Structure and functions of linkage unit intermediates in the biosynthesis of ribitol teichoic acids in Staphylococcus aureus H and Bacillus subtilis W23

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Abstract
The stepwise formation and characterization of linkage unit intermediates and their functions in ribitol teichoic acid biosynthesis were studied with membranes obtained from Staphylococcus aureus H and Bacillus subtilis W23. The formation of labeled polymer from CDP‐[14C]ribitol and CDP‐glycerol in each membrane system was markedly stimulated by the addition of N‐acetylmannosaminyl(β1→4)N‐acetylglucosamine (ManNAc‐GlcNAc) linked to pyrophosphorylpolyisoprenol. Whereas incubation of S. aureus membranes with CDP‐glycerol and ManNAc‐[14C]GlcNAc‐P P‐prenol led to synthesis of (glycerol phosphate)1–3‐ManNAc‐[14C]GlcNAc‐P P‐prenol, incubation of B. subtilis membranes with the same substrates yielded (glycerol phosphate)1–2‐ManNAc‐[14C]GlcNAc‐P P‐prenol. In S. aureus membranes, (glycerol phosphate)2‐ManNAc‐[14C]GlcNAc‐P P‐prenol as well as (glycerol phosphate)3‐ManNAc‐[14C]GlcNAc‐P P‐prenol served as an acceptor for ribitol phosphate units, but (glycerol phosphate)‐ManNAc‐[14C]GlcNAc‐P P‐prenol did not. In B. subtilis W23 membranes, (glycerol phosphate)‐ManNAc‐[14C]GlcNAc‐P P‐prenol served as a better acceptor for ribitol phosphate units than (glycerol phosphate)2‐ManNAc‐[14C]GlcNAc‐P P‐prenol. In this membrane system (ribitol phosphate)‐(glycerol phosphate)‐ManNAc‐[14C]GlcNAc‐P P‐prenol was formed from ManNAc‐[14C]GlcNAc‐P P‐prenol, CDP‐glycerol and CDP‐ribitol. The results indicate that (glycerol phosphate)1–3‐ManNAc‐GlcNAc‐P P‐prenol and (glycerol phosphate)1–2‐ManNAc‐GlcNAc‐P P‐prenol are involved in the pathway for the synthesis of wall ribitol teichoic acids in S. aureus H and B. subtilis W23 respectively.