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Review
. 2010 Jan 4;11(1):35-45.
doi: 10.1002/cbic.200900557.

Wall teichoic acid function, biosynthesis, and inhibition

Jonathan G Swoboda  1 , Jennifer Campbell, Timothy C Meredith, Suzanne Walker
Affiliations
Review

Wall teichoic acid function, biosynthesis, and inhibition

Jonathan G Swoboda et al. Chembiochem. .
No abstract available

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Figures

Figure 1
Figure 1
Simplified depiction of Gram-positive and Gram-negative bacterial cell envelopes. Gram-negative organisms have a distinct periplasm; Gram-positive organisms do not, but recent studies have suggested that they have a periplasmic-like compartment between the plasma membrane and the base of the peptidoglycan layers.[3] Proteins are omitted from the depictions for clarity. Membrane-embedded, membrane-anchored, and peptidoglycan-associated proteins are abundant in the cell membranes of both Gram-positive and Gram-negative organisms. LTA: lipoteichoic acid; LPS: lipopolysaccharide; WTA: wall teichoic acid.
Figure 2
Figure 2
Representative chemical structures of wall teichoic acids from different Gram-positive bacteria (m = 1–3 and n = 20–40).
Figure 3
Figure 3
Genetic organization of wall teichoic acid biosynthetic genes; tag: teichoic acid glycerol; tar: teichoic acid ribitol. Adapted from Qian et al.[48] (//: number of nucleic acids between genes if > 120 base pairs).
Figure 4
Figure 4
Differences in wall teichoic acid biosynthesis for: A) B. subtilis 168, B) B. subtilis W23, and C) S. aureus.
Figure 5
Figure 5
Proposed role for the distinct TarK and TarL WTA polymers. A) TarK and TarL make electrophoretically distinct WTA polymers. PAGE analysis of WTAs extracted from various S. aureus strains shows that poly(ribitol phosphate) polymer length corresponds to gene regulation. The agr system directly or indirectly represses the expression of TarK, leading to an increase in WTA polymer length. RN4220 has a partial defect in agr while RN450 has a fully functional agr system (agr+). TarK makes a short secondary polymer, K-WTA, while TarL makes a longer primary polymer, L-WTA. The L-WTA was extracted from a ΔtarK mutant of S. aureus RN4220. K-WTA was extracted from an S. aureus RN4220 mutant over-expressing tarK in a ΔtarL background.[61] B) Expression of the shorter K-WTA at low cell density might allow for increased accessibility of adhesins, leading to a pro-adhesion state; whereas, the expression of the longer L-WTA at high cell density (mediated by the activation of agr) might lead to a low-adhesion phenotype.
Figure 6
Figure 6
Depiction of the primary Staphylococcus aureus wall teichoic acid (L-WTA) biosynthetic pathway. Nonessential WTA pathway enzymes are colored green and their deletion leads to an avirulent phenotype. Conditionally essential enzymes are colored red and their deletion is lethal in a wild-type background but permitted in a ΔtarO or ΔtarA background. Following intracellular assembly, the poly(ribitol phosphate) polymer is transported to the outside by a two-component ABC transporter, TarGH, and then covalently linked through a phosphodiester bond to the MurNAc sugars of peptidoglycan by an unidentified enzyme the biological and genetic properties of which have not been established. In addition to TarI, J, and L, all S. aureus strains contain a homologous set of enzymes (designated TarI′,J′ and K; Figure 3) that directs the synthesis of a distinct WTA polymer (K-WTA); their cellular functions remain incompletely understood.
Figure 7
Figure 7
Chemical structures of currently known inhibitors of wall teichoic acid synthesis and export in Staphylococcus aureus. An inhibitor of DltA, which is involved in modification of both WTAs and LTAs, has also been reported.[43]
Figure 8
Figure 8
General screening strategy for the identification of small-molecule inhibitors of conditionally essential enzymes/targets in nonessential biosynthetic pathways; *: the mutant strain is incapable of initiating polymer synthesis. In the described screen, the paired strain lacked the first enzyme involved in WTA biosynthesis (TarO).
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