Unusual LipidA from a Cold-Adapted Bacterium: Detailed Structural Characterization

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.