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Taxonomic group: bacteria / Firmicutes (Phylum: Firmicutes)
Associated disease: infection due to Bacillus subtilis [ICD11: XM4SG9

]

NCBI PubMed ID: 8892816
Publication DOI: 10.1128/jb.178.21.6173-6183.1996
Journal NLM ID: 2985120R
Publisher: American Society for Microbiology
Correspondence: s.foster

sheffield.ac.uk
Institutions: Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, S10 2TN, United Kingdom, Institute for Analytical Chemistry, University of Vienna, A-1090 Vienna, Austria

The structure of the endospore cell wall peptidoglycan of Bacillus subtilis has been examined. Spore peptidoglycan was produced by the development of a method based on chemical permeabilization of the spore coats and enzymatic hydrolysis of the peptidoglycan. The resulting muropeptides which were >97% pure were analyzed by reverse-phase high-performance liquid chromatography, amino acid analysis, and mass spectrometry. This revealed that 49% of the muramic acid residues in the glycan backbone were present in the δ-lactam form which occurred predominantly every second muramic acid. The glycosidic bonds adjacent to the muramic acid δ-lactam residues were resistant to the action of muramidases. Of the muramic acid residues, 25.7 and 23.3% were substituted with a tetrapeptide and a single L-alanine, respectively. Only 2% of the muramic acids had tripeptide side chains and may constitute the primordial cell wall, the remainder of the peptidoglycan being spore cortex. The spore peptidoglycan is very loosely cross-linked at only 2.9% of the muramic acid residues, a figure approximately 11-fold less than that of the vegetative cell wall. The peptidoglycan from strain AA110 (dacB) had fivefold-greater cross-linking (14.4%) than the wild type and an altered ratio of muramic acid substituents having 37.0, 46.3, and 12.3% δ-lactam, tetrapeptide, and single L-alanine, respectively. This suggests a role for the DacB protein (penicillin-binding protein 5*) in cortex biosynthesis. The sporulationspecific putative peptidoglycan hydrolase CwlD plays a pivotal role in the establishment of the mature spore cortex structure since strain AA107 (cwlD) has spore peptidoglycan which is completely devoid of muramic acid δ-lactam residues. Despite this drastic change in peptidoglycan structure, the spores are still stable but are unable to germinate. The role of δ-lactam and other spore peptidoglycan structural features in the maintenance of dormancy, heat resistance, and germination is discussed.

role, structural, analysis, structural analysis, peptidoglycan, Bacillus, Bacillus subtilis, differentiation

Structure type: polymer chemical repeating unit ; 1803.5 [M-H]+
Location inside paper: Fig. 2, compound Y
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_1635957,IEDB_241115,IEDB_423183,IEDB_885814

Methods: enzymatic hydrolysis, amino acid analysis, MALDI-TOF MS, HPLC, chemical extraction of dormant spores, physical disruption of spores, chemical extraction of integuments, FDNB determination of peptidoglycan cross-linking
Biological activity: biological data
Comments, role: unsubstituted MurNAc is in the form of δ-lactam

Related record ID(s): 59, 237, 238, 239, 240, 241, 242, 243, 244, 245, 246, 247, 248, 249, 250, 251
NCBI Taxonomy refs (TaxIDs): 1423
Show glycosyltransferases

There are too many chemically distinct structures (~82944), so only one is shown:

-4)[Ac(1-2)]bDGlcpN(1-4)bXMurp(1-4)[Ac(1-2)]bDGlcpN(1-4)[xDAla?(1-2)xXmPmN2?(1-2)xDGlu?(1-2)xLAla?(1-2)[xDAla?(1-6)]xXmPmN2?(1-2)xDGlu?(1-1)xLAla?(2-8),Ac(1-2)]bXMurp(1-

*O[C@H]1[C@H](O)[C@@H](NC(C)=O)[C@H](O[C@H]2[C@H](O[C@H](C)C(=O)O)[C@@H](N)[C@H](O[C@H]3[C@H](O)[C@@H](NC(C)=O)[C@H](O[C@H]4[C@H](O[C@H](C)C(=O)N[C@@H](C)C(=O)OC(=O)[C@@H](CCC(=O)O)NC(=O)[C@H](CCC[C@@H](NC(=O)[C@@H](C)N)C(=O)O)NC(=O)[C@H](C)NC(=O)[C@@H](CCC(=O)O)NC(=O)[C@H](CCC[C@@H](N)C(=O)O)NC(=O)[C@@H](C)N)[C@@H](NC(C)=O)[C@H](*)O[C@@H]4CO)O[C@@H]3CO)O[C@@H]2CO)O[C@@H]1CO

SVG MW SMILES 3D mol Ionize