Title |
Unusual Lipid A from a Cold‐Adapted Bacterium: Detailed Structural Characterization
|
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Published in |
ChemBioChem, July 2017
|
DOI | 10.1002/cbic.201700287 |
Pubmed ID | |
Authors |
Angela Casillo, Marcello Ziaco, Buko Lindner, Ermenegilda Parrilli, Dominik Schwudke, Aurora Holgado, Lynn Verstrepen, Filomena Sannino, Rudi Beyaert, Rosa Lanzetta, Maria Luisa Tutino, Maria Michela Corsaro |
Abstract |
Colwellia psychrerythraea 34H is a Gram-negative cold-adapted microorganism that adopts many strategies to cope with the limitations due to the low temperatures of its habitat. In this study, we reported the complete characterization of the lipid A moiety from the lipopolysaccharide of Colwellia, to find out if structural features could be linked to the cold-adaptation strategy. The lipid A and its partially deacylated derivative were completely characterized by means of high resolution mass spectrometry, NMR spectroscopy, and chemical analysis. An unusual structure, consisting of 3-hydroxy unsaturated tetradecenoic acid as component of the primary acylation pattern, was identified. In addition, the presence of a partially acylated phosphoglycerol moiety on the secondary acylation site at 3-position of the reducing GlcN caused a tremendous natural heterogeneity of the lipid A structure. Biological activity assays indicated that Colwellia psychrerythraea 34H lipid A did not show any either agonistic or antagonistic effect when tested in human macrophages. |
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