Unusual LipidA from a Cold-Adapted Bacterium: Detailed Structural Characterization
Unusual LipidA from a Cold-Adapted Bacterium: Detailed Structural Characterization
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DOI：
10.1002/cbic.201700287
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发表时间：
2017-09-19
期刊：
影响因子：
3.2
通讯作者：
Corsaro, Maria Michela
中科院分区：
文献类型：
--
作者：
Casillo, Angela;Ziaco, Marcello;Corsaro, Maria Michela
Colwellia psychrerythraea 34H 是一种革兰氏阴性冷适应微生物，它采用多种策略来应对与其栖息地低温相关的限制。在这项研究中，我们报告了科尔韦利亚脂多糖脂质A部分的完整表征。 LipidA 及其部分脱酰基衍生物通过高分辨率质谱、核磁共振波谱和化学分析进行了完全表征。鉴定出一种不寻常的结构，其中 3-羟基不饱和十四碳烯酸作为初级酰化模式的组成部分。此外，还原性2-氨基-2-脱氧吡喃葡萄糖单元的3位二级酰化位点上部分酰化的磷酸甘油部分的存在导致脂质A结构中巨大的天然异质性。生物活性测定表明，在人巨噬细胞中进行测试时，C.psychrerythraea 34H LipidA 并未表现出激动或拮抗作用。
Colwellia psychrerythraea 34H is a Gram-negative cold-adapted microorganism that adopts many strategies to cope with the limitations associated with the low temperatures of its habitat. In this study, we report the complete characterization of the lipidA moiety from the lipopolysaccharide of Colwellia. LipidA and its partially deacylated derivative were completely characterized by high-resolution mass spectrometry, NMR spectroscopy, and chemical analysis. An unusual structure with a 3-hydroxy unsaturated tetradecenoic acid as a component of the primary acylation pattern was identified. In addition, the presence of a partially acylated phosphoglycerol moiety on the secondary acylation site at the 3-position of the reducing 2-amino-2-deoxyglucopyranose unit caused tremendous natural heterogeneity in the structure of lipidA. Biological-activity assays indicated that C.psychrerythraea 34H lipidA did not show an agonistic or antagonistic effect upon testing in human macrophages.