action in Cell Walls of Proteus mirabilis

Cited by 68 publications

References 28 publications

Peptidoglycan cross‐linking in Staphylococcus aureus

Peptidoglycan cross‐linking in Staphylococcus aureus

Peptidoglycan synthesis in Salmonella typhimurium 2616

Dependence of lysozyme‐catalysed solubilization of Proteus mirabilis peptidoglycan on the extent of O‐acetylation

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