Relevant bibliographies by topics / Peptidoglycan polymerization

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Academic literature on the topic 'Peptidoglycan polymerization'

Author: Grafiati
Published: 25 May 2024

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Journal articles on the topic "Peptidoglycan polymerization"

1

Arthur, Michel. "Regulation of Bacterial Peptidoglycan Polymerization." Trends in Microbiology 24, no. 7 (July 2016): 519–21. http://dx.doi.org/10.1016/j.tim.2016.05.003.

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Vasudevan, Pradeep, Jessica McElligott, Christa Attkisson, Michael Betteken, and David L. Popham. "Homologues of the Bacillus subtilis SpoVB Protein Are Involved in Cell Wall Metabolism." Journal of Bacteriology 191, no. 19 (July 31, 2009): 6012–19. http://dx.doi.org/10.1128/jb.00604-09.

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ABSTRACT Members of the COG2244 protein family are integral membrane proteins involved in synthesis of a variety of extracellular polymers. In several cases, these proteins have been suggested to move lipid-linked oligomers across the membrane or, in the case of Escherichia coli MviN, to flip the lipid II peptidoglycan precursor. Bacillus subtilis SpoVB was the first member of this family implicated in peptidoglycan synthesis and is required for spore cortex polymerization. Three other COG2244 members with high similarity to SpoVB are encoded within the B. subtilis genome. Mutant strains lacking any or all of these genes (yabM, ykvU, and ytgP) in addition to spoVB are viable and produce apparently normal peptidoglycan, indicating that their function is not essential in B. subtilis. Phenotypic changes associated with loss of two of these genes suggest that they function in peptidoglycan synthesis. Mutants lacking YtgP produce long cells and chains of cells, suggesting a role in cell division. Mutants lacking YabM exhibit sensitivity to moenomycin, an antibiotic that blocks peptidoglycan polymerization by class A penicillin-binding proteins. This result suggests that YabM may function in a previously observed alternate pathway for peptidoglycan strand synthesis.
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3

Chan, Yvonne G. Y., Matthew B. Frankel, Dominique Missiakas, and Olaf Schneewind. "SagB Glucosaminidase Is a Determinant of Staphylococcus aureus Glycan Chain Length, Antibiotic Susceptibility, and Protein Secretion." Journal of Bacteriology 198, no. 7 (January 25, 2016): 1123–36. http://dx.doi.org/10.1128/jb.00983-15.

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ABSTRACTThe envelope ofStaphylococcus aureusis comprised of peptidoglycan and its attached secondary polymers, teichoic acid, capsular polysaccharide, and protein. Peptidoglycan synthesis involves polymerization of lipid II precursors into glycan strands that are cross-linked at wall peptides. It is not clear whether peptidoglycan structure is principally determined during polymerization or whether processive enzymes affect cell wall structure and function, for example, by generating conduits for protein secretion. We show here thatS. aureuslacking SagB, a membrane-associatedN-acetylglucosaminidase, displays growth and cell-morphological defects caused by the exaggerated length of peptidoglycan strands. SagB cleaves polymerized glycan strands to their physiological length and modulates antibiotic resistance in methicillin-resistantS. aureus(MRSA). Deletion ofsagBperturbs protein trafficking into and across the envelope, conferring defects in cell wall anchoring and secretion, as well as aberrant excretion of cytoplasmic proteins.IMPORTANCEStaphylococcus aureusis thought to secrete proteins across the plasma membrane via the Sec pathway; however, protein transport across the cell wall envelope has heretofore not been studied. We report thatS. aureus sagBmutants generate elongated peptidoglycan strands and display defects in protein secretion as well as aberrant excretion of cytoplasmic proteins. These results suggest that the thick peptidoglycan layer of staphylococci presents a barrier for protein secretion and that SagB appears to extend the Sec pathway across the cell wall envelope.
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4

Zuber, Benoît, Marisa Haenni, Tânia Ribeiro, Kathrin Minnig, Fátima Lopes, Philippe Moreillon, and Jacques Dubochet. "Granular Layer in the Periplasmic Space of Gram-Positive Bacteria and Fine Structures of Enterococcus gallinarum and Streptococcus gordonii Septa Revealed by Cryo-Electron Microscopy of Vitreous Sections." Journal of Bacteriology 188, no. 18 (September 15, 2006): 6652–60. http://dx.doi.org/10.1128/jb.00391-06.

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ABSTRACT High-resolution structural information on optimally preserved bacterial cells can be obtained with cryo-electron microscopy of vitreous sections. With the help of this technique, the existence of a periplasmic space between the plasma membrane and the thick peptidoglycan layer of the gram-positive bacteria Bacillus subtilis and Staphylococcus aureus was recently shown. This raises questions about the mode of polymerization of peptidoglycan. In the present study, we report the structure of the cell envelope of three gram-positive bacteria (B. subtilis, Streptococcus gordonii, and Enterococcus gallinarum). In the three cases, a previously undescribed granular layer adjacent to the plasma membrane is found in the periplasmic space. In order to better understand how nascent peptidoglycan is incorporated into the mature peptidoglycan, we investigated cellular regions known to represent the sites of cell wall production. Each of these sites possesses a specific structure. We propose a hypothetic model of peptidoglycan polymerization that accommodates these differences: peptidoglycan precursors could be exported from the cytoplasm to the periplasmic space, where they could diffuse until they would interact with the interface between the granular layer and the thick peptidoglycan layer. They could then polymerize with mature peptidoglycan. We report cytoplasmic structures at the E. gallinarum septum that could be interpreted as cytoskeletal elements driving cell division (FtsZ ring). Although immunoelectron microscopy and fluorescence microscopy studies have demonstrated the septal and cytoplasmic localization of FtsZ, direct visualization of in situ FtsZ filaments has not been obtained in any electron microscopy study of fixed and dehydrated bacteria.
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Ruiz, Natividad. "Bioinformatics identification of MurJ (MviN) as the peptidoglycan lipid II flippase inEscherichia coli." Proceedings of the National Academy of Sciences 105, no. 40 (October 1, 2008): 15553–57. http://dx.doi.org/10.1073/pnas.0808352105.

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Peptidoglycan is a cell-wall glycopeptide polymer that protects bacteria from osmotic lysis. Whereas in Gram-positive bacteria it also serves as scaffold for many virulence factors, in Gram-negative bacteria, peptidoglycan is an anchor for the outer membrane. For years, we have known the enzymes required for the biosynthesis of peptidoglycan; what was missing was the flippase that translocates the lipid-anchored precursors across the cytoplasmic membrane before their polymerization into mature peptidoglycan. Using a reductionist bioinformatics approach, I have identified the essential inner-membrane protein MviN (renamed MurJ) as a likely candidate for the peptidoglycan flippase inEscherichia coli. Here, I present genetic and biochemical data that confirm the requirement of MurJ for peptidoglycan biosynthesis and that are in agreement with a role of MurJ as a flippase. Because of its essential nature, MurJ could serve as a target in the continuing search for antimicrobial compounds.
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Yagi, Tetsuya, Sebabrata Mahapatra, Katarína Mikušová, Dean C. Crick, and Patrick J. Brennan. "Polymerization of Mycobacterial Arabinogalactan and Ligation to Peptidoglycan." Journal of Biological Chemistry 278, no. 29 (April 28, 2003): 26497–504. http://dx.doi.org/10.1074/jbc.m302216200.

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7

Arbeloa, Ana, Heidi Segal, Jean-Emmanuel Hugonnet, Nathalie Josseaume, Lionnel Dubost, Jean-Paul Brouard, Laurent Gutmann, Dominique Mengin-Lecreulx, and Michel Arthur. "Role of Class A Penicillin-Binding Proteins in PBP5-Mediated β-Lactam Resistance in Enterococcus faecalis." Journal of Bacteriology 186, no. 5 (March 1, 2004): 1221–28. http://dx.doi.org/10.1128/jb.186.5.1221-1228.2004.

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ABSTRACT Peptidoglycan polymerization complexes contain multimodular penicillin-binding proteins (PBP) of classes A and B that associate a conserved C-terminal transpeptidase module to an N-terminal glycosyltransferase or morphogenesis module, respectively. In Enterococcus faecalis, class B PBP5 mediates intrinsic resistance to the cephalosporin class of β-lactam antibiotics, such as ceftriaxone. To identify the glycosyltransferase partner(s) of PBP5, combinations of deletions were introduced in all three class A PBP genes of E. faecalis JH2-2 (ponA, pbpF, and pbpZ). Among mutants with single or double deletions, only JH2-2 ΔponA ΔpbpF was susceptible to ceftriaxone. Ceftriaxone resistance was restored by heterologous expression of pbpF from Enterococcus faecium but not by mgt encoding the monofunctional glycosyltransferase of Staphylococcus aureus. Thus, PBP5 partners essential for peptidoglycan polymerization in the presence of β-lactams formed a subset of the class A PBPs of E. faecalis, and heterospecific complementation was observed with an ortholog from E. faecium. Site-directed mutagenesis of pbpF confirmed that the catalytic serine residue of the transpeptidase module was not required for resistance. None of the three class A PBP genes was essential for viability, although deletion of the three genes led to an increase in the generation time and to a decrease in peptidoglycan cross-linking. As the E. faecalis chromosome does not contain any additional glycosyltransferase-related genes, these observations indicate that glycan chain polymerization in the triple mutant is performed by a novel type of glycosyltransferase. The latter enzyme was not inhibited by moenomycin, since deletion of the three class A PBP genes led to high-level resistance to this glycosyltransferase inhibitor.
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Rice, Louis B., Lenore L. Carias, Susan Rudin, Rebecca Hutton, Steven Marshall, Medhat Hassan, Nathalie Josseaume, Lionel Dubost, Arul Marie, and Michel Arthur. "Role of Class A Penicillin-Binding Proteins in the Expression of β-Lactam Resistance in Enterococcus faecium." Journal of Bacteriology 191, no. 11 (March 20, 2009): 3649–56. http://dx.doi.org/10.1128/jb.01834-08.

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ABSTRACT Peptidoglycan is polymerized by monofunctional d,d-transpeptidases belonging to class B penicillin-binding proteins (PBPs) and monofunctional glycosyltransferases and by bifunctional enzymes that combine both activities (class A PBPs). Three genes encoding putative class A PBPs (pbpF, pbpZ, and ponA) were deleted from the chromosome of Enterococcus faecium D344R in all possible combinations in order to identify the glycosyltransferases that cooperate with low-affinity class B Pbp5 for synthesis of peptidoglycan in the presence of β-lactam antibiotics. The viability of the triple mutant indicated that glycan strands can be polymerized independently from class A PBPs by an unknown glycosyltranferase. The susceptibility of the ΔpbpF ΔponA mutant and triple mutants to extended spectrum cephalosporins (ceftriaxone and cefepime) identified either PbpF or PonA as essential partners of Pbp5 for peptidoglycan polymerization in the presence of the drugs. Mass spectrometry analysis of peptidoglycan structure showed that loss of PonA and PbpF activity led to a minor decrease in the extent of peptidoglycan cross-linking by the remaining PBPs without any detectable compensatory increase in the participation of the l,d-transpeptidase in peptidoglycan synthesis. Optical density measurements and electron microscopy analyses showed that the ΔpbpF ΔponA mutant underwent increased stationary-phase autolysis compared to the parental strain. Unexpectedly, deletion of the class A pbp genes revealed dissociation between the expression of resistance to cephalosporins and penicillins, although the production of Pbp5 was required for resistance to both classes of drugs. Thus, susceptibility of Pbp5-mediated peptidoglycan cross-linking to different β-lactam antibiotics differed as a function of its partner glycosyltransferase.
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Allen, N. E., J. N. Hobbs, and T. I. Nicas. "Inhibition of peptidoglycan biosynthesis in vancomycin-susceptible and -resistant bacteria by a semisynthetic glycopeptide antibiotic." Antimicrobial Agents and Chemotherapy 40, no. 10 (October 1996): 2356–62. http://dx.doi.org/10.1128/aac.40.10.2356.

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LY191145 is a p-chlorobenzyl derivative of LY264826 (A82846B) with activity against both vancomycin-susceptible and -resistant enterococci. Incorporation of L-[14C]lysine into peptidoglycan of intact vancomycin-susceptible and -resistant Enterococcus faecium was inhibited by LY191145 (50% inhibitory concentrations of 1 and 5 microgram/ml, respectively). Inhibition was accompanied by accumulation of UDP-muramyl-peptide precursors in the cytoplasm. This agent inhibited late-stage steps in peptidoglycan biosynthesis in permeabilized E. faecium when either the UDP-muramyl-pentapeptide precursor from vancomycin-susceptible E. faecium or the UDP-muramyl-pentadepsipeptide precursor from vancomycin-resistant E. faecium was used as a substrate. Inhibition of late-stage steps led to accumulation of an N-acetyl-[14C]glucosamine-labeled lipid intermediate indicative of inhibition of the transglycosylation step. Inhibition of peptidoglycan polymerization without affecting cross-linking in a particulate membrane-plus-wall-fragment assay from Aerococcus viridans was consistent with this explanation. The fact that inhibition of peptidoglycan biosynthesis by LY191145 was not readily antagonized by an excess of free acyl-D-alanyl-D-alanine or acyl-D-alanyl-D-lactate ligands indicates that the manner in which this compound inhibits transglycosylation may not be identical to that of vancomycin.
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Braddick, Darren, Sandeep Sandhu, David I. Roper, Michael J. Chappell, and Timothy D. H. Bugg. "Observation of the time-course for peptidoglycan lipid intermediate II polymerization by Staphylococcus aureus monofunctional transglycosylase." Microbiology 160, no. 8 (August 1, 2014): 1628–36. http://dx.doi.org/10.1099/mic.0.079442-0.

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The polymerization of lipid intermediate II by the transglycosylase activity of penicillin-binding proteins (PBPs) represents an important target for antibacterial action, but limited methods are available for quantitative assay of this reaction, or screening potential inhibitors. A new labelling method for lipid II polymerization products using Sanger’s reagent (fluoro-2,4-dinitrobenzene), followed by gel permeation HPLC analysis, has permitted the observation of intermediate polymerization products for Staphylococcus aureus monofunctional transglycosylase MGT. Peak formation is inhibited by 6 µM ramoplanin or enduracidin. Characterization by mass spectrometry indicates the formation of tetrasaccharide and octasaccharide intermediates, but not a hexasaccharide intermediate, suggesting a dimerization of a lipid-linked tetrasaccharide. Numerical modelling of the time-course data supports a kinetic model involving addition to lipid-linked tetrasaccharide of either lipid II or lipid-linked tetrasaccharide. Observation of free octasaccharide suggests that hydrolysis of the undecaprenyl diphosphate lipid carrier occurs at this stage in peptidoglycan transglycosylation.
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Dissertations / Theses on the topic "Peptidoglycan polymerization"

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Yunck, Rachel. "Identification of MltG as a Potential Terminase for Peptidoglycan Polymerization in Bacteria." Thesis, Harvard University, 2016. http://nrs.harvard.edu/urn-3:HUL.InstRepos:33493474.

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Bacterial cells are fortified against osmotic lysis by a cell wall made of peptidoglycan (PG). Synthases called penicillin-binding proteins (PBPs), the targets of penicillin and related antibiotics, polymerize the glycan strands of PG and crosslink them into the cell wall meshwork via attached peptides. The average length of glycan chains inserted into the matrix by the PBPs is thought to play an important role in bacterial morphogenesis, but polymerization termination factors controlling this process have yet to be discovered. Here, we report the identification of Escherichia coli MltG (YceG) as a potential terminase for glycan polymerization that is broadly conserved in bacteria. A clone containing mltG was initially isolated in a screen for multicopy plasmids generating a lethal phenotype in cells defective for the PG synthase PBP1b. Biochemical studies revealed that MltG is an inner membrane enzyme with endolytic transglycosylase activity capable of cleaving at internal positions within a glycan polymer. Radiolabeling experiments further demonstrated MltG-dependent nascent PG processing in vivo, and bacterial two-hybrid analysis identified an MltG-PBP1b interaction. Mutants lacking MltG were also shown to have longer glycans in their PG relative to wild-type cells. Our combined results are thus consistent with a model in which MltG associates with PG synthetic complexes to cleave nascent polymers and terminate their elongation.
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Atze, Heiner. "Optimization of beta-lactamase inhibitors belonging to the diazabicyclo-octane family and design of a mass spectrometry-based approach for exploring peptidoglycan polymerization." Electronic Thesis or Diss., Sorbonne université, 2021. https://accesdistant.sorbonne-universite.fr/login?url=https://theses-intra.sorbonne-universite.fr/2021SORUS159.pdf.

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Le peptidoglycane (PG) forme un réseau covalent comprenant de chaînes glycanes reliées par des peptides. Le PG est une cible validée pour développer de nouveaux antibiotiques parce que c’est un composant spécifique et essentiel des bactéries. En effet, les antibiotiques appartenant à la famille des β-lactamines inactivent les protéines de liaisons à la pénicilline (PLP) qui catalysent la dernière étape de polymérisation du PG. Un mécanisme répandu de résistance est la production de β-lactamases (βL) qui inactivent les β-lactamines. Une première génération d’inhibiteurs de βL a été basée sur le noyau β-lactame suivi par les diazabicyclooctanes (DBO) entrés sur le marché en 2015 avec l’avibactam. L’émergence de mutations compromettant l’efficacité des DBO nous a incités à étudier une série de dérivés obtenue par chimie click qui contenait un groupement triazole. Ce dernier s’est avéré défavorable en raison de l’absence de la liaison hydrogène reliant le carboxamide des DBO commercialisés au résidu conservé N132 des βL. Cependant, la fonctionnalisation du triazole a partiellement restauré l’efficacité des DBO sans altérer leur pénétration. Les PLP peuvent être remplacées par des L,D-transpeptidases (LDT) entrainant une résistance aux β-lactamines. Nous avons étudié le mode d’insertion de nouvelles sous-unités dans le PG en expansion en développant une nouvelle méthode basée sur le marquage avec des isotopes lourds et la spectrométrie de masse. Nous rapportons les modes de polymérisation du PG dans des souches utilisant des PBP et une LDT, seules ou en combinaison, et en présence ou en absence de β-lactamine, ainsi que la participation du recyclage au métabolisme du PG
Bacterial peptidoglycan (PG) is a mesh like structure comprising glycan strands cross-linked by peptide stems. Since PG is a specific and essential component of bacterial cells it is an attractive and validated target for antibacterial agents. Indeed, the first antibiotic in clinical use - the β-lactam penicillin - targets the enzymes catalyzing the final transpeptidation step of PG synthesis - the Penicillin-Binding-Proteins (PBPs). A prevalent mechanism of resistance to β-lactams is the production of β-lactamases (βLs) that inactivate the drugs. A first generation of β-lactamase inhibitors (BLIs) was based on the β-lactam core followed by diazabicyclooctanes (DBOs), which entered the market in 2015 with avibactam. Emergence of mutations compromising the efficacy of DBOs prompted us to study a series of triazole-substituted DBOs that were obtained by click chemistry. The triazole ring was found to be disfavored due to the absence of a hydrogen bond connecting the carboxamide of marketed DBOs to the conserved N132 residue of βLs. However, functionalization of the triazole partially restored inhibition efficacy without impairing drug penetration. Besides the major cross-links formed by PBPs, alternative cross-links are formed by the structurally distinct l,d-transpeptidases (LDTs) mediating resistance to several β-lactams. We investigated the mechanisms of insertion of new subunits into the expanding PG mesh by developing a method based on labeling with heavy isotopes and mass spectrometry. We report the modes of PG polymerization in strains relying on PBPs and LDTs for PG cross-linking in the presence or absence of β-lactams together with the extent of PG recycling
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Book chapters on the topic "Peptidoglycan polymerization"

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van Heijenoort, Jean, Dominique Mengin-Lecreulx, Yveline van Heijenoort, Didier Blanot, Bernard Flouret, Catherine Michaud, Claudine Parquet, Flore Pratviel-Sosa, Manolo Gomez, and Juan A. Ayala. "Variations in the Metabolism of Peptidoglycan Prior to Polymerization." In Bacterial Growth and Lysis, 127–38. Boston, MA: Springer US, 1993. http://dx.doi.org/10.1007/978-1-4757-9359-8_15.

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