The Lipid A from the Lipopolysaccharide of the Phototrophic Bacterium Rhodomicrobium vannielii ATCC 17100 Revisited

Autor: Otto Holst, Katarzyna Susniak, Iwona Komaniecka, Adam Choma, Holger Heine
Jazyk: angličtina
Rok vydání: 2020
Předmět:
Lipopolysaccharides
0301 basic medicine
Magnetic Resonance Spectroscopy
Lipopolysaccharide
Mannose
medicine.disease_cause
01 natural sciences
Mass Spectrometry
lcsh:Chemistry
Lipid A
chemistry.chemical_compound
Tandem Mass Spectrometry
galacturonic acid
lcsh:QH301-705.5
lipid A
Spectroscopy
Molecular Structure
biology
lipopolysaccharide
structure elucidation
Biological activity
General Medicine
Rhodomicrobium
Computer Science Applications
Rhodomicrobium vannielii
Phototrophic Processes
Biochemistry
lipids (amino acids
peptides
and proteins)
budding bacteria
Spectrometry
Mass
Electrospray Ionization
Article
Catalysis
Inorganic Chemistry
03 medical and health sciences
Residue (chemistry)
medicine
Humans
Physical and Theoretical Chemistry
Molecular Biology
Escherichia coli
010405 organic chemistry
mannose
Organic Chemistry
biology.organism_classification
0104 chemical sciences
030104 developmental biology
lcsh:Biology (General)
lcsh:QD1-999
chemistry
Bacteria
Chromatography
Liquid
Zdroj: International Journal of Molecular Sciences
Volume 22
Issue 1
International Journal of Molecular Sciences, Vol 22, Iss 258, p 258 (2021)
ISSN: 1422-0067
DOI: 10.3390/ijms22010258
Popis: The structure of lipid A from lipopolysaccharide (LPS) of Rhodomicrobium vannielii ATCC 17100 (Rv) a phototrophic, budding bacterium was re-investigated using high-resolution mass spectrometry, NMR, and chemical degradation protocols. It was found that the (GlcpN)-disaccharide lipid A backbone was substituted by a GalpA residue that was connected to C-1 of proximal GlcpN. Some of this GalpA residue was &beta
eliminated by alkaline de-acylation, which indicated the possibility of the presence of another so far unidentified substituent at C-4 in non-stoichiometric amounts. One Manp residue substituted C-4&prime
of distal GlcpN. The lipid A backbone was acylated by 16:0(3-OH) at C-2 of proximal GlcpN, and by 16:0(3-OH), i17:0(3-OH), or 18:0(3-OH) at C-2&prime
of distal GlcpN. Two acyloxy-acyl moieties that were mainly formed by 14:0(3-O-14:0) and 16:0(3-O-22:1) occupied the distal GlcpN of lipid A. Genes that were possibly involved in the modification of Rv lipid A were compared with bacterial genes of known function. The biological activity was tested at the model of human mononuclear cells (MNC), showing that Rv lipid A alone does not significantly stimulate MNC. At low concentrations of toxic Escherichia coli O111:B4 LPS, pre-incubation with Rv lipid A resulted in a substantial reduction of activity, but, when higher concentrations of E. coli LPS were used, the stimulatory effect was increased.
Databáze: OpenAIRE
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