Structural characterization of phosphoethanolamine-modified lipid A from probiotic: Escherichia coli strain Nissle 1917
- Authors
- Jo, S.-H.; Park, H.-G.; Song, W.-S.; Kim, S.-M.; Kim, E.-J.; Yang, Y.-H.; Kim, J.-S.; Kim, B.-G.; Kim, Y.-G.
- Issue Date
- Jun-2019
- Publisher
- Royal Society of Chemistry
- Citation
- RSC Advances, v.9, no.34, pp.19762 - 19771
- Journal Title
- RSC Advances
- Volume
- 9
- Number
- 34
- Start Page
- 19762
- End Page
- 19771
- URI
- http://scholarworks.bwise.kr/ssu/handle/2018.sw.ssu/34906
- DOI
- 10.1039/c9ra02375e
- ISSN
- 2046-2069
- Abstract
- Gut microbiota, a complex microbial community inhabiting human or animal intestines recently regarded as an endocrine organ, has a significant impact on human health. Probiotics can modulate gut microbiota and the gut environment by releasing a range of bioactive compounds. Escherichia coli (E. coli) strain Nissle 1917 (EcN), a Gram-negative bacterial strain, has been used to treat gastrointestinal (GI) disorders (i.e., inflammatory bowel disease, diarrhea, ulcerative colitis, and so on). However, endotoxicity of lipopolysaccharide (LPS), a major component of the cell wall of Gram-negative bacteria in the gut, is known to have a strong influence on gut inflammation and maintenance of gut homeostasis. Therefore, characterizing the chemical structure of lipid A which determines the toxicity of LPS is needed to understand nonpathogenic colonization and commensalism properties of EcN in the gut more precisely. In the present study, MALDI multiple-stage mass spectrometry analysis of lipid A extracted from EcN demonstrates that hexaacylated lipid A (m/z 1919.19) contains a glucosamine disaccharide backbone, a myristate, a laurate, four 3-hydroxylmyristates, two phosphates, and phosphoethanolamine (PEA). PEA modification of lipid A is known to contribute to cationic antimicrobial peptide (CAMP) resistance of Gram-negative bacteria. To confirm the role of PEA in CAMP resistance of EcN, minimum inhibitory concentrations (MICs) of polymyxin B and colistin were determined using a wild-type strain and a mutant strain with deletion of eptA gene encoding PEA transferase. Our results confirmed that MICs of polymyxin B and colistin for the wild-type were twice as high as those for the mutant. These results indicate that EcN can more efficiently colonize the intestine through PEA-mediated tolerance despite the presence of CAMPs in human gut such as human defensins. Thus, EcN can be used to help treat and prevent many GI disorders. © The Royal Society of Chemistry 2019.
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