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Unusual Lipid A from a Cold-Adapted Bacterium: Detailed Structural Characterization
ChemBioChem ( IF 2.6 ) Pub Date : 2017-07-27 08:15:34 , DOI: 10.1002/cbic.201700287
Angela Casillo 1 , Marcello Ziaco 1 , Buko Lindner 2 , Ermenegilda Parrilli 1 , Dominik Schwudke 2 , Aurora Holgado 3, 4 , Lynn Verstrepen 3, 4 , Filomena Sannino 1 , Rudi Beyaert 3, 4 , Rosa Lanzetta 1 , Maria Luisa Tutino 1 , Maria Michela Corsaro 1
Affiliation  

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 lipid A moiety from the lipopolysaccharide of Colwellia. Lipid A 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 lipid A. Biological-activity assays indicated that C. psychrerythraea 34H lipid A did not show an agonistic or antagonistic effect upon testing in human macrophages.

中文翻译:

来自冷适应细菌的不寻常脂质A:详细的结构表征

Colwellia psychrerythraea 34H是革兰氏阴性的冷适应微生物,它采用许多策略来应对与其栖息地的低温相关的局限性。在这项研究中,我们报告了来自Colwellia脂多糖的脂质A部分的完整表征。脂质A及其部分脱酰基的衍生物已通过高分辨率质谱,NMR光谱和化学分析进行了全面表征。鉴定出具有3-羟基不饱和十四碳烯酸作为主要酰化图案的组分的异常结构。另外,在还原性2-氨基-2-脱氧葡萄糖吡喃糖单元的3-位的次级酰化位点上存在部分酰化的磷酸甘油部分,导致脂质A的结构具有极大的自然异质性。生物活性测定表明,C在人巨噬细胞中测试时,Psychrerythraea 34H脂质A没有显示出拮抗或拮抗作用。
更新日期:2017-07-28
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