Peptidoglycan synthesis in Salmonella typhimurium 2616

Gally, David L.; Cooper, Stephen

doi:10.1099/00221287-139-7-1469

Cited by 8 publications

(9 citation statements)

References 37 publications

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“…The S. typhimurium peptidoglycan structure was shown consistently to be similar to that described for Escherichia coli (Pisabarro et al, 1985;Glauner et al, 1988;Gally and Cooper, 1993). However, in our study we used the highly virulent strain S. typhimurium SL1344, and specific growth conditions, such as non-shaking static growth, to render bacteria competent to infect cultured mammalian cells (Lee and Falkow, 1990).…”

Section: Resultssupporting

confidence: 52%

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Peptidoglycan structure of Salmonella typhimurium growing within cultured mammalian cells

Zöllner

et al. 1997

Molecular Microbiology

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SummaryThe cell wall structure of Salmonella typhimurium has been studied for the first time during transit from freeliving to parasitic lifestyles. Peptidoglycan of S. typhimurium proliferating within human epithelial cells contains a high proportion of previously unidentified muropeptides (5-10-fold higher than in extracellular bacteria). Amino acid and mass-spectrometry analyses showed that these new components consist of

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Section: Resultssupporting

confidence: 52%

“…Muropeptide composition of S. typhimurium peptidoglycan has been previously reported only for non-virulent laboratory strains (Gally and Cooper, 1993). The S. typhimurium peptidoglycan structure was shown consistently to be similar to that described for Escherichia coli (Pisabarro et al, 1985;Glauner et al, 1988;Gally and Cooper, 1993).…”

Section: Resultsmentioning

confidence: 78%

Peptidoglycan structure of Salmonella typhimurium growing within cultured mammalian cells

Zöllner

et al. 1997

Molecular Microbiology

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“…Cellosyl is a muramidase produced by Streptomyces coelicolor which is able to efficiently hydrolyze bacterial peptidoglycan (19). Electron microscopy of Cellosyl-hydrolyzed, permeabilized spores revealed that the cortex and primordial cell wall layers had disappeared but that vestigial coat layers and insoluble core material remained (data not shown).…”

Section: Resultsmentioning

confidence: 99%

Structural analysis of Bacillus subtilis 168 endospore peptidoglycan and its role during differentiation

et al. 1996

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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 ␦-lactam form which occurred predominantly every second muramic acid. The glycosidic bonds adjacent to the muramic acid ␦-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% ␦-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 ␦-lactam residues. Despite this drastic change in peptidoglycan structure, the spores are still stable but are unable to germinate. The role of ␦-lactam and other spore peptidoglycan structural features in the maintenance of dormancy, heat resistance, and germination is discussed. Dormant bacterial endospores formed by the genera Bacillus and Clostridium are the most resistant living structures known and are able to survive thousands if not millions of years (9). During the quiescent state, spores exhibit high-level resistance to many treatments, including heat, UV light, desiccation, and the action of deleterious chemicals. As a result of their resistance properties, spores are able to survive many food preservation and pasteurization procedures and thus cause huge problems to the food industry (11).Endospores are characterized by a relatively dehydrated protoplast encased in integument layers (20). The most prominent of the integuments are the spore coat layers which determine the physical properties of the spore surface and are responsible for resistance to enzymatic assault (56). However, the spore coats are not involved in the maintenance of dormancy and heat resistance (56). Between the spore coats and the protoplast membrane is a thick layer of bacterial peptidoglycan, consisting of two sublayers. Innermost is the ...

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“…The envelope structure is similar in S. enterica and E. coli (Glauner et al ., ; Gally and Cooper, ). A major component is the peptidoglycan sacculus (PG, also called murein), which is located in the periplasmic space and provides both mechanical strength and cell shape (Vollmer et al ., ; Page, ).…”

Section: Introductionmentioning

confidence: 99%