Envelope Structures of Gram-Positive Bacteria

Rajagopal, Mithila; Walker, Suzanne

doi:10.1007/82_2015_5021

Cited by 190 publications

(203 citation statements)

References 360 publications

(244 reference statements)

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“…The core component of the cell w a l l i s f o r m e d b y a m e s h o f Nacetylg lucosamine (GlcNAc) and Nacetylmuramic acid (MurNAc) glycan chains, which are cross-linked by peptide stems to form the peptidoglycan (PG) sacculus 1 . Bacteria have been classified into two groups based on their cell envelope architecture: monoderm bacteria have a cell envelope that consists of a cytoplasmic membrane and a multilayered envelope, consisting of PG, teichoic acids (TAs) 2,3 and a variety of capsular glycans [4][5][6][7] . Teichoic acids are long, anionic polymers and can be classified into wall teichoic acids (WTAs) and lipoteichoic acids (LTAs), based on their linkages to either the PG or lipid membrane respectively 8,9 .…”

Section: Introductionmentioning

confidence: 99%

Teichoic acids anchor distinct cell wall lamellae in an apically growing bacterium

Ultee

Aart

Dissel

et al. 2019

Preprint

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The bacterial cell wall is a dynamic, multicomponent structure that provides structural support for cell shape and physical protection from the environment. In monoderm species, the thick cell wall is made up predominantly of peptidoglycan, teichoic acids and a variety of capsular glycans. Filamentous monoderm Actinobacteria, such as Streptomyces coelicolor, incorporate new cell wall material at the apex of their hyphal cells during growth. In this study we use cryo-electron tomography to reveal the structural architecture of the cell wall of this bacterium. Our data shows a density difference between the apex and subapical regions of chemically isolated sacculi. Removal of the teichoic acids with hydrofluoric acid reveals a rough and patchy cell wall and distinct lamellae in a number of sacculi. Absence of the extracellular glycans poly-β-1,6-N-acetylglucosamine and a cellulose-like polymer, produced by the MatAB and CslA proteins respectively, results in a thinner sacculus and absence of lamellae and patches. Extracellular glycans might thus form or lead to the formation of the outer cell wall lamella. Based on these findings we propose a revisited model for the complex cell wall architecture of an apically growing bacterium, in which the network of peptidoglycan together with extracellular polymers is structurally supported by teichoic acids. " 1 " 2 " 13

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Section: Introductionmentioning

confidence: 99%

Teichoic acids anchor distinct cell wall lamellae in an apically growing bacterium

Ultee

Aart

Dissel

et al. 2019

Preprint

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“…In Gram-positive organisms, peptidoglycan (PG), the biosynthesis of which is targeted by many clinically used antibiotics, makes up only about fifty percent of the sacculus by mass 3 . The other fifty percent of the mass largely comprises glycopolymers that are covalently bound to peptidoglycan 4 .…”

Section: Introductionmentioning

confidence: 99%

In vitro reconstitution demonstrates the cell wall ligase activity of LCP proteins

et al. 2017

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Sacculus is a peptidoglycan matrix that protects bacteria from osmotic lysis. In Gram-positive organisms, the sacculus is densely functionalized with glycopolymers important for survival, but how assembly occurs is not known. In Staphylococcus aureus, three LCP family members have been implicated in attaching the major glycopolymer wall teichoic acid (WTA) to peptidoglycan, but ligase activity has not been demonstrated for these or any other LCP proteins. Using WTA and peptidoglycan substrates produced chemoenzymatically, we show that all three proteins can transfer WTA precursors to nascent peptidoglycan, establishing that LCP proteins are peptidoglycan-glycopolymer ligases. Although all S. aureus LCP proteins have the capacity to attach WTA to PG, we show that their cellular functions are not redundant. Strains lacking lcpA have phenotypes similar to WTA null strains, indicating that this is the most important WTA ligase. This work provides a foundation for studying how LCP enzymes participate in cell wall assembly.

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“…It is called by either of three synonyms: the murein, the sacculus, or (most commonly) the peptidoglycan. The peptide stems of the peptidoglycan have function beyond their primary role of crosslinking: they are used to covalently attach yet different glycan strands (called wall teichoic acids) and proteins . The genera of notable pathogenic Gram‐positive bacteria include the Enterococci, the Staphylococci, and the Streptococci.…”

Section: The Cell Envelope Of Bacteriamentioning

confidence: 99%

“…The peptide stems of the peptidoglycan have function beyond their primary role of crosslinking: they are used to covalently attach yet different glycan strands (called wall teichoic acids) and proteins. [67][68][69][70][71] The genera of notable pathogenic Gram-positive bacteria include the Enterococci, the Staphylococci, and the Streptococci. The cell envelope of Gram-negative bacteria is more complex.…”

Section: The Cell Envelope Of Bacteriamentioning

confidence: 99%

Constructing and deconstructing the bacterial cell wall

Fisher

Mobashery

2019

Protein Science

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The history of modern medicine cannot be written apart from the history of the antibiotics. Antibiotics are cytotoxic secondary metabolites that are isolated from Nature. The antibacterial antibiotics disproportionately target bacterial protein structure that is distinct from eukaryotic protein structure, notably within the ribosome and within the pathways for bacterial cell‐wall biosynthesis (for which there is not a eukaryotic counterpart). This review focuses on a pre‐eminent class of antibiotics—the β‐lactams, exemplified by the penicillins and cephalosporins—from the perspective of the evolving mechanisms for bacterial resistance. The mechanism of action of the β‐lactams is bacterial cell‐wall destruction. In the monoderm (single membrane, Gram‐positive staining) pathogen Staphylococcus aureus the dominant resistance mechanism is expression of a β‐lactam‐unreactive transpeptidase enzyme that functions in cell‐wall construction. In the diderm (dual membrane, Gram‐negative staining) pathogen Pseudomonas aeruginosa a dominant resistance mechanism (among several) is expression of a hydrolytic enzyme that destroys the critical β‐lactam ring of the antibiotic. The key sensing mechanism used by P. aeruginosa is monitoring the molecular difference between cell‐wall construction and cell‐wall deconstruction. In both bacteria, the resistance pathways are manifested only when the bacteria detect the presence of β‐lactams. This review summarizes how the β‐lactams are sensed and how the resistance mechanisms are manifested, with the expectation that preventing these processes will be critical to future chemotherapeutic control of multidrug resistant bacteria.

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Envelope Structures of Gram-Positive Bacteria

Cited by 190 publications

References 360 publications

Teichoic acids anchor distinct cell wall lamellae in an apically growing bacterium

Teichoic acids anchor distinct cell wall lamellae in an apically growing bacterium

In vitro reconstitution demonstrates the cell wall ligase activity of LCP proteins

Constructing and deconstructing the bacterial cell wall

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