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The Cell Wall of

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  • Authors: Waldemar Vollmer1, Orietta Massidda2, Alexander Tomasz3
  • Editors: Vincent A. Fischetti4, Richard P. Novick5, Joseph J. Ferretti6, Daniel A. Portnoy7, Miriam Braunstein8, Julian I. Rood9
  • VIEW AFFILIATIONS HIDE AFFILIATIONS
    Affiliations: 1: Institute for Cell and Molecular Biosciences, The Centre for Bacterial Cell Biology, Newcastle University, Newcastle upon Tyne, United Kingdom; 2: Department of Cellular, Computational and Integrative Biology, University of Trento, Trento, Italy; 3: The Rockefeller University, New York, NY; 4: The Rockefeller University, New York, NY; 5: Skirball Institute for Molecular Medicine, NYU Medical Center, New York, NY; 6: Department of Microbiology & Immunology, University of Oklahoma Health Science Center, Oklahoma City, OK; 7: Department of Molecular and Cellular Microbiology, University of California, Berkeley, Berkeley, CA; 8: Department of Microbiology and Immunology, University of North Carolina-Chapel Hill, Chapel Hill, NC; 9: Infection and Immunity Program, Monash Biomedicine Discovery Institute, Monash University, Melbourne, Australia
  • Source: microbiolspec June 2019 vol. 7 no. 3 doi:10.1128/microbiolspec.GPP3-0018-2018
  • Received 11 January 2018 Accepted 19 April 2019 Published 07 June 2019
  • Alexander Tomasz, [email protected]
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  • Abstract:

    has a complex cell wall that plays key roles in cell shape maintenance, growth and cell division, and interactions with components of the human host. The peptidoglycan has a heterogeneous composition with more than 50 subunits (muropeptides)—products of several peptidoglycan-modifying enzymes. The amidation of glutamate residues in the stem peptide is needed for efficient peptide cross-linking, and peptides with a dipeptide branch prevail in some beta-lactam-resistant strains. The glycan strands are modified by deacetylation of -acetylglucosamine residues and -acetylation of -acetylmuramic acid residues, and both modifications contribute to pneumococcal resistance to lysozyme. The glycan strands carry covalently attached wall teichoic acid and capsular polysaccharide. Pneumococci are unique in that the wall teichoic acid and lipoteichoic acid contain the same unusually complex repeating units decorated with phosphoryl choline residues, which anchor the choline-binding proteins. The structures of lipoteichoic acid and the attachment site of wall teichoic acid to peptidoglycan have recently been revised. During growth, pneumococci assemble their cell walls at midcell in coordinated rounds of cell elongation and division, leading to the typical ovococcal cell shape. Cell wall growth depends on the cytoskeletal FtsA and FtsZ proteins and is regulated by several morphogenesis proteins that also show patterns of dynamic localization at midcell. Some of the key regulators are phosphorylated by StkP and dephosphorylated by PhpP to facilitate robust selection of the division site and plane and to maintain cell shape.

  • Citation: Vollmer W, Massidda O, Tomasz A. 2019. The Cell Wall of . Microbiol Spectrum 7(3):GPP3-0018-2018. doi:10.1128/microbiolspec.GPP3-0018-2018.

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/content/journal/microbiolspec/10.1128/microbiolspec.GPP3-0018-2018
2019-06-07
2019-10-15

Abstract:

has a complex cell wall that plays key roles in cell shape maintenance, growth and cell division, and interactions with components of the human host. The peptidoglycan has a heterogeneous composition with more than 50 subunits (muropeptides)—products of several peptidoglycan-modifying enzymes. The amidation of glutamate residues in the stem peptide is needed for efficient peptide cross-linking, and peptides with a dipeptide branch prevail in some beta-lactam-resistant strains. The glycan strands are modified by deacetylation of -acetylglucosamine residues and -acetylation of -acetylmuramic acid residues, and both modifications contribute to pneumococcal resistance to lysozyme. The glycan strands carry covalently attached wall teichoic acid and capsular polysaccharide. Pneumococci are unique in that the wall teichoic acid and lipoteichoic acid contain the same unusually complex repeating units decorated with phosphoryl choline residues, which anchor the choline-binding proteins. The structures of lipoteichoic acid and the attachment site of wall teichoic acid to peptidoglycan have recently been revised. During growth, pneumococci assemble their cell walls at midcell in coordinated rounds of cell elongation and division, leading to the typical ovococcal cell shape. Cell wall growth depends on the cytoskeletal FtsA and FtsZ proteins and is regulated by several morphogenesis proteins that also show patterns of dynamic localization at midcell. Some of the key regulators are phosphorylated by StkP and dephosphorylated by PhpP to facilitate robust selection of the division site and plane and to maintain cell shape.

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Image of FIGURE 1
FIGURE 1

Diagram of the cell wall complex of pneumococci. Some of the MurNAc and GlcNAc residues in the glycan chains of peptidoglycan are modified by -acetylation or -deacetylation, respectively. Direct and indirect peptide cross-links are shown. Capsular polysaccharides have been assumed to be connected to MurNAc residues in peptidoglycan, but recent work showed that they might be connected to GlcNAc residues. Surface proteins are covalently linked to peptides in peptidoglycan; choline-binding proteins attach noncovalently to phosphoryl choline residues in WTA.

Source: microbiolspec June 2019 vol. 7 no. 3 doi:10.1128/microbiolspec.GPP3-0018-2018
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Image of FIGURE 2
FIGURE 2

Role of MurM and MurN in cell wall branching. The substrate of the MurM- and MurN-catalyzed branching reaction is lipid II, which is composed of -acetylated disaccharide units of glucosamine (hexagon with G) and muramic acid (hexagon with M) with the pentapeptide attached to the M residues. Lipid II is anchored on the plasma membrane through the carrier lipid bactoprenyl phosphate (zig-zag line). Attachment of the completed precursor to the preexisting cell wall occurs on the outer surface of the plasma membrane by the activity of glycosyltransferases and transpeptidases. Reproduced with permission from reference 82 .

Source: microbiolspec June 2019 vol. 7 no. 3 doi:10.1128/microbiolspec.GPP3-0018-2018
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FIGURE 3

HPLC elution profiles of stem peptides of the peptidoglycan from the penicillin-susceptible strain R36A and several penicillin-resistant strains that carry different abnormal alleles. Structures of cell wall stem peptides identified in the pneumococcal peptidoglycan of penicillin-susceptible and -resistant strains of pneumococci. Reproduced with permission from reference 42 .

Source: microbiolspec June 2019 vol. 7 no. 3 doi:10.1128/microbiolspec.GPP3-0018-2018
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FIGURE 4

Structure of the pneumococcal LTA and WTA. Both types of teichoic acid have identical chains (top) which carry phosphoryl choline and -alanine residues. In LTA the teichoic acid chains are β-glycosidically linked from AATGal to the lipid anchor (bottom left). In WTA the linkage occurs via an α-linkage from AATGal to MurNAc-phosphate in peptidoglycan. The figure was kindly provided by Nicolas Gisch (Research Centre Borstel, Germany). RU, repeating unit.

Source: microbiolspec June 2019 vol. 7 no. 3 doi:10.1128/microbiolspec.GPP3-0018-2018
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FIGURE 5

Cartoon of a cell wall growth and division complex at midcell showing elongation and cell division proteins and the peptidoglycan hydrolases PcsB and LytB, which cleave the septum for pole formation and cell separation.

Source: microbiolspec June 2019 vol. 7 no. 3 doi:10.1128/microbiolspec.GPP3-0018-2018
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Tables

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TABLE 1

Cell wall peptide composition of several strains of

Source: microbiolspec June 2019 vol. 7 no. 3 doi:10.1128/microbiolspec.GPP3-0018-2018

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