Bacterial Cell Wall: Morphology and Biochemistry

Benedetti, Stefania De; Fisher, Jed F.; Mobashery, Shahriar

doi:10.1201/9781003099277-20

Cited by 9 publications

(9 citation statements)

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“…We first sought to understand the role that host HTGs may play in Buchnera PGN metabolism by characterizing Buchnera ’s cell wall. Cell wall PGN is comprised of repeating units of β-1,4-linked N- acetylglucosamine (GlcNAc) and N -acetylmuramic acid (MurNAc) disaccharide with a short stem peptide attached to the MurNAc lactyl moiety via amide bond ( 33 ). In Gram-negative bacteria, the stem peptide typically consists of five amino acids: l -Ala, γ- d -glutamate, meso -diaminopimelic acid ( m Dap), d -Ala, and d -Ala (pentapeptide).…”

Section: Resultsmentioning

confidence: 99%

“…In Gram-negative bacteria, the stem peptide typically consists of five amino acids: l -Ala, γ- d -glutamate, meso -diaminopimelic acid ( m Dap), d -Ala, and d -Ala (pentapeptide). Synthesis of PGN, the major constituent of the cell wall (also called murein), begins in the cytoplasm with the multistep construction of lipid II and transitions to the periplasm where the cell wall, or murein sacculus, is assembled from lipid II by a series of additional enzymes ( 33 ). Cell wall remodeling is necessary for bacterial growth and division, for antibiotic resistance, for repair of the cell wall, and for the insertion of outer membrane proteins ( 34 , 35 ).…”

Section: Resultsmentioning

confidence: 99%

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Horizontal-Acquisition of a Promiscuous Peptidoglycan-Recycling Enzyme Enables Aphids To Influence Symbiont Cell Wall Metabolism

Smith

Lee

Person

et al. 2021

mBio

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Horizontal-Acquisition of a Promiscuous Peptidoglycan-Recycling Enzyme Enables Aphids To Influence Symbiont Cell Wall Metabolism

Smith

Lee

Person

et al. 2021

mBio

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“…The second modification of Lipid II in S. aureus is the presence of a pentaglycine bridge peptide attached to the ε-amine of the l -lysine of the stem peptide . Peptide bridge extensions to the l -lysine of the stem are commonly encountered in Gram-positive bacteria, with different bacteria using different short oligopeptide sequences for their bridge. , Cytoplasmic modification of Lipid II to install the Gly 5 bridge is accomplished by the FemXAB enzyme family: FemX adds the first glycine; FemA the second glycine; and FemB the third, fourth, and fifth glycines. , For all three enzymes the glycyl donor is Gly-tRNA gly . , The Fem designation to these enzymes (and to their genes) has significance: F actors e nhancing m ethicillin (β-lactam) resistance . FemX, the first enzyme in bridge peptide elongation, is an essential enzyme .…”

Section: Gram-positive Cell Envelopementioning

confidence: 99%

β-Lactams against the Fortress of the Gram-Positive Staphylococcus aureus Bacterium

Fisher

Mobashery

2020

Chem. Rev.

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The biological diversity of the unicellular bacteriawhether assessed by shape, food, metabolism, or ecological nichesurely rivals (if not exceeds) that of the multicellular eukaryotes. The relationship between bacteria whose ecological niche is the eukaryote, and the eukaryote, is often symbiosis or stasis. Some bacteria, however, seek advantage in this relationship. One of the most successfulto the disadvantage of the eukaryoteis the small (less than 1 μm diameter) and nearly spherical Staphylococcus aureus bacterium. For decades, successful clinical control of its infection has been accomplished using β-lactam antibiotics such as the penicillins and the cephalosporins. Over these same decades S. aureus has perfected resistance mechanisms against these antibiotics, which are then countered by new generations of β-lactam structure. This review addresses the current breadth of biochemical and microbiological efforts to preserve the future of the β-lactam antibiotics through a better understanding of how S. aureus protects the enzyme targets of the β-lactams, the penicillin-binding proteins. The penicillin-binding proteins are essential enzyme catalysts for the biosynthesis of the cell wall, and understanding how this cell wall is integrated into the protective cell envelope of the bacterium may identify new antibacterials and new adjuvants that preserve the efficacy of the β-lactams.

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“…All of these β-lactams are enzyme inhibitors. Most pathogenic bacteria contain a cell wall that is made biosynthetically from glycan strands, which have peptide stems on their alternate saccharides [ 22 ]. In the final stage of cell-wall biosynthesis, these stems are cross-linked so as to conjoin adjacent glycan strands.…”

Section: Introductionmentioning

confidence: 99%

β-Lactams from the Ocean

Fisher

Mobashery

2023

Marine Drugs

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The title of this essay is as much a question as it is a statement. The discovery of the β-lactam antibiotics—including penicillins, cephalosporins, and carbapenems—as largely (if not exclusively) secondary metabolites of terrestrial fungi and bacteria, transformed modern medicine. The antibiotic β-lactams inactivate essential enzymes of bacterial cell-wall biosynthesis. Moreover, the ability of the β-lactams to function as enzyme inhibitors is of such great medical value, that inhibitors of the enzymes which degrade hydrolytically the β-lactams, the β-lactamases, have equal value. Given this privileged status for the β-lactam ring, it is therefore a disappointment that the exemplification of this ring in marine secondary metabolites is sparse. It may be that biologically active marine β-lactams are there, and simply have yet to be encountered. In this report, we posit a second explanation: that the value of the β-lactam to secure an ecological advantage in the marine environment might be compromised by its close structural similarity to the β-lactones of quorum sensing. The steric and reactivity similarities between the β-lactams and the β-lactones represent an outside-of-the-box opportunity for correlating new structures and new enzyme targets for the discovery of compelling biological activities.

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Bacterial Cell Wall: Morphology and Biochemistry

Cited by 9 publications

References 1 publication

Horizontal-Acquisition of a Promiscuous Peptidoglycan-Recycling Enzyme Enables Aphids To Influence Symbiont Cell Wall Metabolism

Horizontal-Acquisition of a Promiscuous Peptidoglycan-Recycling Enzyme Enables Aphids To Influence Symbiont Cell Wall Metabolism

β-Lactams against the Fortress of the Gram-Positive Staphylococcus aureus Bacterium

β-Lactams from the Ocean

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