Biosynthesis of wall tiechoic acids in Staphylococcus aureus H, <i>Micrococcus varians and Bacillus subtilis</i> W23

Harrington, Charles R.; Baddiley, J.

doi:10.1111/j.1432-1033.1985.tb09348.x

Cited by 36 publications

(22 citation statements)

References 35 publications

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“…Teichoic acid (19) and surface-associated proteins (26,30) are first synthesized in vivo in the form of the corresponding biosynthetic precursors, which are closely related to the precursors of murein biosynthesis (39). These precursors could concomitantly participate in cell wall assembly, i.e., teichoic acid and surface-associated proteins could become attached to murein in the course of its assembly.…”

Section: Discussionmentioning

confidence: 99%

Tertiary Structure of Staphylococcus aureus Cell Wall Murein

et al. 2004

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Staphylococcus aureus is an important human pathogen that causes life-threatening diseases including septicemia, endocarditis, toxic shock syndrome, and abscesses in organ tissues (15,25). The cell wall of the microorganism plays an important role in infectivity and pathogenicity (40). Over several decades of research, extensive knowledge has accumulated concerning epidemiology (9), virulence (25, 28), genetics (3), genomic evolution (14), the biochemistry of cell wall assembly (31), the crystal structures of ␤-lactam-resistant enzymes (24), the ultrastructure of the cell wall (4, 18), and the muropeptide composition of wild-type, methicillin-resistant (7), and vancomycinresistant strains (34). Nonetheless, the tertiary molecular structure of the cell wall, which is central for understanding cell growth and division in staphylococci, has remained elusive. As a consequence, there is no graphic illustration of the wall architecture in the literature that adequately represents known physicochemical details of staphylococcal peptidoglycan.Staphylococci are gram-positive bacteria, and their cell walls are composed of murein (32, 38, 41), teichoic acids (2), and wall-associated surface proteins (20,26,30). Stress-bearing murein represents a continuous macromolecular sacculus covering the whole cell. Murein consists of glycan strands, which are cross-linked by peptide bridges furnishing the structural integrity of the sacculus. It is a distinctive feature of staphylococci that the observed degree of murein cross-linking, which was determined as a ratio of bridged peptides to the total amount of all peptide ends in general, is extremely high, on the order of 80 to 90% (16, 35).Glycan strands in staphylococcal murein are composed of N-acetylglucosamine (GlcpNAc) and N-acetylmuramic acid (MurpNAc) residues that furnish ␤-(134)-linked disaccharide repeating units, with MurpNAc representing the reducing terminus of the chain. The carboxyl group of each MurpNAc residue is amidated by the stem pentapeptide L-Ala-D-isoGln-L-Lys-D-Ala-D-Ala, and the ε-amino group of the lysine residue is substituted with a pentaglycine appendage (37). Thus, each peptide attached to a MurpNAc residue is a branched decapeptide with an amino group on the Gly and a carboxyl group on the D-Ala terminus, and arms of the peptide side chains interact with each other to provide a high degree of murein cross-linking. Although the general principle of murein structural organization is simple, the muropeptide composition of the staphylococcal sacculi appears very complex, as a standard digestion of sacculi with muramidase (the enzyme that cleaves MurpNAc glycosidic bonds) releases more than 20 distinct components plus an unresolved material. The latter makes up about 50 to 60% of the muropeptide-containing oligomers, with up to 20 repeating units (7,38). Thus, the major part of staphylococcal murein architecture could be envisaged as being constructed of interlinked glycan and oligopeptide chains, both varying in their lengths.On electron micrographs, the ...

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Section: Discussionmentioning

confidence: 99%

Tertiary Structure of Staphylococcus aureus Cell Wall Murein

et al. 2004

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“…The assembly of WTA requires four phases: (i) synthesis of the (Gro-P) 3 -ManNAc-GlcNAc-PP-polyprenol carrier (linkage unit carrier) (9,200,201,502), (ii) polymerization of the poly(alditol-P) on this lipid intermediate (78,154,183,198,205,294,326,431), (iii) glycosylation of this moiety (184), and (iv) attachment of the WTA linkage unit to peptidoglycan. Undecaprenol phosphate is the carrier lipid on which this linkage intermediate is assembled prior to attachment (69,201,502).…”

Section: Pathways Of Lta and Wta Biosynthesismentioning

confidence: 99%

“…WTA is attached to peptidoglycan via the linkage unit (Gro-P) 2 or 3 ManNAc(␤1-4)GlcNAc-P to C-6 of the MurNAc residues ( Fig. 2A) (9,102,205,273).…”

Section: Structures Of Wta and Ltamentioning

confidence: 99%

A Continuum of Anionic Charge: Structures and Functions ofd-Alanyl-Teichoic Acids in Gram-Positive Bacteria

Neuhaus

Baddiley

2003

Microbiol Mol Biol Rev

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1,097

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SUMMARY Teichoic acids (TAs) are major wall and membrane components of most gram-positive bacteria. With few exceptions, they are polymers of glycerol-phosphate or ribitol-phosphate to which are attached glycosyl and d-alanyl ester residues. Wall TA is attached to peptidoglycan via a linkage unit, whereas lipoteichoic acid is attached to glycolipid intercalated in the membrane. Together with peptidoglycan, these polymers make up a polyanionic matrix that functions in (i) cation homeostasis; (ii) trafficking of ions, nutrients, proteins, and antibiotics; (iii) regulation of autolysins; and (iv) presentation of envelope proteins. The esterification of TAs with d-alanyl esters provides a means of modulating the net anionic charge, determining the cationic binding capacity, and displaying cations in the wall. This review addresses the structures and functions of d-alanyl-TAs, the d-alanylation system encoded by the dlt operon, and the roles of TAs in cell growth. The importance of dlt in the physiology of many organisms is illustrated by the variety of mutant phenotypes. In addition, advances in our understanding of d-alanyl ester function in virulence and host-mediated responses have been made possible through targeted mutagenesis of dlt. Studies of the mechanism of d-alanylation have identified two potential targets of antibacterial action and provided possible screening reactions for designing novel agents targeted to d-alanyl-TA synthesis.

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“…GlmU, the final enzyme required to convert D-fructose-6-phosphate to UDP-N-acetylglucosamine, utilizes acetyl-CoA for the acetylation of glucosamine-1-phosphate (26). Furthermore, UDP-N-acetylglucosamine is a precursor to teichoic acid(s) in Gram-positive bacteria (19) and lipid A in Gram-negative bacteria (4), both of which are surface-exposed molecules that impact the permeability of the bacterial cell. Finally, the majority of Gram-positive pathogens, including Staphylococcus aureus, Enterococcus faecalis, and Streptococcus pneumoniae, utilize the mevalonate pathway for isoprenoid biosynthesis.…”

mentioning

confidence: 99%

Pantethine Rescues Phosphopantothenoylcysteine Synthetase and Phosphopantothenoylcysteine Decarboxylase Deficiency in Escherichia coli but Not in Pseudomonas aeruginosa

Balibar¹,

Hollis-Symynkywicz²,

Tao³

2011

J Bacteriol

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Coenzyme A (CoA) plays a central and essential role in all living organisms. The pathway leading to CoA biosynthesis has been considered an attractive target for developing new antimicrobial agents with novel mechanisms of action. By using an arabinose-regulated expression system, the essentiality of coaBC, a single gene encoding a bifunctional protein catalyzing two consecutive steps in the CoA pathway converting 4-phosphopantothenate to 4-phosphopantetheine, was confirmed in Escherichia coli. Utilizing this regulated coaBC strain, it was further demonstrated that E. coli can effectively metabolize pantethine to bypass the requirement for coaBC. Interestingly, pantethine cannot be used by Pseudomonas aeruginosa to obviate coaBC. Through reciprocal complementation studies in combination with biochemical characterization, it was demonstrated that the differential characteristics of pantethine utilization in these two microorganisms are due to the different substrate specificities associated with endogenous pantothenate kinase, the first enzyme in the CoA biosynthetic pathway encoded by coaA in E. coli and coaX in P. aeruginosa.

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Biosynthesis of wall tiechoic acids in Staphylococcus aureus H, Micrococcus varians and Bacillus subtilis W23

Cited by 36 publications

References 35 publications

Tertiary Structure of Staphylococcus aureus Cell Wall Murein

Tertiary Structure of Staphylococcus aureus Cell Wall Murein

A Continuum of Anionic Charge: Structures and Functions ofd-Alanyl-Teichoic Acids in Gram-Positive Bacteria

Pantethine Rescues Phosphopantothenoylcysteine Synthetase and Phosphopantothenoylcysteine Decarboxylase Deficiency in Escherichia coli but Not in Pseudomonas aeruginosa

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