Release of cell wall peptides into culture medium by exponentially growing Escherichia coli

Goodell, E. W.; Schwarz, Uli

doi:10.1128/jb.162.1.391-397.1985

Cited by 169 publications

(93 citation statements)

References 29 publications

(36 reference statements)

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“…This indicates that the AmpG and AmpD proteins are both required for its accumulation. Because of its apparent molecular weight, peak (D) was provisionally identified as the tripeptide which Goodell and Schwarz (1985) had characterized. Goodell and Higgins (1987) have shown that tripeptide could be efficiently taken up by oligopeptide permease (Opp).…”

Section: Resultsmentioning

confidence: 99%

“…Bonds are broken to allow insertion of new glycan chains during enlargement of the cell and to effect separation of daughter cells. In addition, Escherichia coli, and presumably most other Gram-negative bacteria, recycles components from 40-50% of its murein sacculus each generation (Goodell, 1985;Goodell and Schwarz, 1985;Park, 1993). The studies by Goodell strongly suggest that as peptidoglycan is degraded in the periplasm, the murein tripeptide, L-Ala-D-Glu-DAP, derived therefrom is transported into the cytoplasm.…”

Section: Introductionmentioning

confidence: 99%

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Bacterial cell wall recycling provides cytosolic muropeptides as effectors for beta-lactamase induction.

et al. 1994

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A mechanism for bacteria to monitor the status of their vital cell wall peptidoglycan is suggested by the convergence of two phenomena: peptidoglycan recycling and beta‐lactamase induction. ampG and ampD, genes essential for beta‐lactamase regulation, are here shown to be required for recycling as well. Cells lacking either AmpG or AmpD lose up to 40% of their peptidoglycan per generation, whereas Escherichia coli normally suffers minimal losses and instead recycles 40 or 50% of the tripeptide, L‐alanyl‐D‐glutamyl‐meso‐diaminopimelic acid, from its peptidoglycan each generation. The ampG mutant releases peptidoglycan‐derived material into the medium. In contrast, the ampD mutant accumulates a novel cell wall muropeptide, 1,6‐anhydro N‐acetylmuramyl‐L‐alanyl‐D‐glutamyl‐meso‐diaminopimelic acid (anhMurNAc‐tripeptide), in its cytoplasm. This work suggests that AmpG is the permease for a large muropeptide and AmpD is a novel cytosolic N‐acetylmuramyl‐L‐alanine amidase that cleaves anhMurNAc‐tripeptide to release tripeptide, which is then recycled. These results also suggest that the phenomenon of beta‐lactamase induction is regulated by the level of muropeptide(s) in the cytoplasm, since an ampD mutation that results in beta‐lactamase expression even in the absence of a beta‐lactamase inducer coincides with accumulation of anhMurNAc‐tripeptide. The transcriptional regulator AmpR is presumably converted into an activator for beta‐lactamase production by sensing the higher level of muropeptide(s). This may be an example of a general mechanism for signaling the progress of external events such as cell wall maturation, cell division or cell wall damage.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Bacterial cell wall recycling provides cytosolic muropeptides as effectors for beta-lactamase induction.

et al. 1994

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“…In this study we analysed the contribution of PGN sensing to the overall cellular response to Shigella infection. First, we investigated whether Shigella releases PGN fragments during PGN remodelling as originally shown for E. coli (Goodell and Schwarz, 1985) and for two human pathogens, Bordetella pertussis (Goldman et al, 1982;Cookson et al, 1989) and Neisseria gonorrhoeae (Sinha and Rosenthal, 1980). Then, we evaluated whether and how the PGN derivatives shed by Shigella could stimulate the innate immune response.…”

Section: Discussionmentioning

confidence: 99%

Muramylpeptide shedding modulates cell sensing of Shigella flexneri

et al. 2008

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SummaryBacterial infections trigger the activation of innate immunity through the interaction of pathogenassociated molecular patterns (PAMPs) with pattern recognition molecules (PRMs). The nucleotidebinding oligomerization domain (Nod) proteins are intracellular PRMs that recognize muramylpeptides contained in peptidoglycan (PGN) of bacteria. It is still unclear how Nod1 physically interacts with PGN, a structure internal to the Gram-negative bacterial envelope. To contribute to the understanding of this process, we demonstrate that, like Escherichia coli, Bordetella pertussis and Neisseria gonorrheae, the Gram-negative pathogen Shigella spontaneously releases PGN fragments and that this process can be increased by inactivating either ampG or mppA, genes involved in PGN recycling. Both Shigella mutants, but especially the strain carrying the mppA deletion, trigger Nod1-mediated NF-kB activation to a greater extent than the wild-type strain. Likewise, muramylpeptides spontaneously shed by Shigella are able per se to trigger a Nod1-mediated response consistent with the relative amount. Finally, we found that qualitative changes in muramylpeptide shedding can alter in vivo host responses to Shigella infection. Our findings support the idea that muramylpeptides released by pathogens during infection could modulate the immune response through Nod proteins and thereby influence the outcome of disease.

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“…This cell wall turnover phenomenon was discovered in the early 1960s byŘíhová L. and coworkers, and the activity of cell wall degradation has since been discovered in a variety of Gram-positive and Gram-negative bacteria, including E. coli (Chaloupka, Křečková,Řfhová, 1962;Chaloupka et al, 2008;Doyle, Chaloupka, & Vinter, 1988;Park & Uehara, 2008). Using radiolabeled PG from E. coli, Goodell and Schwarz calculated the percentage of PG that is lost during each generation and identified intermediate molecules from the cell medium (Goodell, 1985;Goodell & Schwarz, 1985). These findings led to the theory that bacterial PG fragments are recycled during cell growth and division.…”

Section: Background Informationmentioning

confidence: 99%

Metabolic Incorporation of N‐Acetyl Muramic Acid Probes into Bacterial Peptidoglycan

DeMeester

Liang

Zhou

et al. 2019

CP Chemical Biology

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Bacterial cells utilize small carbohydrate building blocks to construct peptidoglycan (PG), a highly conserved mesh‐like polymer that serves as a protective coat for the cell. PG production has long been a target for antibiotics, and its breakdown is a source for human immune recognition. A key component of bacterial PG, N‐acetyl muramic acid (NAM), is a vital element in many synthetically derived immunostimulatory compounds. However, the exact molecular details of these structures and how they are generated remain unknown due to a lack of chemical probes surrounding the NAM core. A robust synthetic strategy to generate bioorthogonally tagged NAM carbohydrate units is implemented. These molecules serve as precursors for PG biosynthesis and recycling. Escherichia coli cells are metabolically engineered to incorporate the bioorthogonal NAM probes into their PG network. The probes are subsequently modified using copper‐catalyzed azide‐alkyne cycloaddition to install fluorophores directly into the bacterial PG, as confirmed by super‐resolution microscopy and high‐resolution mass spectrometry. Here, synthetic notes for key elements of this process to generate the sugar probes as well as streamlined user‐friendly metabolic labeling strategies for both microbiology and immunological applications are described. © 2019 by John Wiley & Sons, Inc. Basic Protocol 1: Synthesis of peracetylated 2‐azido glucosamine Basic Protocol 2: Synthesis of 2‐azido and 2‐alkyne NAM Basic Protocol 3: Synthesis of 3‐azido NAM methyl ester Basic Protocol 4: Incorporation of NAM probes into bacterial peptidoglycan Basic Protocol 5: Confirmation of bacterial cell wall remodeling by mass spectrometry

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Release of cell wall peptides into culture medium by exponentially growing Escherichia coli

Cited by 169 publications

References 29 publications

Bacterial cell wall recycling provides cytosolic muropeptides as effectors for beta-lactamase induction.

Bacterial cell wall recycling provides cytosolic muropeptides as effectors for beta-lactamase induction.

Muramylpeptide shedding modulates cell sensing of Shigella flexneri

Metabolic Incorporation of N‐Acetyl Muramic Acid Probes into Bacterial Peptidoglycan

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