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Journal articles on the topic 'Pyocyanin, Staphylococcus aureus peptidoglycan'

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Author: Grafiati

Published: 4 June 2021

Last updated: 14 February 2022

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1

Vemula, Harika, Navid J. Ayon, and William G. Gutheil. "Cytoplasmic peptidoglycan intermediate levels in Staphylococcus aureus." Biochimie 121 (February 2016): 72–78. http://dx.doi.org/10.1016/j.biochi.2015.11.017.

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2

Szweda, Piotr, Marta Schielmann, Roman Kotlowski, Grzegorz Gorczyca, Magdalena Zalewska, and Slawomir Milewski. "Peptidoglycan hydrolases-potential weapons against Staphylococcus aureus." Applied Microbiology and Biotechnology 96, no. 5 (October 18, 2012): 1157–74. http://dx.doi.org/10.1007/s00253-012-4484-3.

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3

Pozur, V. V., L. M. Skivka, and G. P. Potebnia. "Peptidoglycan Staphylococcus aureus and its immune-biological features." Biopolymers and Cell 24, no. 1 (January 20, 2008): 3–13. http://dx.doi.org/10.7124/bc.00078a.

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4

GROV, A., and K. SVEEN. "INDUCTION OF LEUKOCHEMOTAXIS BY PEPTIDOGLYCAN OF STAPHYLOCOCCUS AUREUS." Acta Pathologica Microbiologica Scandinavica Section B Microbiology 86B, no. 1-6 (August 15, 2009): 375–78. http://dx.doi.org/10.1111/j.1699-0463.1978.tb00059.x.

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5

Fournier, Bénédicte, and Dana J. Philpott. "Recognition of Staphylococcus aureus by the Innate Immune System." Clinical Microbiology Reviews 18, no. 3 (July 2005): 521–40. http://dx.doi.org/10.1128/cmr.18.3.521-540.2005.

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SUMMARY The gram-positive bacterium Staphylococcus aureus is a major pathogen responsible for a variety of diseases ranging from minor skin infections to life-threatening conditions such as sepsis. Cell wall-associated and secreted proteins (e.g., protein A, hemolysins, and phenol-soluble modulin) and cell wall components (e.g., peptidoglycan and alanylated lipoteichoic acid) have been shown to be inflammatory, and these staphylococcal components may contribute to sepsis. On the host side, many host factors have been implicated in the innate detection of staphylococcal components. One class of pattern recognition molecules, Toll-like receptor 2, has been shown to function as the transmembrane component involved in the detection of staphylococcal lipoteichoic acid and phenol-soluble modulin and is involved in the synthesis of inflammatory cytokines by monocytes/macrophages in response to these components. Nod2 (nucleotide-binding oligomerization domain 2) is the intracellular sensor for muramyl dipeptide, the minimal bioactive structure of peptidoglycan, and it may contribute to the innate immune defense against S. aureus. The staphylococcal virulence factor protein A was recently shown to interact directly with tumor necrosis factor receptor 1 in airway epithelium and to reproduce the effects of tumor necrosis factor alpha. Finally, peptidoglycan recognition protein L is an amidase that inactivates the proinflammatory activities of peptidoglycan. However, peptidoglycan recognition protein L probably plays a minor role in the innate immune response to S. aureus. Thus, several innate immunity receptors may be implicated in host defense against S. aureus.

6

Mattsson, Eva, Heiko Herwald, Lars Björck, and Arne Egesten. "Peptidoglycan from Staphylococcus aureus Induces Tissue Factor Expression and Procoagulant Activity in Human Monocytes." Infection and Immunity 70, no. 6 (June 2002): 3033–39. http://dx.doi.org/10.1128/iai.70.6.3033-3039.2002.

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ABSTRACT Staphylococcus aureus is one of the most significant pathogens in human sepsis and endocarditis. S. aureus can initiate blood coagulation, leading to the formation of microthrombi and multiorgan dysfunction in sepsis, whereas in endocarditis the bacterium induces fibrin clots on the inner surface of the heart, so-called endocardial vegetations. In the present study, we show that live and heat-killed S. aureus bacteria are potent inducers of procoagulant activity in human peripheral blood mononuclear cells. Furthermore, purified peptidoglycan, the main cell wall component of S. aureus, induced procoagulant activity in mononuclear cells in a concentration-dependent fashion. The procoagulant activity in these cells was dependent on expression of tissue factor, since antibodies to tissue factor inhibited the effect of peptidoglycan. In mononuclear cells stimulated with peptidoglycan, reverse transcription-PCR showed tissue factor gene expression, and the gene product was detected by enzyme-linked immunosorbent assay. Finally, flow cytometry identified tissue factor at the surface of CD14-positive monocytes. Peptidoglycan is known to induce proinflammatory cytokine production in monocytes. The present investigation shows that peptidoglycan also activates the extrinsic pathway of coagulation by inducing the expression of tissue factor in these cells. This mechanism helps to explain the procoagulant activity, which plays such an important role in the pathogenicity of severe S. aureus infections.

7

Sutton, Joshua A. F., Oliver T. Carnell, Lucia Lafage, Joe Gray, Jacob Biboy, Josie F. Gibson, Eric J. G. Pollitt, et al. "Staphylococcus aureus cell wall structure and dynamics during host-pathogen interaction." PLOS Pathogens 17, no. 3 (March 31, 2021): e1009468. http://dx.doi.org/10.1371/journal.ppat.1009468.

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Peptidoglycan is the major structural component of the Staphylococcus aureus cell wall, in which it maintains cellular integrity, is the interface with the host, and its synthesis is targeted by some of the most crucial antibiotics developed. Despite this importance, and the wealth of data from in vitro studies, we do not understand the structure and dynamics of peptidoglycan during infection. In this study we have developed methods to harvest bacteria from an active infection in order to purify cell walls for biochemical analysis ex vivo. Isolated ex vivo bacterial cells are smaller than those actively growing in vitro, with thickened cell walls and reduced peptidoglycan crosslinking, similar to that of stationary phase cells. These features suggested a role for specific peptidoglycan homeostatic mechanisms in disease. As S. aureus missing penicillin binding protein 4 (PBP4) has reduced peptidoglycan crosslinking in vitro its role during infection was established. Loss of PBP4 resulted in an increased recovery of S. aureus from the livers of infected mice, which coincided with enhanced fitness within murine and human macrophages. Thicker cell walls correlate with reduced activity of peptidoglycan hydrolases. S. aureus has a family of 4 putative glucosaminidases, that are collectively crucial for growth. Loss of the major enzyme SagB, led to attenuation during murine infection and reduced survival in human macrophages. However, loss of the other three enzymes Atl, SagA and ScaH resulted in clustering dependent attenuation, in a zebrafish embryo, but not a murine, model of infection. A combination of pbp4 and sagB deficiencies resulted in a restoration of parental virulence. Our results, demonstrate the importance of appropriate cell wall structure and dynamics during pathogenesis, providing new insight to the mechanisms of disease.

8

Wang, Yong, Zhiguang Liang, Yuanyuan Zheng, Alan Siu-Lun Leung, Siu-Cheong Yan, Pui-Kin So, Yun-Chung Leung, Wing-Leung Wong, and Kwok-Yin Wong. "Rational structural modification of the isatin scaffold to develop new and potent antimicrobial agents targeting bacterial peptidoglycan glycosyltransferase." RSC Advances 11, no. 29 (2021): 18122–30. http://dx.doi.org/10.1039/d1ra02119b.

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9

Biswas, Lalitha, Raja Biswas, Martin Schlag, Ralph Bertram, and Friedrich Götz. "Small-Colony Variant Selection as a Survival Strategy for Staphylococcus aureus in the Presence of Pseudomonas aeruginosa." Applied and Environmental Microbiology 75, no. 21 (August 28, 2009): 6910–12. http://dx.doi.org/10.1128/aem.01211-09.

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ABSTRACT Previously it has been demonstrated that Staphylococcus aureus is sensitive toward Pseudomonas-secreted exotoxins, which preferentially target the electron transport chain in staphylococci. Here it is shown that a subpopulation of S. aureus survives these respiratory toxins of P seudomonas aeruginosa by selection of the small-colony variant (SCV) phenotype. Purified pyocyanin alone causes the same effect. A hem B mutant of S. aureus survives cocultivation with P. aeruginosa without a decrease in CFU.

10

Francius, Grégory, Oscar Domenech, Marie Paule Mingeot-Leclercq, and Yves F. Dufrêne. "Direct Observation of Staphylococcus aureus Cell Wall Digestion by Lysostaphin." Journal of Bacteriology 190, no. 24 (October 3, 2008): 7904–9. http://dx.doi.org/10.1128/jb.01116-08.

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ABSTRACT The advent of Staphylococcus aureus strains that are resistant to virtually all antibiotics has increased the need for new antistaphylococcal agents. An example of such a potential therapeutic is lysostaphin, an enzyme that specifically cleaves the S. aureus peptidoglycan, thereby lysing the bacteria. Here we tracked over time the structural and physical dynamics of single S. aureus cells exposed to lysostaphin, using atomic force microscopy. Topographic images of native cells revealed a smooth surface morphology decorated with concentric rings attributed to newly formed peptidoglycan. Time-lapse images collected following addition of lysostaphin revealed major structural changes in the form of cell swelling, splitting of the septum, and creation of nanoscale perforations. Notably, treatment of the cells with lysostaphin was also found to decrease the bacterial spring constant and the cell wall stiffness, demonstrating that structural changes were correlated with major differences in cell wall nanomechanical properties. We interpret these modifications as resulting from the digestion of peptidoglycan by lysostaphin, eventually leading to the formation of osmotically fragile cells. This study provides new insight into the lytic activity of lysostaphin and offers promising prospects for the study of new antistaphylococcal agents.

11

Leanse, Leon G., Xiaojing Zeng, and Tianhong Dai. "Potentiated antimicrobial blue light killing of methicillin resistant Staphylococcus aureus by pyocyanin." Journal of Photochemistry and Photobiology B: Biology 215 (February 2021): 112109. http://dx.doi.org/10.1016/j.jphotobiol.2020.112109.

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12

Mattsson, Eva, Terese Persson, Pia Andersson, Jan Rollof, and Arne Egesten. "Peptidoglycan Induces Mobilization of the Surface Marker for Activation Marker CD66b in Human Neutrophils but Not in Eosinophils." Clinical Diagnostic Laboratory Immunology 10, no. 3 (May 2003): 485–88. http://dx.doi.org/10.1128/cdli.10.3.485-488.2003.

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ABSTRACT Peptidoglycan from Staphylococcus aureus mobilized CD66b in human neutrophils but did not upregulate surface activation markers in eosinophils. In addition, Toll-like receptor 2, implicated in the recognition of peptidoglycan, was detected on the surface of resting neutrophils but not on eosinophils. These findings suggest roles for neutrophils but not eosinophils in innate recognition of peptidoglycan.

13

Imegwu, Obi, Tsueng H. Chang, Jacob J. Steinberg, and Stanley M. Levenson. "Staphylococcus aureus peptidoglycan ameliorates cyclophosphamide-induced impairment of wound healing." Wound Repair and Regeneration 5, no. 4 (October 1997): 364–72. http://dx.doi.org/10.1046/j.1460-9568.1997.50411.x.

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14

Singh, Vineet K., Mary R. Carlos, and Kuldeep Singh. "Physiological significance of the peptidoglycan hydrolase, LytM, in Staphylococcus aureus." FEMS Microbiology Letters 311, no. 2 (August 25, 2010): 167–75. http://dx.doi.org/10.1111/j.1574-6968.2010.02087.x.

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15

Qiu, Jian-Gian, Stephen Factor, Tsueng H. Chang, David Knighton, Howard Nadel, and Stanley M. Levenson. "Wound Healing: Captopril, an Angiogenesis Inhibitor, and Staphylococcus aureus Peptidoglycan." Journal of Surgical Research 92, no. 2 (August 2000): 177–85. http://dx.doi.org/10.1006/jsre.2000.5839.

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16

Gonzalez-Delgado, Luz S., Hannah Walters-Morgan, Bartłomiej Salamaga, Angus J. Robertson, Andrea M. Hounslow, Elżbieta Jagielska, Izabela Sabała, Mike P. Williamson, Andrew L. Lovering, and Stéphane Mesnage. "Two-site recognition of Staphylococcus aureus peptidoglycan by lysostaphin SH3b." Nature Chemical Biology 16, no. 1 (November 4, 2019): 24–30. http://dx.doi.org/10.1038/s41589-019-0393-4.

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17

WYKE, Anne W., J. Barrie WARD, and Michael V. HAYES. "Synthesis of Peptidoglycan in vivo in Methicillin-Resistant Staphylococcus aureus." European Journal of Biochemistry 127, no. 3 (March 3, 2005): 553–58. http://dx.doi.org/10.1111/j.1432-1033.1982.tb06907.x.

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18

Towhid, Syeda T., Mulugeta Nega, Eva-Maria Schmidt, Evi Schmid, Till Albrecht, Patrick Münzer, Oliver Borst, Friedrich Götz, and Florian Lang. "Stimulation of platelet apoptosis by peptidoglycan from Staphylococcus aureus 113." Apoptosis 17, no. 9 (July 3, 2012): 998–1008. http://dx.doi.org/10.1007/s10495-012-0718-1.

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19

Dörries, Kirsten, Rabea Schlueter, and Michael Lalk. "Impact of Antibiotics with Various Target Sites on the Metabolome of Staphylococcus aureus." Antimicrobial Agents and Chemotherapy 58, no. 12 (September 15, 2014): 7151–63. http://dx.doi.org/10.1128/aac.03104-14.

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ABSTRACTIn this study, global intra- and extracellular metabolic profiles were exploited to investigate the impact of antibiotic compounds with different cellular targets on the metabolome ofStaphylococcus aureusHG001. Primary metabolism was largely covered, yet uncommon staphylococcal metabolites were detected in the cytosol ofS. aureus, including sedoheptulose-1,7-bisphosphate and the UDP-MurNAc-pentapeptide with an alanine-seryl residue. By comparing the metabolic profiles of unstressed and stressed staphylococcal cells in a time-dependent manner, we found far-ranging effects within the metabolome. For each antibiotic compound, accumulation as well as depletion of metabolites was detected, often comprising whole biosynthetic pathways, such as central carbon and amino acid metabolism and peptidoglycan, purine, and pyrimidine synthesis. Ciprofloxacin altered the pool of (deoxy)nucleotides as well as peptidoglycan precursors, thus linking stalled DNA and cell wall synthesis. Erythromycin tended to increase the amounts of intermediates of the pentose phosphate pathway and lysine. Fosfomycin inhibited the first enzymatic step of peptidoglycan synthesis, which was followed by decreased levels of peptidoglycan precursors but enhanced levels of substrates such as UDP-GlcNAc and alanine-alanine. In contrast, vancomycin and ampicillin inhibited the last stage of peptidoglycan construction on the outer cell surface. As a result, the amounts of UDP-MurNAc-peptides drastically increased, resulting in morphological alterations in the septal region and in an overall decrease in central metabolite levels. Moreover, each antibiotic affected intracellular levels of tricarboxylic acid cycle intermediates.

20

Kraus, Dirk, Hubert Kalbacher, Julia Buschmann, Brigitte Berger-Bächi, Friedrich Götz, and Andreas Peschel. "Muropeptide Modification-Amidation of Peptidoglycan d-Glutamate Does Not Affect the Proinflammatory Activity of Staphylococcus aureus." Infection and Immunity 75, no. 4 (January 29, 2007): 2084–87. http://dx.doi.org/10.1128/iai.01576-06.

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ABSTRACT Peptidoglycan muropeptides, potent proinflammatory components, are amidated in Staphylococcus aureus for unknown reasons. To study whether this modification may modulate proinflammatory capacity, cytokine induction by isogenic S. aureus strains with different amidation levels and by synthetic amidated/nonamidated muramyldipeptides was evaluated. However, amidation did not significantly affect cytokine induction. This finding contributes to defining peptidoglycan receptor specificities and indicates that further rationales for muropeptide amidation have to be considered.

21

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.

22

Bera, Agnieszka, Raja Biswas, Silvia Herbert, Emir Kulauzovic, Christopher Weidenmaier, Andreas Peschel, and Friedrich Götz. "Influence of Wall Teichoic Acid on Lysozyme Resistance in Staphylococcus aureus." Journal of Bacteriology 189, no. 1 (November 3, 2006): 280–83. http://dx.doi.org/10.1128/jb.01221-06.

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ABSTRACT Staphylococcus aureus peptidoglycan (PG) is completely resistant to the hydrolytic activity of lysozyme. Here we show that modifications in PG by O acetylation, wall teichoic acid, and a high degree of cross-linking contribute to this resistance.

23

Nasibian, L. S., H. V. Sotkis, O. M. Tzugorko, I. B. Philippov, and Ya M. Shuba. "PEPTIDOGLYCAN OF STAPHYLOCOCCUS AUREUS ALTERS THE MYOMETRIAL CONTRACTILITY OF NON-PREGNANT RATS TROUGH INCREASING INTRACELLULAR CALCIUM LEVELS." Fiziolohichnyĭ zhurnal 66, no. 6 (November 22, 2020): 56–65. http://dx.doi.org/10.15407/fz66.06.056.

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The work is devoted to the study of the effect of Staphylococcus aureus peptidoglycan on the main parameters of myometrial contractions and the mechanism of this influence. The research was carried out by tensometry and calcimetry methods. The results of the experiments demonstrated that peptidoglycan modulates all the main parameters of contractions of the non-pregnant rat uterus, including increasing their amplitude and duration by 10 and 30%, respectively, mainly by prolonging the relaxation phase (56.7 ± 1.6%): myometrial band relative to quickly shrunk and relaxed for a long time. Application of peptidoglycan on freshly isolated uterine myocytes for 5 min led to a periodic increase in their intracellular content of calcium ions. Peptidoglycan enhanced myometrial contractions caused by hyperpotassium solution at a concentration of 60 mmol. Administration of 1 μmol of nifedipine, a blocker of potential-directed L-type calcium channels, suppressed spontaneous contractions enhanced by peptidoglycan. These changes in myometrium contractility of on the background of peptidoglycan action occur not only due to increased transmembrane calcium intake, but also its mobilization from the sarcoplasmic reticulum.

24

Mattsson, Eva, Thomas Hartung, Siegfried Morath, and Arne Egesten. "Highly Purified Lipoteichoic Acid from Staphylococcus aureus Induces Procoagulant Activity and Tissue Factor Expression in Human Monocytes but Is a Weak Inducer in Whole Blood: Comparison with Peptidoglycan." Infection and Immunity 72, no. 7 (July 2004): 4322–26. http://dx.doi.org/10.1128/iai.72.7.4322-4326.2004.

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ABSTRACT Lipoteichoic acid from Staphylococcus aureus was a potent inducer of procoagulant activity in isolated mononuclear cells but not in whole blood. In contrast, staphylococcal peptidoglycan showed equal levels of potency in isolated mononuclear cells and whole blood, suggesting that peptidoglycan is an important inducer of procoagulant activity in severe sepsis involving gram-positive bacteria.

25

Pereira, S. F. F., A. O. Henriques, M. G. Pinho, H. de Lencastre, and A. Tomasz. "Role of PBP1 in Cell Division of Staphylococcus aureus." Journal of Bacteriology 189, no. 9 (February 16, 2007): 3525–31. http://dx.doi.org/10.1128/jb.00044-07.

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ABSTRACT We constructed a conditional mutant of pbpA in which transcription of the gene was placed under the control of an IPTG (isopropyl-β-d-thiogalactopyranoside)-inducible promoter in order to explore the role of PBP1 in growth, cell wall structure, and cell division. A methicillin-resistant strain and an isogenic methicillin-susceptible strain, each carrying the pbpA mutation, were unable to grow in the absence of the inducer. Conditional mutants of pbpA transferred into IPTG-free medium underwent a four- to fivefold increase in cell mass, which was not accompanied by a proportional increase in viable titer. Examination of thin sections of such cells by transmission electron microscopy or fluorescence microscopy of intact cells with Nile red-stained membranes showed a morphologically heterogeneous population of bacteria with abnormally increased sizes, distorted axial ratios, and a deficit in the number of cells with completed septa. Immunofluorescence with an antibody specific for PBP1 localized the protein to sites of cell division. No alteration in the composition of peptidoglycan was detectable in pbpA conditional mutants grown in the presence of a suboptimal concentration of IPTG, which severely restricted the rate of growth, and the essential function of PBP1 could not be replaced by PBP2A present in methicillin-resistant cells. These observations suggest that PBP1 is not a major contributor to the cross-linking of peptidoglycan and that its essential function must be intimately integrated into the mechanism of cell division.

26

Quiblier, Chantal, Agnieszka Luczak-Kadlubowska, Esther Holdener, Daniela Alborn, Tanja Schneider, Imke Wiedemann, Mariana Pinho, et al. "The Staphylococcus aureus Membrane Protein SA2056 Interacts with Peptidoglycan Synthesis Enzymes." Antibiotics 2, no. 1 (January 22, 2013): 11–27. http://dx.doi.org/10.3390/antibiotics2010011.

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27

Wang, X., N. Mani, P. A. Pattee, B. J. Wilkinson, and R. K. Jayaswal. "Analysis of a peptidoglycan hydrolase gene from Staphylococcus aureus NCTC 8325." Journal of Bacteriology 174, no. 19 (1992): 6303–6. http://dx.doi.org/10.1128/jb.174.19.6303-6306.1992.

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28

Snowden, Michael A., and Harold R. Perkins. "Peptidoglycan cross-linking in Staphylococcus aureus. An apparent random polymerisation process." European Journal of Biochemistry 191, no. 2 (July 1990): 373–77. http://dx.doi.org/10.1111/j.1432-1033.1990.tb19132.x.

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29

Jacob, E., L. C. Durham, M. C. Falk, T. J. Williams, and L. J. Wheat. "Antibody response to teichoic acid and peptidoglycan in Staphylococcus aureus osteomyelitis." Journal of Clinical Microbiology 25, no. 1 (1987): 122–27. http://dx.doi.org/10.1128/jcm.25.1.122-127.1987.

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30

Pintar, Sara, Jure Borišek, Aleksandra Usenik, Andrej Perdih, and Dušan Turk. "Interdomain conformational flexibility of the peptidoglycan N-acetylglucosaminidases of Staphylococcus aureus." Acta Crystallographica Section A Foundations and Advances 75, a2 (August 18, 2019): e125-e125. http://dx.doi.org/10.1107/s2053273319094312.

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31

Reikerås, Olav, Jacob E. Wang, Simon J. Foster, and Stein E. Utvåg. "Staphylococcus aureus peptidoglycan impairs fracture healing: An experimental study in rats." Journal of Orthopaedic Research 25, no. 2 (February 2007): 262–66. http://dx.doi.org/10.1002/jor.20274.

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32

Voggu, Lalitha, Steffen Schlag, Raja Biswas, Ralf Rosenstein, Christian Rausch, and Friedrich Götz. "Microevolution of Cytochrome bd Oxidase in Staphylococci and Its Implication in Resistance to Respiratory Toxins Released by Pseudomonas." Journal of Bacteriology 188, no. 23 (December 1, 2006): 8079–86. http://dx.doi.org/10.1128/jb.00858-06.

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ABSTRACT Pseudomonas aeruginosa and Staphylococcus aureus are opportunistic pathogens and frequently coinfect the lungs of cystic fibrosis patients. P. aeruginosa secretes an arsenal of small respiratory inhibitors, like pyocyanin, hydrogen cyanide, or quinoline N-oxides, that may act against the commensal flora as well as host cells. Here, we show that with respect to their susceptibility to these respiratory inhibitors, staphylococcal species can be divided into two groups: the sensitive group, comprised of pathogenic species such as S. aureus and S. epidermidis, and the resistant group, represented by nonpathogenic species such as S. carnosus, S. piscifermentans, and S. gallinarum. The resistance in the latter group of species was due to cydAB genes that encode a pyocyanin- and cyanide-insensitive cytochrome bd quinol oxidase. By exchanging cydB in S. aureus with the S. carnosus-specific cydB, we could demonstrate that CydB determines resistance. The resistant or sensitive phenotype was based on structural alterations in CydB, which is part of CydAB, the cytochrome bd quinol oxidase. CydB represents a prime example of both microevolution and the asymmetric pattern of evolutionary change.

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Gründling, Angelika, and Olaf Schneewind. "Cross-Linked Peptidoglycan Mediates Lysostaphin Binding to the Cell Wall Envelope of Staphylococcus aureus." Journal of Bacteriology 188, no. 7 (April 1, 2006): 2463–72. http://dx.doi.org/10.1128/jb.188.7.2463-2472.2006.

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ABSTRACT Staphylococcus simulans bv. staphylolyticus secretes lysostaphin, a bacteriocin that cleaves pentaglycine cross bridges in the cell wall of Staphylococcus aureus. The C-terminal cell wall-targeting domain (CWT) of lysostaphin is required for selective binding of this bacteriocin to S. aureus cells; however, the molecular target for this was unknown. We used purified green fluorescent protein fused to CWT (GFP-CWT) to reveal species-specific association of the reporter with staphylococci. GFP-CWT bound S. aureus cells as well as purified peptidoglycan sacculi. The addition of cross-linked murein, disaccharides linked to interconnected wall peptides, blocked GFP-CWT binding to staphylococci, whereas murein monomers or lysostaphin-solubilized cell wall fragments did not. S. aureus strain Newman variants lacking the capacity for synthesizing polysaccharide capsule (capFO), poly-N-acetylglucosamine (icaAC), lipoprotein (lgt), cell wall-anchored proteins (srtA), or the glycolipid anchor of lipoteichoic acid (ypfP) bound GFP-CWT similar to wild-type staphylococci. A tagO mutant strain, defective in the synthesis of polyribitol wall teichoic acid attached to the cell wall envelope, displayed increased GFP-CWT binding. In contrast, a femAB mutation, reducing both the amount and the length of peptidoglycan cross-linking (monoglycine cross bridges), showed a dramatic reduction in GFP-CWT binding. Thus, the CWT domain of lysostaphin directs the bacteriocin to cross-linked peptidoglycan, which also serves as the substrate for its glycyl-glycine endopeptidase domain.

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Leemans, Jaklien C., Mirjam Heikens, Kok P. M. van Kessel, Sandrine Florquin, and Tom van der Poll. "Lipoteichoic Acid and Peptidoglycan from Staphylococcus aureus Synergistically Induce Neutrophil Influx into the Lungs of Mice." Clinical Diagnostic Laboratory Immunology 10, no. 5 (September 2003): 950–53. http://dx.doi.org/10.1128/cdli.10.5.950-953.2003.

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ABSTRACT Staphylococcus aureus is an important pathogen in nosocomial pneumonia. Lipoteichoic acid (LTA) and peptidoglycan (PepG) are part of the staphylococcal cell wall. Here we show that LTA and PepG act in synergy to cause polymorphonuclear cell recruitment in the pulmonary compartment during S. aureus pneumonia.

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Balibar, Carl J., Xiaoyu Shen, and Jianshi Tao. "The Mevalonate Pathway of Staphylococcus aureus." Journal of Bacteriology 191, no. 3 (November 21, 2008): 851–61. http://dx.doi.org/10.1128/jb.01357-08.

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ABSTRACT Isoprenoids are a class of ubiquitous organic molecules synthesized from the five-carbon starter unit isopentenyl pyrophosphate (IPP). Comprising more than 30,000 known natural products, isoprenoids serve various important biological functions in many organisms. In bacteria, undecaprenyl pyrophosphate is absolutely required for the formation of cell wall peptidoglycan and other cell surface structures, while ubiquinones and menaquinones, both containing an essential prenyl moiety, are key electron carriers in respiratory energy generation. There is scant knowledge on the nature and regulation of bacterial isoprenoid pathways. In order to explore the cellular responses to perturbations in the mevalonate pathway, responsible for producing the isoprenoid precursor IPP in many gram-positive bacteria and eukaryotes, we constructed three strains of Staphylococcus aureus in which each of the mevalonate pathway genes is regulated by an IPTG (isopropyl-β-d-thiogalactopyranoside)-inducible promoter. We used DNA microarrays to profile the transcriptional effects of downregulating the components of the mevalonate pathway in S. aureus and demonstrate that decreased expression of the mevalonate pathway leads to widespread downregulation of primary metabolism genes, an upregulation in virulence factors and cell wall biosynthetic determinants, and surprisingly little compensatory expression in other isoprenoid biosynthetic genes. We subsequently correlate these transcriptional changes with downstream metabolic consequences.

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Bon, Jon, Nagraj Mani, and R. K. Jayaswal. "Molecular analysis of lytic genes of bacteriophage 80α ofStaphylococcus aureus." Canadian Journal of Microbiology 43, no. 7 (July 1, 1997): 612–16. http://dx.doi.org/10.1139/m97-087.

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Nucleotide sequencing of a 3779-bp fragment of the Staphylococcus aureus bacteriophage 80α revealed two open reading frames: ORF1, designated as lytA, which encodes a polypeptide of 481 amino acids with an apparent Mrof 53.81 kDa; and ORF2, designated as holin, which encodes for a hydrophobic polypeptide of 145 amino acids with an apparent Mrof 15.58 kDa and exhibits two putative transmembrane helices. Both genes showed 100% sequence homology to that of the peptidoglycan hydrolase and holin genes of the S. aureus phage [Formula: see text] reported earlier. In addition, the downstream sequences of the lytA gene were homologous to the phage attachment site (attP) of the phage [Formula: see text]. Based on our data we propose that the lytic system of the phage 80α evolved from that of phage [Formula: see text].Key words: attachment site, bacteriophage 80α, holin, peptidoglycan hydrolase, Staphylococcus aureus.

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Stapleton, Melanie R., Malcolm J. Horsburgh, Emma J. Hayhurst, Lynda Wright, Ing-Marie Jonsson, Andrej Tarkowski, John F. Kokai-Kun, James J. Mond, and Simon J. Foster. "Characterization of IsaA and SceD, Two Putative Lytic Transglycosylases of Staphylococcus aureus." Journal of Bacteriology 189, no. 20 (August 3, 2007): 7316–25. http://dx.doi.org/10.1128/jb.00734-07.

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ABSTRACT Bacterial cell wall peptidoglycan is a dynamic structure requiring hydrolysis to allow cell wall growth and division. Staphylococcus aureus has many known and putative peptidoglycan hydrolases, including two likely lytic transglycosylases. These two proteins, IsaA and SceD, were both found to have autolytic activity. Regulatory studies showed that the isaA and sceD genes are partially mutually compensatory and that the production of SceD is upregulated in an isaA mutant. The expression of sceD is also greatly upregulated by the presence of NaCl. Several regulators of isaA and sceD expression were identified. Inactivation of sceD resulted in impaired cell separation, as shown by light microscopy, and “clumping” of bacterial cultures. An isaA sceD mutant is attenuated for virulence, while SceD is essential for nasal colonization in cotton rats, thus demonstrating the importance of cell wall dynamics in host-pathogen interactions.

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Wu, Julie A., Caroline Kusuma, James J. Mond, and John F. Kokai-Kun. "Lysostaphin Disrupts Staphylococcus aureus and Staphylococcus epidermidis Biofilms on Artificial Surfaces." Antimicrobial Agents and Chemotherapy 47, no. 11 (November 2003): 3407–14. http://dx.doi.org/10.1128/aac.47.11.3407-3414.2003.

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ABSTRACT Staphylococci often form biofilms, sessile communities of microcolonies encased in an extracellular matrix that adhere to biomedical implants or damaged tissue. Infections associated with biofilms are difficult to treat, and it is estimated that sessile bacteria in biofilms are 1,000 to 1,500 times more resistant to antibiotics than their planktonic counterparts. This antibiotic resistance of biofilms often leads to the failure of conventional antibiotic therapy and necessitates the removal of infected devices. Lysostaphin is a glycylglycine endopeptidase which specifically cleaves the pentaglycine cross bridges found in the staphylococcal peptidoglycan. Lysostaphin kills Staphylococcus aureus within minutes (MIC at which 90% of the strains are inhibited [MIC90], 0.001 to 0.064 μg/ml) and is also effective against Staphylococcus epidermidis at higher concentrations (MIC90, 12.5 to 64 μg/ml). The activity of lysostaphin against staphylococci present in biofilms compared to those of other antibiotics was, however, never explored. Surprisingly, lysostaphin not only killed S. aureus in biofilms but also disrupted the extracellular matrix of S. aureus biofilms in vitro on plastic and glass surfaces at concentrations as low as 1 μg/ml. Scanning electron microscopy confirmed that lysostaphin eradicated both the sessile cells and the extracellular matrix of the biofilm. This disruption of S. aureus biofilms was specific for lysostaphin-sensitive S. aureus, as biofilms of lysostaphin-resistant S. aureus were not affected. High concentrations of oxacillin (400 μg/ml), vancomycin (800 μg/ml), and clindamycin (800 μg/ml) had no effect on the established S. aureus biofilms in this system, even after 24 h. Higher concentrations of lysostaphin also disrupted S. epidermidis biofilms.

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de Jonge, B. L., Y. S. Chang, N. Xu, and D. Gage. "Effect of exogenous glycine on peptidoglycan composition and resistance in a methicillin-resistant Staphylococcus aureus strain." Antimicrobial Agents and Chemotherapy 40, no. 6 (June 1996): 1498–503. http://dx.doi.org/10.1128/aac.40.6.1498.

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A highly homogeneously methicillin-resistant Staphylococcus aureus strain was grown in the presence of various concentrations of exogenous glycine. Increasing concentrations of glycine in the medium resulted in a decrease in methicillin resistance and the appearance of a heterogeneous resistance phenotype. Parallel to the gradual changes in resistance was an alteration in the muropeptide composition of peptidoglycan. Increasing concentrations of glycine in the medium resulted in peptidoglycan in which muropeptides with a D-alanyl-D-alanine terminus were replaced with D-alanyl-glycine-terminating muropeptides. The disappearance of D-alanyl-D-alanine-terminating muropeptides in peptidoglycan and the concomitant decrease in resistance indicate a central role for D-alanyl-D-alanine-terminating precursors in methicillin resistance.

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Jones, Carys S., Alexander C. Anderson, and Anthony J. Clarke. "Mechanism of Staphylococcus aureus peptidoglycan O-acetyltransferase A as an O-acyltransferase." Proceedings of the National Academy of Sciences 118, no. 36 (September 3, 2021): e2103602118. http://dx.doi.org/10.1073/pnas.2103602118.

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The O-acetylation of exopolysaccharides, including the essential bacterial cell wall polymer peptidoglycan, confers resistance to their lysis by exogenous hydrolases. Like the enzymes catalyzing the O-acetylation of exopolysaccharides in the Golgi of animals and fungi, peptidoglycan O-acetyltransferase A (OatA) is predicted to be an integral membrane protein comprised of a membrane-spanning acyltransferase-3 (AT-3) domain and an extracytoplasmic domain; for OatA, these domains are located in the N- and C-terminal regions of the enzyme, respectively. The recombinant C-terminal domain (OatAC) has been characterized as an SGNH acetyltransferase, but nothing was known about the function of the N-terminal AT-3 domain (OatAN) or its homologs associated with other acyltransferases. We report herein the experimental determination of the topology of Staphylococcus aureus OatAN, which differs markedly from that predicted in silico. We present the biochemical characterization of OatAN as part of recombinant OatA and demonstrate that acetyl-CoA serves as the substrate for OatAN. Using in situ and in vitro assays, we characterized 35 engineered OatA variants which identified a catalytic triad of Tyr-His-Glu residues. We trapped an acetyl group from acetyl-CoA on the catalytic Tyr residue that is located on an extracytoplasmic loop of OatAN. Further enzymatic characterization revealed that O-acetyl-Tyr represents the substrate for OatAC. We propose a model for OatA action involving the translocation of acetyl groups from acetyl-CoA across the cytoplasmic membrane by OatAN and their subsequent intramolecular transfer to OatAC for the O-acetylation of peptidoglycan via the concerted action of catalytic Tyr and Ser residues.

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Dziarski, Roman, and Dipika Gupta. "Staphylococcus aureus Peptidoglycan Is a Toll-Like Receptor 2 Activator: a Reevaluation." Infection and Immunity 73, no. 8 (August 2005): 5212–16. http://dx.doi.org/10.1128/iai.73.8.5212-5216.2005.

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ABSTRACT Since the ability of peptidoglycan (PGN) to activate Toll-like receptor 2 (TLR2) was recently questioned, we reevaluated activation of TLR2 by PGN. Polymeric soluble or insoluble Staphylococcus aureus PGN, repurified by sodium dodecyl sulfate or phenol extraction, activated TLR2 at 0.1 to 1 or 10 μg/ml, respectively, and induced tumor necrosis factor alpha production. The TLR2 activation by PGN, but not by lipoteichoic acid, was abolished by muramidase digestion. We conclude that polymeric S. aureus PGN is a TLR2 activator.

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Johannsen, L., L. A. Toth, R. S. Rosenthal, M. R. Opp, F. Obal, A. B. Cady, and J. M. Krueger. "Somnogenic, pyrogenic, and hematologic effects of bacterial peptidoglycan." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 258, no. 1 (January 1, 1990): R182—R186. http://dx.doi.org/10.1152/ajpregu.1990.258.1.r182.

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Bacterial infections and certain muramyl peptides elicit a variety of pathophysiological effects including increases in body temperature and slow-wave sleep. Bacterial cell wall peptidoglycan is composed of muramyl peptides. To investigate the ability of isolated bacterial cell walls to enhance slow-wave sleep, rabbits were injected intravenously with cell walls isolated from Staphylococcus aureus or with soluble peptidoglycan prepared from Neisseria gonorrhoeae. These injections increased slow-wave sleep, electroencephalographic delta-wave amplitudes, and body temperature, reduced rapid-eye-movement sleep, and induced neutrophilia and lymphopenia. The somnogenic and pyrogenic effects of S. aureus cell walls developed within 1 h and persisted throughout the recording period. Injections of N. gonorrhoeae peptidoglycan induced similar effects but of larger magnitude and shorter duration. We conclude that peptidoglycan is a bacterial component that mediates the increased sleep observed during infectious disease.

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Tong, Steven Y. C., Frieder Schaumburg, Matthew J. Ellington, Jukka Corander, Bruno Pichon, Fabian Leendertz, Stephen D. Bentley, et al. "Novel staphylococcal species that form part of a Staphylococcus aureus-related complex: the non-pigmented Staphylococcus argenteus sp. nov. and the non-human primate-associated Staphylococcus schweitzeri sp. nov." International Journal of Systematic and Evolutionary Microbiology 65, Pt_1 (January 1, 2015): 15–22. http://dx.doi.org/10.1099/ijs.0.062752-0.

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We define two novel species of the genus Staphylococcus that are phenotypically similar to and have near identical 16S rRNA gene sequences to Staphylococcus aureus . However, compared to S. aureus and each other, the two species, Staphylococcus argenteus sp. nov. (type strain MSHR1132T = DSM 28299T = SSI 89.005T) and Staphylococcus schweitzeri sp. nov. (type strain FSA084T = DSM 28300T = SSI 89.004T), demonstrate: 1) at a whole-genome level considerable phylogenetic distance, lack of admixture, average nucleotide identity <95 %, and inferred DNA–DNA hybridization <70 %; 2) different profiles as determined by MALDI-TOF MS; 3) a non-pigmented phenotype for S. argenteus sp. nov.; 4) S. schweitzeri sp. nov. is not detected by standard nucA PCR; 5) distinct peptidoglycan types compared to S. aureus ; 6) a separate ecological niche for S. schweitzeri sp. nov.; and 7) a distinct clinical disease profile for S. argenteus sp. nov. compared to S. aureus .

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Boyle-Vavra, Susan, Harald Labischinski, Christine C. Ebert, Kerstin Ehlert, and Robert S. Daum. "A Spectrum of Changes Occurs in Peptidoglycan Composition of Glycopeptide-Intermediate Clinical Staphylococcus aureus Isolates." Antimicrobial Agents and Chemotherapy 45, no. 1 (January 1, 2001): 280–87. http://dx.doi.org/10.1128/aac.45.1.280-287.2001.

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ABSTRACT The mechanism of glycopeptide resistance in Staphylococcus aureus is not known with certainty. Because the target of vancomycin is the d-Ala–d-Ala terminus of the stem peptide of the peptidoglycan precursor, by subjecting muropeptides to reversed-phase high-performance liquid chromatography, we investigated peptidoglycan obtained from glycopeptide-intermediateS. aureus (GISA) isolates for changes in composition and evaluated whether any peptidoglycan structural change was a consistent feature of clinical GISA isolates. GISA isolates Mu50 and Mu3 from Japan had the large glutamate-containing monomeric peak demonstrated previously, although strain H1, a vancomycin-susceptible MRSA isolate from Japan that was clonally related to Mu3 and Mu50, and afemC mutant that we studied, did also. For the U.S. GISA isolates, strain NJ had a large monomeric peak with a retention time identical to that described for the glutamate-containing monomer in strains H1, Mu3, and Mu50. However, a much smaller corresponding peak was seen in GISA MI, and this peak was absent from both GISA PC and a recent GISA isolate obtained from an adult patient in Illinois (strain IL). These data suggest that a uniform alteration in peptidoglycan composition cannot be discerned among the GISA isolates and indicate that a single genetic or biochemical change is unlikely to account for the glycopeptide resistance phenotype in the clinical GISA isolates observed to date. Furthermore, a large monomeric glutamate-containing peak is not sufficient to confer the resistance phenotype.

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Zhao, Wei-Hua, Zhi-Qing Hu, Sachie Okubo, Yukihiko Hara, and Tadakatsu Shimamura. "Mechanism of Synergy between Epigallocatechin Gallate and β-Lactams against Methicillin-Resistant Staphylococcus aureus." Antimicrobial Agents and Chemotherapy 45, no. 6 (June 1, 2001): 1737–42. http://dx.doi.org/10.1128/aac.45.6.1737-1742.2001.

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ABSTRACT Compared to MICs (more than 800 μg/ml) of (−)-epigallocatechin gallate (EGCg) against Escherchia coli, MICs of EGCg against methicillin-susceptible and methicillin-resistantStaphylococcus aureus (MSSA and MRSA) were 100 μg/ml or less. Furthermore, less than 25 μg EGCg per ml obviously reversed the high level resistance of MRSA to all types of tested β-lactams, including benzylpenicillin, oxacillin, methicillin, ampicillin, and cephalexin. EGCg also induced a supersusceptibility to β-lactams in MSSA which does not express mecA, encoding penicillin-binding protein 2′ (PBP2′). The fractional inhibitory concentration (FIC) indices of the tested β-lactams against 25 isolates of MRSA were from 0.126 to 0.625 in combination with 6.25, 12.5 or 25 μg of EGCg per ml. However, no synergism was observed between EGCg and ampicillin against E. coli. EGCg largely reduced the tolerance of MRSA and MSSA to high ionic strength and low osmotic pressure in their external atmosphere, indicating damage of the cell wall. Unlike dextran and lipopolysaccharide, peptidoglycan fromS. aureus blocked both the antibacterial activity of EGCg and the synergism between EGCg and oxacillin, suggesting a direct binding of EGCg with peptidoglycan on the cell wall. EGCg showed a synergistic effect with dl-cycloserine (an inhibitor of cell wall synthesis unrelated to PBP2′) but additive or indifferent effect with inhibitors of protein and nuclear acid synthesis. EGCg did not suppress either PBP2′ mRNA expression or PBP2′ production, as confirmed by reverse transcription-PCR and a semiquantitative PBP2′ latex agglutination assay, indicating an irrelevance between the synergy and PBP2′ production. In summary, both EGCg and β-lactams directly or indirectly attack the same site, peptidoglycan on the cell wall. EGCg synergizes the activity of β-lactams against MRSA owing to interference with the integrity of the cell wall through direct binding to peptidoglycan.

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Périchon, Bruno, and Patrice Courvalin. "VanA-Type Vancomycin-Resistant Staphylococcus aureus." Antimicrobial Agents and Chemotherapy 53, no. 11 (June 8, 2009): 4580–87. http://dx.doi.org/10.1128/aac.00346-09.

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ABSTRACT Since 2002, nine methicillin (meticillin)-resistant Staphylococcus aureus (MRSA) strains that are also resistant to vancomycin (VRSA) have been reported in the United States, including seven clinical isolates from Michigan. The strains harbor a plasmid-borne Tn1546 element following conjugation from a glycopeptide-resistant Enterococcus strain. In the second step, Tn1546 transposed to a resident plasmid in five strains; the acquired plasmid behaved as a suicide gene delivery vector, and the incoming DNA had been rescued by illegitimate recombination. Surprisingly, combination of a glycopeptide with a β-lactam has a strong synergistic effect against VRSA, both in vitro and in an animal model, despite resistance of the strains to both drug classes when administered separately. This results from the fact that the late peptidoglycan precursors ending in d-alanine-d-lactate (d-Ala-d-Lac) that are mainly synthesized in the presence of glycopeptide inducers are not substrates for PBP2′, which is the only transpeptidase that remains active in the presence of oxacillin. One VRSA strain is partially dependent on vancomycin for growth due to a mutation in the host d-Ala:d-Ala ligase, thus having to rely on the inducible resistance pathway for cell wall synthesis. Competition growth experiments in the absence of inducer between the MRSA recipient and isogenic VRSA transconjugant revealed a disadvantage for the transconjugant, accounting, in part, for the low level of dissemination of the VRSA clinical isolates. The association of multiple molecular and environmental factors has been implicated in the regional emergence of VRSA in Michigan.

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Feng, Bai-Sui, Shao-Heng He, Peng-Yuan Zheng, Linda Wu, and Ping-Chang Yang. "Mast Cells Play a Crucial Role in Staphylococcus aureus Peptidoglycan-Induced Diarrhea." American Journal of Pathology 171, no. 2 (August 2007): 537–47. http://dx.doi.org/10.2353/ajpath.2007.061274.

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Henze, U., T. Sidow, J. Wecke, H. Labischinski, and B. Berger-Bächi. "Influence of femB on methicillin resistance and peptidoglycan metabolism in Staphylococcus aureus." Journal of Bacteriology 175, no. 6 (1993): 1612–20. http://dx.doi.org/10.1128/jb.175.6.1612-1620.1993.

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Wang, Jacob E., Maria K. Dahle, Arne Yndestad, Inge Bauer, Michelle C. McDonald, Pål Aukrust, Simon J. Foster, Michael Bauer, Ansgar O. Aasen, and Christoph Thiemermann. "Peptidoglycan of Staphylococcus aureus causes inflammation and organ injury in the rat*." Critical Care Medicine 32, no. 2 (February 2004): 546–52. http://dx.doi.org/10.1097/01.ccm.0000109775.22138.8f.

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Reichmann, Nathalie T., Andreia C. Tavares, Bruno M. Saraiva, Ambre Jousselin, Patricia Reed, Ana R. Pereira, João M. Monteiro, et al. "SEDS–bPBP pairs direct lateral and septal peptidoglycan synthesis in Staphylococcus aureus." Nature Microbiology 4, no. 8 (May 13, 2019): 1368–77. http://dx.doi.org/10.1038/s41564-019-0437-2.

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