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Relevant bibliographies by topics / Pyocyanin, Staphylococcus aureus peptidoglycan

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Academic literature on the topic 'Pyocyanin, Staphylococcus aureus peptidoglycan'

Author: Grafiati

Published: 4 June 2021

Last updated: 14 February 2022

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

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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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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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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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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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.

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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.

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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.

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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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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.

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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.

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Dissertations / Theses on the topic "Pyocyanin, Staphylococcus aureus peptidoglycan"

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Lund, Victoria A. "Peptidoglycan dynamics in Staphylococcus aureus using super-resolution microscopy." Thesis, University of Sheffield, 2016. http://etheses.whiterose.ac.uk/13652/.

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Pereira, Pedro Matos. "Peptidoglycan assembly machines: The Staphylococcus aureus Penicillin-Binding Proteins." Doctoral thesis, Universidade Nova de Lisboa. Instituto de Tecnologia Química e Biológica, 2013. http://hdl.handle.net/10362/10884.

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Dissertation presented to obtain the Ph.D degree in Biology
The bacterial cell wall (CW) is of critical importance to cell viability. Impairment of CW synthesis or integrity rapidly leads to cell lysis and death. As there is no equivalent structure to the bacterial CW in mammalian cells, many important antibiotics target the enzymes responsible for its synthesis. The scaffold of the CW consists of the polymer peptidoglycan (PGN), a meshlike structure composed of glycan strands cross‐linked by short peptides. The final steps of PGN synthesis are catalysed by the penicillin‐binding proteins (PBPs), which assemble lipid‐linked disaccharide peptide precursors of PGN into high molecular weight oligomers via transglycosylation and transpeptidation reactions. These proteins have been proposed to work in multi‐enzyme complexes that would also include CW hydrolases.(...)

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Alorabi, J. A. "Role of peptidoglycan deacetylase in Staphylococcus aureus virulence and survival." Thesis, University of Liverpool, 2016. http://livrepository.liverpool.ac.uk/3002567/.

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Staphylococcus aureus is an opportunist human pathogen that colonises the anterior nares and is shed onto skin. The bacterium is most frequently a cause of skin and soft-tissue infections, yet is also a major cause of respiratory, urinary tract, bone, eye and brain infections. Evolution of the bacterium has selected strains that are more antibiotic resistant, particularly in the hospital environment and more recently in the community. The pathogen has the capacity for secreting a wide range of proteins that contribute to survival from host immunity and competing microflora. The bacterial cell wall is a vital structural polymer serving mechanical roles to protect bacteria from osmotic challenges and it serves as a scaffold for the attachment of many anchored proteins and anionic polymers for interaction with extracellular components. Peptidoglycan of S. aureus is modified by enzyme catalysed decoration of N-acetyl muramic acid with teichoic acid and O-acetylation which promotes lysozyme resistance. Further modification of teichoic acid engenders properties linked to colonisation and survival during the life-cycle. This research study sought to assign roles of S. aureus secreted proteins of unknown function using bioinformatics. From this approach the study identified a peptidoglycan deacetylase (Pgd) and this enzyme catalyses a reduction in acetylation of N-acetyl glucosamine in biosynthesis of the cell wall. An allelic replacement mutant revealed altered muropeptide composition that was consistent with its proposed N-deacetylase activity, and transmission electron microscopy (TEM) revealed a reduction in cell wall thickness. S. aureus pgd exhibited increased surface charge to influence a range of phenotypes, including autolysis, resistance and biofilm formation. Resistance was increased to lysozyme, and most notably there was rescue of the lysozyme sensitivity phenotype of an oatA mutant (lacking peptidoglycan O-acetyltransferase [oatA] activity). Hydrodynamic flow biofilm assay revealed that both S. aureus pgd and oatA mutants exhibited negligible biofilm formation on a glass surface; treatment of the surface with plasma fluid increased biofilm capability. Biofilms of S. aureus pgd cultured in static conditions revealed an opposite phenotype with a thicker, but loosely adherent biofilm. Confocal laser scanning microscopy (CSLM) combined with viability staining it was revealed that in the biofilm, there were increased dead cells compared with wild-type. An increased lag phase of growth of S. aureus pgd was identified, and quantitative label free proteomics was used to determine that multiple metabolism and cell wall proteins were differentially expressed, compared with the wild-type strain. The proteome analysis revealed that the pgd mutant expressed increased levels of the lytic transglycosylase, IsaA and this might explain the biofilm phenotype. Further contributions to the biofilm phenotype could be due to decreased expression of protein A and reduced pyruvate metabolism enzymes. S. aureus pgd was killed more rapidly in an opsonophagocytosis assay compared with its isogenic parent but showed equivalent levels of complement deposition and serum survival. Infection models of pneumonia and bacteraemia were tested and revealed reduced bacterial loads for lung and kidney, respectively. The S. aureus pgd mutant phenotype requires further study and it should provide insights into cell wall structure and function. Pgd could represent a future candidate vaccine antigen due to its likely cell surface exposure and contribution to key cellular processes.

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Qiao, Yuan. "Reconstitution of the Final Step of Peptidoglycan Assembly in Staphylococcus aureus." Thesis, Harvard University, 2016. http://nrs.harvard.edu/urn-3:HUL.InstRepos:33493392.

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Bacterial peptidoglycan (PG) is an exoskeleton structure that maintains cell shape and protects cells from lysis. Peptidoglycan is essential in bacteria but is not found in mammalian cells. Therefore, it is the target for several classes of antibiotics, including the beta-lactam family. Beta-lactams target the transpeptidase (TP) domain of penicillin-binding proteins (PBPs), the enzymes responsible for the final step of peptidoglycan biosynthesis. Mutations of transpeptidases in Staphylococcus aureus (S. aureus) have been implicated in beta-lactam resistance in the clinic (commonly known as MRSA infections). Despite the fact that PBPs are important antibiotic targets, there have been no direct assays to monitor their enzymatic activity, primarily due to inaccessibility to appropriate substrates. The PG precursor, Lipid II, is required to study transpeptidase activity. Lipid II contains a glycopeptide attached to a pyrophosphate lipid containing 55 carbons. It has poor physical properties and is present in low abundance in bacteria. This thesis describes the reconstitution of peptidoglycan assembly in Staphylococcus aureus by the essential Class A PBP, PBP2. This was enabled by several key advances, which are also described. The first advance is the discovery that PBP4, a low-molecular weight PBP in S. aureus, can use a Lipid II analogue as a transpeptidation substrate. It can incorporate biotin-D-Lys (BDL) and other non-canonical D-amino acids into the terminal position of the stem peptide in Lipid II. BDL labeling of Lipid II with S. aureus PBP4 has enabled the second advance: the direct detection of native Lipid II extracted from bacteria. This has facilitated elucidation of cellular mechanisms of antibiotics that target cell wall biosynthesis. The third advance is a general strategy to accumulate and isolate native Lipid II in bacteria in useful quantities. Access to substantial quantities of native S. aureus Lipid II has enabled reconstitution of PBP2 transpeptidase activity, as well as characterization of several beta-lactam antibiotics by monitoring enzymatic inhibition. In sum, this work establishes important tools for studying enzymatic mechanisms of bacterial transpeptidases and for characterizing inhibitors that target bacterial peptidoglycan biosynthesis.
Chemical Biology

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Wang, Hsin Jayaswal Radheshyam K. Wilkinson Brian J. "Molecular analysis of a Staphylococcus aureus gene encoding a peptidoglycan hydrolase activity." Normal, Ill. Illinois State University, 1991. http://wwwlib.umi.com/cr/ilstu/fullcit?p9219089.

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Thesis (Ph. D.)--Illinois State University, 1991.
Title from title page screen, viewed January 5, 2006. Dissertation Committee: Radheshyam K. Jayaswal, Brian J. Wilkinson (co-chairs), Herman E. Brockman, Anthony J. Otsuka, Hou Tak Cheung. Includes bibliographical references (leaves 117-129) and abstract. Also available in print.

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Dorling, Jack. "Peptidoglycan recycling in the Gram-positive bacterium Staphylococcus aureus and its role in host-pathogen interaction." Thesis, University of Oxford, 2018. http://ora.ox.ac.uk/objects/uuid:3fc4f926-296d-43a1-bb45-af9f37a87d8d.

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Bacteria are enclosed by a peptidoglycan sacculus, an exoskeleton-like polymer composed of glycan strands cross-linked by short peptides. The sacculus surrounds the cell in a closed bag-like structure and forms the main structural component of the bacterial cell wall. As bacteria grow and divide, cell wall remodelling by peptidoglycan hydrolases results in the release of peptidoglycan fragments from the sacculus. In Gram-negative bacteria, these fragments are efficiently trapped and recycled. Gram-positive bacteria however shed large quantities of peptidoglycan fragments into the environment. For nearly five decades, Gram-positive bacteria were thus assumed not to recycle peptidoglycan and this process has remained enigmatic until recently. In this thesis, the occurrence and physiological role of peptidoglycan recycling in the Gram-positive pathogen Staphylococcus aureus was investigated. S. aureus is an important pathogen, and is becoming increasingly resistant to many antibiotics. Through bioinformatic and experimental means it was determined that S. aureus may potentially recycle components of peptidoglycan and novel peptidoglycan recycling components were identified and characterised. Though disruption of putative peptidoglycan recycling in S. aureus appears not affect growth or gross morphology of this bacterium, potential roles for peptidoglycan recycling in cell wall homeostasis and in virulence were identified. This is to my knowledge the first demonstration of a potential role of peptidoglycan recycling in either of these aspects of bacterial physiology in any Gram-positive bacterium. This is an important step forward in understanding the basic biology of Gram-positive bacteria, and in understanding the mechanisms of virulence in S. aureus. Future study of this process in S. aureus and other Gram-positive bacteria promises to reveal yet further facets of this process and its functions, potentially leading to the identification of novel therapeutic approaches to combat infections.

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Sandhu, Sandeep. "Development of an antibody-based assay for methicillin resistant Staphylococcus aureus using synthetic peptidoglycan precursors." Thesis, University of Warwick, 2010. http://wrap.warwick.ac.uk/36857/.

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Methicillin-resistant Staphylococcus aureus (MRSA) are isolates of the bacterium Staphylococcus aureus that have acquired genes encoding antibiotic resistance to all penicillins, including methicillin and other narrow-spectrum β- lactamase-resistant penicillin antibiotics. Outbreaks of MRSA occur quite frequently as there is no quick screening test for the presence of MRSA. The aim of this project is to try and develop an antibody based detection test for rapid detection of MRSA, which could help in the prevention of outbreaks. An antigen (UDP-MurNAc-L-Ala-γ-D-Glu-L-Lys(ε-NH2-Gly)5-D-Ala-D-Ala) that resembles the outer surface of the Staphylococcus aureus (contains a Gly5 moiety that is specific for S. aureus) cell wall peptidoglycan has been prepared, and attached to a carrier protein. Sheep antibodies raised against this antigen were screened using ELISA assays. The results showed that antibodies did have specificity for the antigen. Cell walls were prepared from several different bacteria, including two MRSA and one methicillin-sensitive Staphylococcus aureus (MSSA) strain. ELISA assays using these cell walls showed that the antibodies had specificity for cell walls containing (Gly)5 in the order of S aureus (Gly5) > S. simulans (less Gly5) > S. pneumoniae (no Glyn) > E. coli (no Glyn, Gram-negative strain). A particularly high response was observed for one of the two MRSA strains, detectable at 0.1 μg of cell wall. An HPLC-based UV-Vis assay was developed to monitor the activity of peptidoglycan polymerisation enzymes from S. aureus, while preparing polymeric peptidoglycan as an antigen for immunisation. Several intermediates in peptidoglycan polymerisation were detected using S. aureus monofunctional glycosyltransferase (MGT), which allowed us to propose a new hypothesis for the early steps of peptidoglycan transglycosylation.

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Lee, Yoon-Ik Wilkinson Brian J. Jayaswal Radheshyam K. "Cloning of a Staphylococcus aureus peptidoglycan hydrolase gene, and purification and characterization of the gene product." Normal, Ill. Illinois State University, 1993. http://wwwlib.umi.com/cr/ilstu/fullcit?p9323735.

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Thesis (Ph. D.)--Illinois State University, 1993.
Title from title page screen, viewed February 13, 2006. Dissertation Committee: Brian J. Wilkinson, Radheshyam K. Jayaswal (co-chairs), Anthony E. Liberta, Herman E. Brockman, Hou Tak Cheung. Includes bibliographical references (leaves 115-124) and abstract. Also available in print.

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Roberts, Erin. "Cytokine expression, cytoskeleton organization, and viability of SIM-A9 microglia exposed to Staphylococcus aureus-derived lipoteichoic acid and peptidoglycan." Wright State University / OhioLINK, 2017. http://rave.ohiolink.edu/etdc/view?acc_num=wright1515329731281897.

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Blake, Katy Louise. "Characterisation of MurA and MurZ in staphylococcus aureus: Their role in peptidoglycan bisynthesis and potential as targets for novel inhibitors." Thesis, University of Leeds, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.494156.

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Books on the topic "Pyocyanin, Staphylococcus aureus peptidoglycan"

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Esmaily, Farhad. The immunological properties of peptidoglycan and other cell wall fractions of staphylococcus aureus. Birmingham: University of Birmingham, 1990.

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Book chapters on the topic "Pyocyanin, Staphylococcus aureus peptidoglycan"

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Herzog, Ch, V. Just, R. Berger, and M. Just. "Problems with 'Teichoic Acid" Antigen Used in Staphylococcus aureus Serology." In Biological Properties of Peptidoglycan, edited by Peter H. Seidl and Karl H. Schleifer, 113–20. Berlin, Boston: De Gruyter, 1986. http://dx.doi.org/10.1515/9783110874297-017.

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Loos, Michael, Peter H. Seidl, and K. H. Schleifer. "Teichoic Acid-Free Peptidoglycan Of Staphylococcus Aureus RM 59 Does Not Activate Complement." In Biological Properties of Peptidoglycan, edited by Peter H. Seidl and Karl H. Schleifer, 319–28. Berlin, Boston: De Gruyter, 1986. http://dx.doi.org/10.1515/9783110874297-039.

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Christensson, B. "The Diagnostic Value Of Antibodies To Peptidoglycan And Other Staphylococcus Aureus Antigens In Serious Staphylococcal Infections." In Biological Properties of Peptidoglycan, edited by Peter H. Seidl and Karl H. Schleifer, 21–36. Berlin, Boston: De Gruyter, 1986. http://dx.doi.org/10.1515/9783110874297-004.

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de Jonge, Boudewijn L. M., and Alexander Tomasz. "The Muropeptide Composition of the Peptidoglycan of Staphylococcus aureus Determined with Reversed-Phase High Performance Liquid Chromatography." In Bacterial Growth and Lysis, 77–82. Boston, MA: Springer US, 1993. http://dx.doi.org/10.1007/978-1-4757-9359-8_9.

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