Unusual Lipid A from a cold adapted bacterium: detailed structural characterization
ChemBioChem, June 2017
Corsaro, Maria Michela, Casillo, Angela, Ziaco, Marcello, Lindner, Buko, Parrilli, Ermenegilda, Schwudke, Dominik, Holgado, Aurora, Verstrepen, Lynn, Sannino, Filomena, Beyaert, Rudi, Lanzetta, Rosa, Tutino, Maria Luisa, Corsaro, Maria Michela, Tutino, Maria Luisa
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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