The structure of the ribitol teichoic acid of Staphylococcus aureus H

Baddiley, J.; Buchanan, J. G.; Hardy, F. E.; Martin, R; RajBhandary, Uttam L.; Sanderson, Arnold R.

doi:10.1016/0006-3002(61)90699-0

Cited by 57 publications

(19 citation statements)

References 8 publications

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“…For example, Staphylococcus aureus H contains D-alanyl-[␣,␤-GlcNAc-poly(Rbo-P)] glycosylated on position 4 of the D-ribitol in either an ␣-or ␤-linkage ( Fig. 2C) (38,40). S. aureus Copenhagen contains this WTA with 15% ␣-and 85% ␤-GlcNAc-poly(Rbo-P) WTA (430).…”

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

896

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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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

896

1,097

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“…Together with the abundant peptidoglycan polymers that make up the matrix of the cell wall, WTA and LTA represent the major determinants of the net (-) charge of the Gram-positive bacterial surface and cell wall (31). In S. aureus , the WTA and LTA polymers are comprised of repeating units of ribitol (WTA) or glycerol (LTA) phosphate (32, 33). Together, WTA and LTA form a negatively charged lattice bridging the cell membrane through the cell wall (31).…”

Section: Actions Of Purified Spla2-iia Against Gram-positive Bacteriamentioning

confidence: 99%

Molecular determinants of bacterial sensitivity and resistance to mammalian Group IIA phospholipase A2

Weiss

2015

Biochimica et Biophysica Acta (BBA) - Biomembranes

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Group IIA secretory phospholipase A2 (sPLA2-IIA) of mammalian species is unique among the many structurally and functionally related mammalian sPLA2 in their high net positive charge and potent (nM) antibacterial activity. Toward the Gram-positive bacteria tested thus far, the global cationic properties of sPLA2-IIA are necessary for optimal binding to intact bacteria and penetration of the multi-layered thick cell wall, but not for the degradation of membrane phospholipids that is essential for bacterial killing. Various Gram-positive bacterial species can differ as much as 1000-fold in sPLA2-IIA sensitivity despite similar intrinsic enzymatic activity of sPLA2-IIA toward the membrane phospholipids of the various bacteria. D-alanylation of wall- and lipo-teichoic acids in Stapylococcus aureus and sortase function in Streptococcus pyogenes increase bacterial resistance to sPLA2-IIA by up to 100-fold apparently by affecting translocation of bound sPLA2-IIA to the cell membrane. Action of the sPLA2-IIA and other related sPLA2 against Gram-negative bacteria is more dependent on cationic properties of the enzyme near the amino-terminus of the protein and collaboration with other host defense proteins that produce alterations of the unique Gram-negative bacterial outer membrane that normally represents a barrier to sPLA2-IIA action.

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“…With the exception of some unusual strains, it is considered that WTAs in S. aureus are composed of ribitol phosphate repeating units, while LTAs are polyglycerolphosphate chains (Endl et al, 1983;Vinogradov et al, 2006). Both polymers have a highly variable content of D-alanine ester substitutions that reduce the net negative charge of TAs by introduction of basic amino groups (Baddiley et al, 1961;Fischer, 1994;Neuhaus & Baddiley, 2003). The absence of D-alanine esters in dltA mutants of S. aureus causes a deficiency in their capacity to form biofilms on polystyrene or glass surfaces (Gross et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

Wall teichoic acids are dispensable for anchoring the PNAG exopolysaccharide to the Staphylococcus aureus cell surface

et al. 2008

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Biofilm formation in Staphylococcus aureus is usually associated with the production of the poly-N-acetylglucosamine (PNAG) exopolysaccharide, synthesized by proteins encoded by the icaADBC operon. PNAG is a linear b-(1-6)-linked N-acetylglucosaminoglycan that has to be partially deacetylated and consequently positively charged in order to be associated with bacterial cell surfaces. Here, we investigated whether attachment of PNAG to bacterial surfaces is mediated by ionic interactions with the negative charge of wall teichoic acids (WTAs), which represent the most abundant polyanions of the Gram-positive bacterial envelope. We generated WTA-deficient mutants by in-frame deletion of the tagO gene in two genetically unrelated S. aureus strains. The DtagO mutants were more sensitive to high temperatures, showed a higher degree of cell aggregation, had reduced initial adherence to abiotic surfaces and had a reduced capacity to form biofilms under both steady-state and flow conditions. However, the levels as well as the strength of the PNAG interaction with the bacterial cell surface were similar between DtagO mutants and their corresponding wild-type strains. Furthermore, double DtagO DicaADBC mutants displayed a similar aggregative phenotype to that of single DtagO mutants, indicating that PNAG is not responsible for the aggregative behaviour observed in DtagO mutants. Overall, the absence of WTAs in S. aureus had little effect on PNAG production or anchoring to the cell surface, but did affect the biofilm-forming capacity, cell aggregative behaviour and the temperature sensitivity/stability of S. aureus.

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The structure of the ribitol teichoic acid of Staphylococcus aureus H

Cited by 57 publications

References 8 publications

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

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

Molecular determinants of bacterial sensitivity and resistance to mammalian Group IIA phospholipase A2

Wall teichoic acids are dispensable for anchoring the PNAG exopolysaccharide to the Staphylococcus aureus cell surface

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