Taxonomic group: bacteria / Firmicutes
(Phylum: Firmicutes)
Associated disease: infection due to Bacillus subtilis [ICD11:
XM4SG9 
]
NCBI PubMed ID: 8986824Publication DOI: 10.1073/pnas.93.26.15405Journal NLM ID: 7505876Publisher: National Academy of Sciences
Institutions: Department of Biochemistry, University of Connecticut Health Center, Farmington 06030-3305, USA, Mass Spectrometry Resource, Department of Biophysics, Boston University School of Medicine, 80 East Concord Street, R-806, Boston, MA 02118-2394
Bacterial endospores derive much of their longevity and resistance properties from the relative dehydration of their protoplasts. The spore cortex, a peptidoglycan structure surrounding the protoplasm, maintains, and is postulated to have a role in attaining, protoplast dehydration. A structural modification unique to the spore cortex is the removal of all or part of the peptide side chains from the majority of the muramic acid residues and the conversion of 50% of the muramic acid to muramic lactam. A mutation in the cwlD gene of Bacillus subtilis, predicted to encode a muramoyl-L-alanine amidase, results in the production of spores containing no muramic lactam. These spores have normally dehydrated protoplasts but are unable to complete the germination/ outgrowth process to produce viable cells. Addition of germinants resulted in the triggering of germination with loss of spore refractility and the release of dipicolinic acid but no degradation of cortex peptidoglycan. Germination in the presence of lysozyme allowed the cwlD spores to produce viable cells and showed that they have normal heat resistance properties. These results (i) suggest that a mechanical activity of the cortex peptidoglycan is not required for the generation of protoplast dehydration but rather that it simply serves as a static structure to maintain dehydration, (ii) demonstrate that degradation of cortex peptidoglycan is not required for spore solute release or partial spore core rehydration during germination, (iii) indicate that muramic lactam is a major specificity determinant of germination lytic enzymes, and (iv) suggest the mechanism by which the spore cortex is degraded during germination while the germ cell wall is left intact.
Bacillus subtilis, spore peptidoglycan
Structure type: oligomer
Trivial name: spore peptidoglycan
Compound class: peptidoglycan
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_1635957,IEDB_423183,IEDB_885814
Methods: amino acid analysis, MALDI-TOF MS, HPLC, electron microscopy, spore production, spore germination, amino sugar analysis, muramidase digestion
NCBI Taxonomy refs (TaxIDs): 1423
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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