GtcA is required for LTA glycosylation in Listeria monocytogenes serovar 1/2a and Bacillus subtilis.
GtcA is required for LTA glycosylation in Listeria monocytogenes serovar 1/2a and Bacillus subtilis.
复制标题
单核细胞增生李斯特氏菌血清型 1/2a 和枯草芽孢杆菌中的 LTA 糖基化需要 GtcA。
DOI：
10.1016/j.tcsw.2020.100038
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发表时间：
2020
期刊：
影响因子：
--
通讯作者：
Rismondo J
中科院分区：
文献类型：
--
作者：
Rismondo J
The cell wall polymers wall teichoic acid (WTA) and lipoteichoic acid (LTA) are often modified with glycosyl and D-alanine residues. Recent studies have shown that a three-component glycosylation system is used for the modification of LTA in several Gram-positive bacteria includingBacillus subtilisandListeria monocytogenes. In theL. monocytogenes1/2a strain 10403S, the cytoplasmic glycosyltransferase GtlA is thought to use UDP-galactose to produce the C55-P-galactose lipid intermediate, which is transported across the membrane by an unknown flippase. Next, the galactose residue is transferred onto the LTA backbone on the outside of the cell by the glycosyltransferase GtlB. Here we show that GtcA is necessary for the glycosylation of LTA inL. monocytogenes10403S andB. subtilis168 and we hypothesize that these proteins act as C55-P-sugar flippases. With this we revealed that GtcA is involved in the glycosylation of both teichoic acid polymers inL. monocytogenes10403S, namely WTA with N-acetylglucosamine and LTA with galactose residues. These findings indicate that theL. monocytogenesGtcA protein can act on different C55-P-sugar intermediates. Further characterization of GtcA inL. monocytogenesled to the identification of residues essential for its overall function as well as residues, which predominately impact WTA or LTA glycosylation.
