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Found 3 records.
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1. (CSDB ID: 22342) | report error |
| Myr-(1-3)-3HOMyr-(1-3)-+ 3HOMyr-(1-2)-+ | | Myr-(1-3)-3HOMyr-(1-2)-b-D-GlcpN-(1-6)-a-D-GlcpN-(1-P | | b-L-Arap4N-(1--P--4)--+ 3HOMyr-(1-3)-+ | Show graphically |
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Proteus mirabilis
(NCBI TaxID 584,
species name lookup)
]
usna.edu>; R.K. Ernst <rkernstumaryland.edu>FLATn is a tandem mass spectrometric technique that can be used to rapidly generate spectral information applicable for structural elucidation of lipids like lipid A from Gram-negative bacterial species from a single bacterial colony. In this study, we extend the scope and capability of FLATn by tandem MS fragmentation of lithium-adducted molecular lipid A anions and fragments (FLATn-Li) that provides additional structural and diagnostic data from FLATn samples allowing for the discrimination of terminal phosphate modifications in a variety of pathogenic and environmental species. Using FLATn-Li, we elucidated the lipid A structure from several bacterial species, including novel structures from arctic bacterioplankton of the Duganella and Massilia genera that favor 4-amino-4-deoxy-L-arabinopyranose (Ara4N) modification at the 1-phosphate position and that demonstrate double glycosylation with Ara4N at the 1 and 4' phosphate positions simultaneously. The structures characterized in this work demonstrate that some environmental psychrophilic species make extensive use of this structural lipid A modification previously characterized as a pathogenic adaptation and the structural basis of resistance to cationic antimicrobial peptides. This observation extends the role of phosphate modification(s) in environmental species adaptation and suggests that Ara4N modification can functionally replace the positive charge of the phosphoethanolamine modification that is more typically found attached to the 1-phosphate position of modified lipid A.
lipid A, modification, Structure determination, Ions, tandem MS
Structure type: oligomer|
2. (CSDB ID: 27067) | report error |
| Lau-(1-3)-3HODco-(1-2)-+ | b-L-Arap4N-(1--P--4)--+ | | | Lau-(1-3)-3HODco-(1-2)-b-D-GlcpN-(1-6)-a-D-GlcpN-(1--P--1)--b-L-Arap4N | 3HODco-(1-3)-+ | Show graphically |
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Massilia rubra
(NCBI TaxID 2607910,
species name lookup)
Duganella aceris
(NCBI TaxID 2703883,
species name lookup)
usna.edu>; R.K. Ernst <rkernstumaryland.edu>FLATn is a tandem mass spectrometric technique that can be used to rapidly generate spectral information applicable for structural elucidation of lipids like lipid A from Gram-negative bacterial species from a single bacterial colony. In this study, we extend the scope and capability of FLATn by tandem MS fragmentation of lithium-adducted molecular lipid A anions and fragments (FLATn-Li) that provides additional structural and diagnostic data from FLATn samples allowing for the discrimination of terminal phosphate modifications in a variety of pathogenic and environmental species. Using FLATn-Li, we elucidated the lipid A structure from several bacterial species, including novel structures from arctic bacterioplankton of the Duganella and Massilia genera that favor 4-amino-4-deoxy-L-arabinopyranose (Ara4N) modification at the 1-phosphate position and that demonstrate double glycosylation with Ara4N at the 1 and 4' phosphate positions simultaneously. The structures characterized in this work demonstrate that some environmental psychrophilic species make extensive use of this structural lipid A modification previously characterized as a pathogenic adaptation and the structural basis of resistance to cationic antimicrobial peptides. This observation extends the role of phosphate modification(s) in environmental species adaptation and suggests that Ara4N modification can functionally replace the positive charge of the phosphoethanolamine modification that is more typically found attached to the 1-phosphate position of modified lipid A.
lipid A, modification, Structure determination, Ions, tandem MS
Structure type: oligomer|
3. (CSDB ID: 27068) | report error |
| 3HODco-(1-3)-+ | ?%b-L-Arap4N-(1--P--1)--+ | | | Lau-(1-3)-3HOLau-(1-2)-+ | | | | | ?%b-L-Arap4N-(1--P--4)--b-D-GlcpN-(1-6)-a-D-GlcpN | | 3HODco-(1-3)-+ | | Lau-(1-3)-3HOLau-(1-2)-+ | Show graphically |
|
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Pseudomonas lactucae
(NCBI TaxID 2813360,
species name lookup)
usna.edu>; R.K. Ernst <rkernstumaryland.edu>FLATn is a tandem mass spectrometric technique that can be used to rapidly generate spectral information applicable for structural elucidation of lipids like lipid A from Gram-negative bacterial species from a single bacterial colony. In this study, we extend the scope and capability of FLATn by tandem MS fragmentation of lithium-adducted molecular lipid A anions and fragments (FLATn-Li) that provides additional structural and diagnostic data from FLATn samples allowing for the discrimination of terminal phosphate modifications in a variety of pathogenic and environmental species. Using FLATn-Li, we elucidated the lipid A structure from several bacterial species, including novel structures from arctic bacterioplankton of the Duganella and Massilia genera that favor 4-amino-4-deoxy-L-arabinopyranose (Ara4N) modification at the 1-phosphate position and that demonstrate double glycosylation with Ara4N at the 1 and 4' phosphate positions simultaneously. The structures characterized in this work demonstrate that some environmental psychrophilic species make extensive use of this structural lipid A modification previously characterized as a pathogenic adaptation and the structural basis of resistance to cationic antimicrobial peptides. This observation extends the role of phosphate modification(s) in environmental species adaptation and suggests that Ara4N modification can functionally replace the positive charge of the phosphoethanolamine modification that is more typically found attached to the 1-phosphate position of modified lipid A.
lipid A, modification, Structure determination, Ions, tandem MS
Structure type: oligomer| New query | Export IDs | Home | Help |
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