Six complexes of vancomycin and peptidoglycan precursors were studied via molecular dynamics simulations. The interactions between the antibiotic and peptidoglycan fragments were identified and described in detail. All six studied modifications of the peptidoglycan precursor resulted in a weakening of the interaction with vancomycin when comparing to the native D-Ala-D-Ala-terminated fragment. It was confirmed that the N-terminus of the vancomycin is directly responsible for peptidoglycan recognition and antimicrobial activity. In simulated systems, the saccharide part of the antibiotic interacts with peptide precursors, thus it could also be important for antimicrobial activity. The complex terminated with D-Lac is the only one in which there is a weak interaction with the sugar moiety in the simulated systems. Analysis of conformational changes is a major scope of this work. The lack of interactions resulting from modification of the peptidoglycan precursors (D-Lac, D-Ser or other ...
TY - CHAP. T1 - Peptidoglycan Recognition Proteins and Lysozyme. AU - Dziarski, Roman. AU - Royet, Julien. AU - Gupta, Dipika. PY - 2016/4/27. Y1 - 2016/4/27. N2 - Peptidoglycan recognition proteins (PGRPs or PGLYRPs) are evolutionarily conserved innate immunity molecules homologous to bacteriophage type 2 amidases. Mammalian PGRPs are soluble secreted proteins and bind muramyl peptide fragments of bacterial peptidoglycan. Mammalian PGLYRP1, PGLYRP3, and PGLYRP4 are directly bactericidal and kill bacteria by inducing an exaggerated envelope stress response, which causes oxidative, thiol, and metal stress, membrane depolarization, inhibition of biosynthetic reactions, and bacterial death. Mammalian PGLYRP2 is an enzyme, peptidoglycan amidohydrolase. In vivo, mammalian PGRPs maintain a healthy gut microbiome, which protects animals from experimental colitis. Mammalian PGRPs also modulate sensitivity to skin and joint inflammation and allergic asthma. Human PGRP variants are associated with ...
The peptidoglycan sacculus, or cell wall, is what defines bacterial cell shape. Cell wall composition can be best characterized at the molecular level by digesting the peptidoglycan murein polymer into its muropeptide subunits and quantifying the abundance of muropeptides using high-pressure liquid chromatography. Certain features of the cell wall including muropeptide composition, glycan strand length, degree of crosslinking, type of crosslinking and other peptidoglycan modifications can be quantified using this approach. Well-established protocols provide us with highly-resolved and quantitatively reproducible chromatographic data, which can be used to investigate bacterial cell wall composition under a variety of environmental or genetic perturbations. The method described here enables the purification of muropeptide samples, their quantification by HPLC, and fraction collection for peak identification by mass spectrometry. Although the methods for peptidoglycan purification and HPLC analysis have
Bacterial peptidoglycans were first identified in the 1940s. The nucleotide precursors were isolated and characterized in 1949. Peptidoglycan biosynthesis has been investigated in many bacterial species. The glycan chains of peptidoglycan are small and repeated units composed of N-acetylglucosamine (GlcNAc) and N-acetylmuramic acid (MurNAc). The glmM gene was shown to be essential in Escherichia coli, but genetic data recently suggested that in Staphylococcus aureus there could be an alternative pathway for glucosamine-1-phosphate biosynthesis. The GlmU protein from E. coli is a bifunctional enzyme. Its C-terminal domain catalyzes acetylation of glucosamine-1-phosphate into GlcNAc-1-phosphate, whereas its N-terminal domain catalyzes uridylation to yield UDP-GlcNAc. Nucleoside antibiotics can be subdivided into different classes according to their chemical structures and/or their respective modes of action against MraY: the tunicamycin group, the ribosamino-uridine group, and finally the capuramycin
The peptidoglycan monomers are synthesized in the cytosol and are then attached to a membrane carrier bactoprenol. Bactoprenol transports peptidoglycan monomers across the cell membrane where they are inserted into the existing peptidoglycan.[11] In the first step of peptidoglycan synthesis, the glutamine, which is an amino acid, donates an amino group to a sugar, fructose 6-phosphate. This turns fructose 6-phosphate into glucosamine-6-phosphate. In step two, an acetyl group is transferred from acetyl CoA to the amino group on the glucosamine-6-phosphate creating N-acetyl-glucosamine-6-phosphate.[12] In step three of the synthesis process, the N-acetyl-glucosamine-6-phosphate is isomerized, which will change N-acetyl-glucosamine-6-phosphate to N-acetyl-glucosamine-1-phosphate.[12] In step 4, the N-acetyl-glucosamine-1-phosphate, which is now a monophosphate, attacks UTP. Uridine triphosphate, which is a pyrimidine nucleotide, has the ability to act as an energy source. In this particular ...
The biosynthesis of bacterial cell wall peptidoglycan is a complex process involving many different steps taking place in the cytoplasm (synthesis of the nucleotide precursors) and on the inner and outer sides of the cytoplasmic membrane (assembly and polymerization of the disaccharide-peptide monomer unit, respectively). This review summarizes the current knowledge on the membrane steps leading to the formation of the lipid II intermediate, i.e. the substrate of the polymerization reactions. It makes the point on past and recent data that have significantly contributed to the understanding of the biosynthesis of undecaprenyl phosphate, the carrier lipid required for the anchoring of the peptidoglycan hydrophilic units in the membrane, and to the characterization of the MraY and MurG enzymes which catalyze the successive transfers of the N-acetylmuramoyl-peptide and N-acetylglucosamine moieties onto the carrier lipid, respectively. Enzyme inhibitors and antibacterial compounds interfering with ...
The yet uncharacterized membrane protein SA2056 belongs to the ubiquitous RND (Resistance-Nodulation-cell Division) family of transmembrane efflux transporters. The sa2056 gene is located downstream of femX, the gene encoding the essential, non-ribosomal peptidyl-transferase adding the first glycine in the staphylococcal cell wall pentaglycine interpeptide. Due to its proximity to and weak co-transcription with femX, we assumed that sa2056 may somehow be involved in peptidoglycan synthesis. Specific antibodies against SA2056 showed that this protein is expressed during growth and present in the membrane fraction of cell preparations. Using a bacterial two hybrid system, SA2056 was shown to interact (i) with itself, (ii) with FemB, which adds glycines 4 and 5 to the peptidoglycan interpeptide and (iii) with the essential penicillin binding proteins, PBP1 and PBP2, required for cell division and incorporation of the peptidoglycan into the cell wall. Unexpectedly, deletion of sa2056 led to no phenotype
We have investigated the interaction of soluble peptidoglycan (sPG), in comparison with lipopolysaccharide (LPS), with human mononuclear cells (MNC) by determining the capacity of sPG to induce interleukin-6 (IL-6) and IL-1 release. In addition, we investigated the modulation of their interaction by anti-CD14 monoclonal antibody and by partial structures of LPS. We found that sPG, like LPS, was able to induce IL-6 and IL-1 production by MNC. However, dose-response experiments revealed that at least 3,000 ng of sPG per ml was necessary for induction, whereas the optimal LPS concentration was 1 ng/ml. Anti-CD14 monoclonal antibody reduced sPG- and LPS-induced IL-6 and IL-1 production. Moreover, partial structures of LPS were able to reduce monokine production induced by sPG and LPS. We conclude that sPG constitutes, like LPS, an inflammatory cytokine inducer and that CD14 is involved in the activation of human monocytes not only by LPS but also by sPG. ...
en] A review with 95 refs. The assembly of the bacterial cell wall peptidoglycan relies upon the availability of a ready-made precursor, the lipid II intermediate. This intermediate is taken up by a multifunctional factory that provides the required enzymic activities for polymer assembly at the exterior of the plasma membrane. Morphogenetic networks regulate the synthesis in a cell-cycle-dependent fashion. As essential components of the cell machinery are targets of β-lactam antibiotics, safety devices protect the cells against these toxic agents. Controversy and consensus formation lie at the heart of the scientific research. This review focuses on questions that bacterial cell wall biochemists still strive, with increasing success, to answer. [on SciFinder(R ...
title: Clustering of peptidoglycan recognition protein-SA is required for sensing lysine-type peptidoglycan in insects, doi: 10.1073/pnas.0610924104, category: Article
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Peptidoglycan is a macromolecule made of long aminosugar strands cross-linked by short peptides. It forms the cell wall in bacteria surrounding the cytoplasmic membrane. The glycan strands are typically comprised of repeating N-acetylglucosamine (GlcNAc) and N-acetylmuramic acid (MurNAc) disaccharides. Each MurNAc is linked to a peptide of three to five amino acid residues. Disaccharide subunits are first assembled on the cytoplasmic side of the bacterial membrane on a polyisoprenoid anchor (lipid I and II). Polymerization of disaccharide subunits by transglycosylases and cross-linking of glycan strands by transpeptidases occur on the other side of the membrane. Bacterial cell wall biosynthesis inhibitors form a major class of antibiotics ...
Peptidoglycan is a macromolecule made of long aminosugar strands cross-linked by short peptides. It forms the cell wall in bacteria surrounding the cytoplasmic membrane. The glycan strands are typically comprised of repeating N-acetylglucosamine (GlcNAc) and N-acetylmuramic acid (MurNAc) disaccharides. Each MurNAc is linked to a peptide of three to five amino acid residues. Disaccharide subunits are first assembled on the cytoplasmic side of the bacterial membrane on a polyisoprenoid anchor (lipid I and II). Polymerization of disaccharide subunits by transglycosylases and cross-linking of glycan strands by transpeptidases occur on the other side of the membrane. Bacterial cell wall biosynthesis inhibitors form a major class of antibiotics ...
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Innate immunity is an ancient defense system that distinguishes between self and non self and is present in both vertebrates and invertebrates. Peptidoglycan (PGN), a cell wall component shared by both gram-negative and gram-positive bacteria, is the major recognition molecule for the detection of bacteria in Drosophila. Peptidoglycan Recognition Proteins (PGRPs) are conserved from insect to mammals and bind PGN with high affinity. In Drosophila, distinct PGRPs provide essential signals upstream of the Toll and Imd pathways. This thesis concerns the recognition of PGN by PGRPs and the expression of antibacterial peptides from the Imd pathway.. The PGRP-LC locus encodes three splice forms, a, x, and y. PGRP-LCx and PGRP-LCa form heterodimers in the presence of monomeric PGN. We propose a model for activation of Imd where PGRP-LCx binds to monomeric PGN leading to dimerization with PGRP-LCa and activation of the Imd pathway. With polymeric PGN, PGRP-LCx dimers activate the Imd pathway.. Drosophila ...
A wall-plus-membrane preparation from a Bacillus licheniformis mutant incorporated radioactivity from a peptidoglycan precursor in which the free amino group of diaminopimelic acid was blocked by 14C-labelled acetyl group. This incorporation was penicillin-sensitive. The enzymically degraded product contained cross-linked dimers, showing that newly synthesized peptidoglycan chains had been cross-linked to the pre-existing cell wall.. ...
Yahashiri, A., Jorgenson, M. A. & Weiss, D. S. (2017). The SPOR Domain, a Widely Conserved Peptidoglycan Binding Domain That Targets Proteins to the Site of Cell Division. J Bacteriol, 199(14), e00118-17. PMID: 28396350.. Ransom, E. M., Weiss, D. S. & Ellermeier, C. D. (2016). Use of mCherryOpt Fluorescent Protein in Clostridium difficile. Methods Mol Biol, 1476, 53-67. PMID: 27507333.. Yahashiri, A., Jorgenson, M. A. & Weiss, D. S. (2015). Bacterial SPOR domains are recruited to septal peptidoglycan by binding to glycan strands that lack stem peptides. Proc Natl Acad Sci U S A, 112(36), 11347-52. PMID: 26305949.. Weiss, D. S. (2015). Last but not least: new insights into how FtsN triggers constriction during Escherichia coli cell division. (Vols. 95). (6), pp. 903-9. Mol Microbiol. PMID: 25571948.. Ransom, E. M., Ellermeier, C. D. & Weiss, D. S. (2015). Use of mCherry Red fluorescent protein for studies of protein localization and gene expression in Clostridium difficile. Appl Environ ...
Pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria. Has bactericidal activity towards Gram-positive bacteria. May kill Gram-positive bacteria by interfering with peptidoglycan biosynthesis. Binds also to Gram-negative bacteria, and has bacteriostatic activity towards Gram-negative bacteria. Plays a role in innate immunity ...
El Centro Nacional de Biotecnología es un centro estratégico del Consejo Superior de Investigaciones Científicas con un objetivo mixto académico y de transferencia de tecnología en el área de la Biotecnología.
The action of vancomycin and teicoplanin depends on their ability to bind specifically to the terminal D-alanyl-D-alanine group on the peptide side chain of the membrane-bound intermediates in peptidoglycan synthesis. Bacitracin was isolated in 1943 from a strain of a Bacillus sp., which was originally classified as Bacillus subtilis but now is known as Bacillus licheniformis. Binding of bacitracin prevents the enzymatic dephosphorylation of the lipid carrier molecule to its monophosphate form, a reaction which occurs during the second stage of peptidoglycan biosynthesis. Bacitracin is highly active against most gram-positive bacteria, particularly Staphylococcus aureus and Streptococcus pyogenes. Vancomycin binds reversibly to the D-Ala-D-Ala dipeptide segment of the muramyl pentapeptide present in peptidoglycan monomers which are exposed at the external cell surface of the cytoplasmic membrane. The dimeric structure of vancomycin is held together by four hydrogen bonds between the two amide backbones.
The Brown lab is interested in understanding the principles that govern bacterial morphology, a readily observable facet of microbial cell biology. One of the major unsolved questions in microbiology is how bacteria generate specific shapes. Bacteria exhibit an amazing diversity of shapes and sizes that are precisely reproduced at every generation, indicating that morphology plays an important role in the life of these bacteria. Impressive progress has been made in the past few years in understanding the mechanism of cell shape determination in a few model bacterial systems, including the discovery that bacteria possess a cytoskeleton, but we are still very far having a comprehensive understanding of how bacterial morphologies are generated. The Brown lab takes advantage of recent technical advances in microscopy, construction of fluorescent fusion proteins, and a gene depletion strategy, to make strides in understanding how bacteria generate specific morphologies.. In most bacteria, the cell ...
Reed, P, Atilano ML, Alves R, Hoiczyk E, Sher X, Reichmann NT, Pereira PM, Roemer T, Filipe SR, Pereira-Leal JB, Ligoxygakis P, Pinho MG. 2015. Staphylococcus aureus survives with a minimal peptidoglycan synthesis machinery but sacrifices virulence and antibiotic resistance. PLoS Pathogens. 11:e1004891 ...
Bacteria cell walls are composed of Peptidoglycan, which create rigidity of the cell wall, determine cell shape, and help prevent osmotic lysis. The bacteria cell wall, like most lipid bilayers, is porous and semipermeable. Gram positive bacteria have a very thick peptidoglycan layer and therefore, when dyed during gram staining, retain the crystal violet dye. Gram negative bacteria have a thin peptidoglycan layer which results in an inability to retain the crystal violet dye during gram staining. Peptidoglycan, also known as murein, is composed of alternating units of N-acetylmuramic acid (NAM) and N-acetylglucosamine (NAG). NAM is essentially a molecule of NAG onto which a lactyl group has been added to C3 via phosphoenol pyruvate; it is a signature molecule of bacteria. A pentapeptide chain is attached to the lactyl group during the NAM-NAG unit formation inside the bacteria. Generally, this pentapeptide chain consists of, in order: L-ala-D-Glu-mDAP/L-Lys-D-ala-D-ala. Once the NAG-NAM complex ...
Wang, L, Weber AN, Atilano ML, Filipe SR, Gay NJ, Ligoxygakis P. 2006. Sensing of Gram-positive bacteria in Drosophila: GNBP1 is needed to process and present peptidoglycan to PGRP-SA. EMBO J. 25:5005-5014 ...
The peptidoglycan layer is a unique and essential structural element in the cell wall of most bacteria (Peptidoglycan structure and architecture. FEMS Microbiology Reviews, 08 Jan 2008). Made of glycan strands cross-linked by short peptides, the so-called peptidoglycan sacculus forms a closed, bag-shaped structure surrounding the cytoplasmic membrane. Peptidoglycan sacculi have the strength to withstand…
To maintain cellular structure and integrity during division, Gram-negative bacteria must carefully coordinate constriction of a tripartite cell envelope of inner membrane, peptidoglycan (PG), and outer membrane (OM). It has remained enigmatic how this is accomplished. Here, we show that envelope machines facilitating septal PG synthesis (PBP1B-LpoB complex) and OM constriction (Tol system) are physically and functionally coordinated via YbgF, renamed CpoB (Coordinator of PG synthesis and OM constriction, associated with PBP1B). CpoB localizes to the septum concurrent with PBP1B-LpoB and Tol at the onset of constriction, interacts with both complexes, and regulates PBP1B activity in response to Tol energy state. This coordination links PG synthesis with OM invagination and imparts a unique mode of bifunctional PG synthase regulation by selectively modulating PBP1B cross-linking activity. Coordination of the PBP1B and Tol machines by CpoB contributes to effective PBP1B function in vivo and maintenance of
Vertical scaffold model.Recently, a novel scaffold model for murein structure was proposed (20, 21), in which the glycan strands extend perpendicular from the cytoplasmic membrane and are cross-linked by peptides that are parallel to the surface of the membrane (Fig. 2, left side). The 1,6-anhydro-MurNAc ends of the glycans were assumed to be located near the cytoplasmic membrane in a region of high cross-linkage, whereas the GlcNAc ends were located close to the outer membrane in a poorly cross-linked region. According to the authors who proposed this model, the murein almost completely fills the periplasmic space. However, several experimental findings do not fit the scaffold model, as discussed below.. E. coli contains about 3.5 × 106 molecules of m-Dap per cell, which are present in murein consisting of glycan strands that are, on average, 25 to 35 disaccharides long. If an average of 30 disaccharides is used, this yields a total number of 3.5 × 106/30 or 1.17 × 105 glycan strands. ...
Despite decades of study, an understanding of how the peptidoglycan network is assembled with a robustly maintained micron-scale shape and size has remained elusive. In this work, we introduce a model of rod-shaped cell growth that we use to investigate the roles of spatial regulation of peptidoglycan synthesis, biochemical properties of glycan strands, and mechanical stretching during insertion. Our studies reveal that rod shape maintenance requires insertion to be insensitive to fluctuations in cell-wall density and stress, and that a helical pattern of insertion is sufficient for elongation without significant loss of shape. In addition, we present evidence that left-handed chirality of the cytoskeleton in Escherichia coli gives rise to a global, right-handed chiral ordering of the cell wall. Local, MreB-guided insertion of material into the peptidoglycan network naturally orders the glycan strands and causes cells to twist left-handedly during elongational growth. Through comparison with the ...
Bacillus subtilis spores are encased in a multiprotein coat that surrounds an underlying peptidoglycan layer, the cortex. How the connection between the two layers is enforced is not well established. Here, we elucidate the role of the peptidoglycan-binding LysM domain, present in two proteins, SafA and SpoVID, that govern the localization of additional proteins to... ...
Peptidoglycan (PG) is an essential macromolecular sacculus surrounding most bacteria. It is assembled by the glycosyltransferase (GTase) and transpeptidase (TPase) activities of multinodular penicillin-binding proteins (PBPs) within specialized multiprotein complexes, elongasome and divisome. These complexes include in addition of PG synthases, PG hydrolases lipid II precursor flippase and regulatory proteins that communicate by dynamic protein-protein interactions. These processes are essential and constitute validated or potential antibiotic targets.. We use biochemical and structural approaches to study the interaction, activity and structure of the proteins and complexes with the aim to understand the molecular mechanism of peptidoglycan synthesis and cell division. The results could help in the development of therapeutics solutions to combat resistant pathogens.. ...
The peptidoglycan (murein) sacculus is a unique and essential structural element in the cell wall of most bacteria. Made of glycan strands cross‐linked by ...
epithelial cells by means of a complex terminal organelle at the tip of one end of the organism. Cytoadherence is mediated by interactive adhesins and accessory proteins clustered on this organelle. After extracellular attachment, M. pneumoniae causes injury to host respiratory tissue. The mechanism of injury is thought to be mediated by the production of hydrogen peroxide and of a recently identified ADP-ribosylating and vacuolating cytotoxin of M. pneumoniae that has many similarities to pertussis toxin. Because mycoplasmas lack a cell wall, they also lack cell wall-derived stimulators of the innate immune system, such as lipopolysaccharide, lipoteichoic acid, and murein (peptidoglycan) fragments. However, lipoproteins from the mycoplasmal cell membrane appear to have inflammatory properties, probably acting through Toll-like receptors (primarily TLR2) on macrophages and other cells. Lung ...
Bacterial infection is a major threat to human health. Although pathogenic bacteria vary in their virulence, it has been recognized that many pathogenic bacteria share common mechanisms when attacking host cells and tissues. Some pathogenic bacteria synthesize and secrete polysaccharides to form an extracellular capsule. Capsules serve as virulence determinants by multiple mechanisms including facilitation of bacterial adherence, evasion of the immune response, and antibiotic resistance [1]. Moreover, to the exterior of bacterial plasma membranes are certain toxic components (e.g., lipopolysaccharide (LPS) in Gram-negative bacteria, and peptidoglycan fragments and teichoic acids in Gram-positive bacteria) that play key roles in causing bacterial septic shock or multiple organ dysfunction [2]. Significantly, bacteria may secrete proteinaceous or non-proteinaceous molecules, namely exotoxins, capable of directly destroying host cells. The Repeat-in-Toxin (RTX) family is a group of virulence-associated
James A. Schouten; Sangeev Bagga; Adrian J. Lloyd; Gianfranco de Pascale; Christopher G. Dowson; David I. Roper; and Timothy D. H. Bugg. Fluorescent reagents for in vitro studies of lipid-linked steps of bacterial peptidoglycan biosynthesis: derivatives of UDPMurNAc-pentapeptide containing D-cysteine at position 4 or 5. Mol. BioSyst. 2006, 2484-491.. Shu-Li Yo; and Jeffery W. Kelly.Total Synthesis of Dendroamide A:? Oxazole and Thiazole Construction Using an Oxodiphosphonium Salt. J. Org. Chem. 2003, 66 (24), 9506-9509.. ...
Gene target information for PGRP-LB - Peptidoglycan recognition protein LB (fruit fly). Find diseases associated with this biological target and compounds tested against it in bioassay experiments.
Corresponds to family 2 of the peptidoglycan lytic transglycosylases described by N.T. Blackburn and A.J. Clarke (2001) J. Mol. Evol. 52, 78- ...
I am a graduate student earning my Ph.D. in Chemistry at Caltech. I received a Bachelor of Science in Chemistry at the University of Wisconsin, Madison, in 2012. As an undergraduate, I worked in the Gellman group on X-ray crystallographic characterization of the Pin1 WW domain, which is a small tertiary structure that is useful to study β-sheet folding, using a racemic mixture of the Pin1 WW. I also worked to help solve and refine two crystal structures of α- and α/β-peptide inhibitors, each involved in a HIV protein gp41-mimetic helix bundle. Currently in the Clemons lab, I am working on structural and functional characterization of enzymes involved in the N-linked glycosylation and peptidoglycan biosynthesis pathways ...
Ein. Consequently, MAG_5040 could be a critical pathogenic contributor to M. agalactiae persistence by providing essential nucleotide precursors for
The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits ...
The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits ...
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Cell structureCell envelopeBiosynthesis and degradation of murein sacculus and peptidoglycancell shape determining protein, MreB/Mrl family (TIGR00904; HMM-score: 39.7) ...
Cell structureCell envelopeBiosynthesis and degradation of murein sacculus and peptidoglycanD-alanine--D-alanine ligase (TIGR01205; EC 6.3.2.4; HMM-score: 41.9) ...
Hæmmer bakteriernes evne til at syntetisere det mukopolypeptid (peptidoglycan), der indgår som en væsentlig bestanddel af bakteriens cellevæg. Under påvirkning af penicillin vil bakterier i vækstfasen få stadigt svagere cellevæg. De kan ikke dele sig, men svulmer op pga. det høje osmotiske tryk inde i cellen, og til sidst sprænges de og dør ...
Hæmmer bakteriernes evne til at syntetisere det mukopolypeptid (peptidoglycan), der indgår som en væsentlig bestanddel af bakteriens cellevæg. Under påvirkning af penicillin vil bakterier i vækstfasen få stadigt svagere cellevæg. De kan ikke dele sig, men svulmer op pga. det høje osmotiske tryk inde i cellen, og til sidst sprænges de og dør ...
Peptidoglycan recognition proteins (PGRPs) are pattern recognition molecules of innate immunity. In this study, a long-form PGRP, designated as gcPGRP6, was identified from grass carp Ctenopharyngodon idella. The deduced amino acid sequence of gcPGRP6 is composed of 464 residues with a conserved PGRP domain at the C-terminus. The gcPGRP6 gene consists of four exons and three introns, spacing approximately 2.7 kb of genomic sequence. Phylogenetic analysis demonstrated that gcPGRP6 is clustered closely with zebrafish PGLYRP6, and formed a long-type PGRP subfamily together with PGLYRP2 members identified in teleosts and mammals. Real-time PCR and Western blotting analyses revealed that gcPGRP6 is constitutively expressed in organs/tissues examined, and its expression was significantly induced in liver and intestine of grass carp in response to PGN stimulation and in CIK cells treated with lipoteichoic acid (LTA), polyinosinic polycytidylic acid (Poly I:C) and peptidoglycan (PGN). Immunofluorescence ...
Although not truly unique, the cell walls of Archaea are unusual. Whereas peptidoglycan is a standard component of all bacterial cell walls, all archaeal cell walls lack peptidoglycan,[42] though some methanogens have a cell wall made of a similar polymer called pseudopeptidoglycan.[13] There are four types of cell wall currently known among the Archaea. One type of archaeal cell wall is that composed of pseudopeptidoglycan (also called pseudomurein). This type of wall is found in some methanogens, such as Methanobacterium and Methanothermus.[43] While the overall structure of archaeal pseudopeptidoglycan superficially resembles that of bacterial peptidoglycan, there are a number of significant chemical differences. Like the peptidoglycan found in bacterial cell walls, pseudopeptidoglycan consists of polymer chains of glycan cross-linked by short peptide connections. However, unlike peptidoglycan, the sugar N-acetylmuramic acid is replaced by N-acetyltalosaminuronic acid,[42] and the two sugars ...
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TY - JOUR. T1 - Micrococci and peptidoglycan activate TLR2 →Myd88 →IRAK→TRAF→NIK→IKK→NF-κB signal transduction pathway that induces transcription of interleukin-8. AU - Wang, Q.. AU - Dziarski, R.. AU - Kirschning, C. J.. AU - Muzio, M.. AU - Gupta, D.. PY - 2001/4/5. Y1 - 2001/4/5. N2 - This study was done to elucidate the signal transduction pathway of interleukin-8 (IL-8) induction by gram-positive bacteria. Bacteria (micrococci) and peptidoglycan (PGN) induced transcription of IL-8 in HEK293 cells expressing Toll-like receptor 2 (TLR2) and CD14 but not in those expressing TLR1 or TLR4. A mutation within the NF-κB site in the IL-8 promoter abrogated transcriptional induction of IL-8 by the two stimulants. Dominant negative myeloid differentiation protein (MyD88), IL-1 receptor-associated kinase (IRAK), NFκB-inducing kinase (NIK), and IκB kinase (IKK) mutant forms completely inhibited micrococcus- and PGN-induced activation of NF-κB and expression of the gene for IL-8. ...