Structure Determination of Lipid A with Multiple Glycosylation Sites by Tandem MS of Lithium-Adducted Negative Ions.
| Autor: | Yang H; Department of Microbial Pathogenesis, School of Dentistry, University of Maryland, Baltimore, Maryland 21201, United States of America., Sherman ME; Department of Microbial Pathogenesis, School of Dentistry, University of Maryland, Baltimore, Maryland 21201, United States of America., Koo CJ; Chemistry Department, United States Naval Academy, Annapolis, Maryland 21402, United States of America.; School of Medicine, Uniformed Services University, Bethesda, Maryland 20814, United States of America., Treaster LM; Chemistry Department, United States Naval Academy, Annapolis, Maryland 21402, United States of America.; School of Medicine, University of Kansas, Kansas City, Kansas 66160, United States of America., Smith JP; Oceanography Department, United States Naval Academy, Annapolis, Maryland 21402, United States of America., Gallaher SG; Oceanography Department, United States Naval Academy, Annapolis, Maryland 21402, United States of America., Goodlett DR; Department of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia V8P 5C2, Canada.; Genome British Columbia Proteomics Centre, University of Victoria, Victoria, British Columbia V8Z 7Z8, Canada., Sweet CR; Chemistry Department, United States Naval Academy, Annapolis, Maryland 21402, United States of America., Ernst RK; Department of Microbial Pathogenesis, School of Dentistry, University of Maryland, Baltimore, Maryland 21201, United States of America. |
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| Jazyk: | angličtina |
| Zdroj: | Journal of the American Society for Mass Spectrometry [J Am Soc Mass Spectrom] 2023 Jun 07; Vol. 34 (6), pp. 1047-1055. Date of Electronic Publication: 2023 May 15. |
| DOI: | 10.1021/jasms.3c00014 |
| Abstrakt: | FLAT n 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 FLAT n by tandem MS fragmentation of lithium-adducted molecular lipid A anions and fragments (FLAT n-Li ) that provides additional structural and diagnostic data from FLAT n samples allowing for the discrimination of terminal phosphate modifications in a variety of pathogenic and environmental species. Using FLAT n-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. |
| Databáze: | MEDLINE |
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