Regulation of bacterial cell wall growth

Egan, Alexander J F; Cleverley, Robert M.; Peters, Katharina; Lewis, Richard J.; Vollmer, Waldemar

doi:10.1111/febs.13959

Cited by 145 publications

(114 citation statements)

References 158 publications

(237 reference statements)

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“…Recent clever interdisciplinary study has clarified the identities of the proteins and enzymes that assemble to enable cytoskeleton-driven peptidoglycan synthesis (Bisson-Filho et al , 2017; Egan et al , 2017; Rued et al , 2017; Yang et al , 2017). Their identities are captured in imaginative cartoons suggesting the complexity of the protein-protein interaction network (Egan & Vollmer, 2013; Massidda et al , 2013; Szwedziak & Lowe, 2013; Fleurie et al , 2014; Egan & Vollmer, 2015; Leclercq et al , 2017; Lewis, 2017).…”

Section: Resultsmentioning

confidence: 99%

Lytic transglycosylases: concinnity in concision of the bacterial cell wall

Dik

Marous

Fisher

et al. 2017

Critical Reviews in Biochemistry and Molecular Biology

125

169

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The lytic transglycosylases (LTs) are bacterial enzymes that catalyze the non-hydrolytic cleavage of the peptidoglycan structures of the bacterial cell wall. They are not catalysts of glycan synthesis as might be surmised from their name. Notwithstanding the seemingly mundane reaction catalyzed by the LTs, their lytic reactions serve bacteria for a series of astonishingly diverse purposes. These purposes include cell-wall synthesis, remodeling, and degradation; for the detection of cell-wall-acting antibiotics; for the expression of the mechanism of cell-wall-acting antibiotics; for the insertion of secretion systems and flagellar assemblies into the cell wall; as a virulence mechanism during infection by certain Gram-negative bacteria; and in the sporulation and germination of Gram-positive spores. Significant advances in the mechanistic understanding of each of these processes have coincided with the successive discovery of new LTs structures. In this review, we provide a systematic perspective on what is known on the structure-function correlations for the LTs, while simultaneously identifying numerous opportunities for the future study of these enigmatic enzymes.

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Section: Resultsmentioning

confidence: 99%

Lytic transglycosylases: concinnity in concision of the bacterial cell wall

Dik

Marous

Fisher

et al. 2017

Critical Reviews in Biochemistry and Molecular Biology

125

169

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“…The peptidoglycan biosynthesis machinery is positioned and/or regulated through association with a network of cytosolic and membrane‐bound proteins involved in bacterial growth and morphogenesis (Egan et al ., ). Two major components of the bacterial cytoskeleton are the tubulin homolog FtsZ and the actin homolog MreB (Ouellette et al ., ; Celler et al ., ).…”

Section: Pathways For Peptidoglycan Biosynthesis and Remodellingmentioning

confidence: 97%

Peptidoglycan in obligate intracellular bacteria

Otten

Brilli

Vollmer

et al. 2017

Molecular Microbiology

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SummaryPeptidoglycan is the predominant stress‐bearing structure in the cell envelope of most bacteria, and also a potent stimulator of the eukaryotic immune system. Obligate intracellular bacteria replicate exclusively within the interior of living cells, an osmotically protected niche. Under these conditions peptidoglycan is not necessarily needed to maintain the integrity of the bacterial cell. Moreover, the presence of peptidoglycan puts bacteria at risk of detection and destruction by host peptidoglycan recognition factors and downstream effectors. This has resulted in a selective pressure and opportunity to reduce the levels of peptidoglycan. In this review we have analysed the occurrence of genes involved in peptidoglycan metabolism across the major obligate intracellular bacterial species. From this comparative analysis, we have identified a group of predicted ‘peptidoglycan‐intermediate’ organisms that includes the Chlamydiae, Orientia tsutsugamushi, Wolbachia and Anaplasma marginale. This grouping is likely to reflect biological differences in their infection cycle compared with peptidoglycan‐negative obligate intracellular bacteria such as Ehrlichia and Anaplasma phagocytophilum, as well as obligate intracellular bacteria with classical peptidoglycan such as Coxiella, Buchnera and members of the Rickettsia genus. The signature gene set of the peptidoglycan‐intermediate group reveals insights into minimal enzymatic requirements for building a peptidoglycan‐like sacculus and/or division septum.

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“…These glycan chains are composed of alternating residues of GlcNAc and N-acetylmuramic acid (MurNAc) linked by β-1,4 bonds. 30,31 MurNAc is the ether of lactic acid and GlcNAc, in which a D-lactate residue is attached to the C-3 atom of the glucopyranoside ring. Indeed, the first step during PG biosynthesis is the conversion of UDP-GlcNAc to UDP-MurNAc.…”

Section: Discussionmentioning

confidence: 99%