Direction of Chain Extension during the Biosynthesis of Teichoic Acids in Bacterial Cell Walls

Hussey, Helen; Brooks, D. E.; Baddiley, J.

doi:10.1038/221665a0

Cited by 24 publications

(10 citation statements)

References 9 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…On the other hand, Fiedler et al (1974) were unable to find any evidence for involvement of a polyprenol phosphate intermediate in the synthesis of the wall teichoic acids of Bacillus subtilis and Staphylococcus aureus. The direction of chain extension of a bacterial cell wall polymer containing a repeating unit of D-glycerol 1-phosphate attached to the 3-position of N-acetylglucosamine 1-phosphate (Staphylococcus lactis 13) and another made up of N-acetylglucosamine 1-phosphate units (S. lactis 2102) has also been studied (Hussey et al, 1969). In each case chain extension occurred in the same direction as in the synthesis of the B. subtilis polymer (Kennedy & Shaw, 1968).…”

Section: Discussionmentioning

confidence: 99%

The direction of glycan synthesis in a bacterial peptidoglycan

Ward¹,

Perkins²

1973

Biochemical Journal

View full text Add to dashboard Cite

A cell-free membrane preparation from a poorly lytic mutant of Bacillus licheniformis was used to synthesize radioactive peptidoglycan. The product was apparently un-cross-linked. When UDP-N-acetyl[(14)C]glucosamine was used and the final peptidoglycan subjected to Smith degradation, no radioactive glycerol was found. On the other hand, when peptidoglycan labelled with meso-diamino[(14)C]pimelic acid was first hydrolysed in 0.1m-HCl at 60 degrees C for 2h and then subjected to alkaline conditions, radioactive lactyl-peptides were eliminated. The proportion of radioactive lactyl-peptide decreased with increasing time of incorporation. It is concluded that the glycan chains grow by extension at their reducing ends while remaining attached by some linkage labile to mild acid, such as a glycosyl link to undecaprenol pyrophosphate.

show abstract

Section: Discussionmentioning

confidence: 99%

The direction of glycan synthesis in a bacterial peptidoglycan

Ward¹,

Perkins²

1973

Biochemical Journal

View full text Add to dashboard Cite

show abstract

“…lactis 2102 is a simple linear polymer. Its biosynthesis is accomplished by membrane-bound enzymes and proceeds by transfer of Nacetylglucosamine 1-phosphate residues from UDP-N-acetylglucosamine to a lipid intermediate and thence to the non-reducing terminal end of the growing chain (Hussey et al, 1969). It resembles teichoic acid in being rich in phosphate groups and it may serve a similar role in the uptake of metal ions, although it differs from teichoic acids in not possessing D-alanyl ester residues, the presence of which in teichoic acids can substantially influence their Mg2+binding capacity (Heptinstall et al, 1970).…”

Section: Discussionmentioning

confidence: 99%

A polymer of N-acetylglucosamine 1-phosphate in the wall of Staphylococcus lactis 2102

Archibald

Stafford

1972

Biochemical Journal

View full text Add to dashboard Cite

1. Walls of Staphylococcus lactis 2102 contain about 40% of a phosphorylated polysaccharide, which was isolated by extraction with cold trichloroacetic acid, with dilute NaOH, and also by digestion with a Flavobacterium peptidase. 2. The purified polymer contained equimolar proportions of N-acetylglucosamine and phosphate as its sole constituents and was readily hydrolysed under gentle acidic conditions to N-acetylglucosamine 6-phosphate. 3. Studies on the intact polymer showed that it is linear and that adjacent acetamido sugar units are joined by phosphodiester bonds between their 1- and 6-positions, the glycosidic linkages having the alpha-configuration. This polymer is thus the simplest of the known microbial wall polymers possessing sugar 1-phosphate linkages. 4. Alkali degradation of the extracted polymer proceeds predominantly in a stepwise manner from the reducing end, but evidence was obtained for the direct hydrolysis of some of the inter-unit phosphodiester groups.

show abstract

“…This lipid is identical to that involved in peptidoglycan synthesis (490). Chain elongation in WTA assembly occurs by successive addition of monomer from either CDP-glycerol or CDP-ribitol to the terminal alditol-P that is distal to the linkage unit (235,259).…”

Section: Pathways Of Lta and Wta Biosynthesismentioning

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

900

1,097

View full text Add to dashboard Cite

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.

show abstract

Direction of Chain Extension during the Biosynthesis of Teichoic Acids in Bacterial Cell Walls

Cited by 24 publications

References 9 publications

The direction of glycan synthesis in a bacterial peptidoglycan

The direction of glycan synthesis in a bacterial peptidoglycan

A polymer of N-acetylglucosamine 1-phosphate in the wall of Staphylococcus lactis 2102

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

Contact Info

Product

Resources

About