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Unusual LipidA from a cold-adapted bacterium: detailed structural characterization
Casillo, A.; Ziaco, M.; Lindner, B.; Parrilli, E.; Schwudke, D.; Holgado, A.; Verstrepen, L.; Sannino, F.; Beyaert, R.; Lanzetta, R.; Tutino, M.L.; Corsaro, M.M. (2017). Unusual LipidA from a cold-adapted bacterium: detailed structural characterization. ChemBioChem 18(18): 1845-1854. https://dx.doi.org/10.1002/cbic.201700287
In: ChemBioChem. Wiley-VCH: Weinheim. ISSN 1439-4227; e-ISSN 1439-7633
Peer reviewed article  
Beschikbaar in  Auteurs 
Trefwoord
    Marien/Kust
Author keywords
    cold adaptation; glycerol phosphate; lipids; mass spectrometry;structure elucidation
Auteurs  Top 
  • Casillo, A.
  • Ziaco, M.
  • Lindner, B.
  • Parrilli, E.
  • Schwudke, D.
  • Holgado, A.
  • Verstrepen, L.
  • Sannino, F.
  • Beyaert, R.
  • Lanzetta, R.
  • Tutino, M.L.
  • Corsaro, M.M.
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.
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