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Microbiology and Molecular Biology Reviews, December 2003, p. 686-723, Vol. 67, No. 4
1092-2172/03/$08.00+0     DOI: 10.1128/MMBR.67.4.686-723.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

A Continuum of Anionic Charge: Structures and Functions of D-Alanyl-Teichoic Acids in Gram-Positive Bacteria{dagger}

Francis C. Neuhaus1* and James Baddiley2

Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois 60208,1 Department of Biochemistry, University of Cambridge, Cambridge CB2 1QW, United Kingdom2

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.

* Corresponding author. Mailing address: Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, 2153 Sheridan Rd., Evanston, IL 60208-3500. Phone: (847) 491-5656. Fax: (847) 467-1380. E-mail: f-neuhaus{at}northwestern.edu.

{dagger} Dedicated to the memory of Werner Fischer (1930-2000), whose insights and inspiration as a friend and colleague are recognized.

Microbiology and Molecular Biology Reviews, December 2003, p. 686-723, Vol. 67, No. 4
1092-2172/03/$08.00+0     DOI: 10.1128/MMBR.67.4.686-723.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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