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Unusual Lipid A from a Cold‐Adapted Bacterium: Detailed Structural Characterization |
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| Authors: | Dr. Angela Casillo Marcello Ziaco Dr. Buko Lindner Prof. Ermenegilda Parrilli Dr. Dominik Schwudke Aurora Holgado Dr. Lynn Verstrepen Dr. Filomena Sannino Prof. Rudi Beyaert Prof. Rosa Lanzetta Prof. Maria Luisa Tutino Prof. Maria Michela Corsaro |
| Affiliation: | 1. Department of Chemical Sciences, University of Naples “Federico II”, Complesso Universitario Monte S. Angelo, Naples, Italy;2. Division of Bioanalytical Chemistry, Research Center Borstel, Leibniz-Center for Medicine and Biosciences, Borstel, Germany;3. Unit for Molecular Signal Transduction in Inflammation, VIB-UGent Center for Inflammation Research, VIB, Zwijnaarde, Ghent, Belgium;4. Department of Biomedical Molecular Biology, Ghent University, Zwijnaarde, Ghent, Belgium |
| Abstract: | 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. |
| Keywords: | cold adaptation glycerol phosphate lipids mass spectrometry structure elucidation |