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
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单核细胞增生李斯特菌血清型 1/2a 和枯草芽孢杆菌中的 LTA 糖基化需要 GtcA

DOI:
10.1101/2019.12.12.873851
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发表时间:
2019
期刊:
--
影响因子:
--
通讯作者:
Rismondo J
Rismondo J
中科院分区:
--
文献类型:
--
作者:
Rismondo J

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细胞壁聚合物壁磷壁酸(WTA)和脂磷壁酸(LTA)通常用糖基和D-丙氨酸残基修饰。最近的研究表明,三组分糖基化系统被用于几种革兰氏阳性细菌包括枯草芽孢杆菌和单核细胞增生李斯特菌中的LTA的修饰。在L.在单核细胞增多症1/2a菌株10403 S中,细胞质糖基转移酶GtlA被认为使用UDP-半乳糖来产生C55-β-半乳糖脂质中间体,其通过未知的翻转酶跨膜转运。接下来,半乳糖残基通过糖基转移酶GtlB转移到细胞外部的LTA骨架上。在这里,我们表明,GtcA是必要的糖基化的LTA在L。单核细胞增多症10403 S和B。subtilis 168,我们假设这些蛋白质充当C55-P-糖翻转酶。由此,我们揭示了GtcA参与了L.单核细胞增多症10403 S,即具有N-乙酰葡糖胺的WTA和具有半乳糖残基的LTA。这些结果表明,L。单核细胞增多症GtcA蛋白可以作用于不同的C55-P-糖中间体。对L.单核细胞增多症导致鉴定了对其总体功能必需的残基以及主要影响WTA或LTA糖基化的残基。
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 including Bacillus subtilis and Listeria monocytogenes. In the L. monocytogenes 1/2a strain 10403S, the cytoplasmic glycosyltransferase GtlA is thought to use UDP-galactose to produce the C 55-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 in L. monocytogenes 10403S and B. subtilis 168 and we hypothesize that these proteins act as C 55-P-sugar flippases. With this we revealed that GtcA is involved in the glycosylation of both teichoic acid polymers in L. monocytogenes 10403S, namely WTA with N-acetylglucosamine and LTA with galactose residues. These findings indicate that the L. monocytogenes GtcA protein can act on different C 55-P-sugar intermediates. Further characterization of GtcA in L. monocytogenes led to the identification of residues essential for its overall function as well as residues, which predominately impact WTA or LTA glycosylation.
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