Profiling and tandem mass spectrometry analysis of aminoacylated phospholipids in Bacillus subtilis  [version 1; referees: 1 approved, 2 approved with reservations]

Cationic modulation of the dominantly negative electrostatic structure of phospholipids plays an important role in bacterial response to changes in the environment. In addition to zwitterionic phosphatidylethanolamine, Gram-positive bacteria are also abundant in positively charged lysyl-phosphatidyl...

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Main Authors: Metin Atila, Yu Luo
Format: Article
Language:English
Published: F1000 Research Ltd 2016-01-01
Series:F1000Research
Subjects:
Online Access:http://f1000research.com/articles/5-121/v1
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spelling doaj-2d48d4f8be394125af8ae90b9226c2c92020-11-25T03:50:53ZengF1000 Research LtdF1000Research2046-14022016-01-01510.12688/f1000research.7842.18441Profiling and tandem mass spectrometry analysis of aminoacylated phospholipids in Bacillus subtilis  [version 1; referees: 1 approved, 2 approved with reservations]Metin Atila0Yu Luo1Department of Biochemistry, University of Saskatchewan, Saskatoon, CanadaDepartment of Biochemistry, University of Saskatchewan, Saskatoon, CanadaCationic modulation of the dominantly negative electrostatic structure of phospholipids plays an important role in bacterial response to changes in the environment. In addition to zwitterionic phosphatidylethanolamine, Gram-positive bacteria are also abundant in positively charged lysyl-phosphatidylglycerol. Increased amounts of both types of lipids render Gram-positive bacterial cells more resistant to cationic antibiotic peptides such as defensins.  Lysyl and alanyl-phosphatidylglycerol as well as alanyl-cardiolipin have also been studied by mass spectroscopy. Phospholipids modified by other amino acids have been discovered by chemical analysis of the lipid lysate but have yet to be studied by mass spectroscopy. We exploited the high sensitivity of modern mass spectroscopy in searching for substructures in complex mixtures to establish a sensitive and thorough screen for aminoacylated phospholipids. The search for deprotonated aminoacyl anions in lipid extracted from Bacillus subtilis strain 168 yielded strong evidence as well as relative abundance of aminoacyl-phosphatidylglycerols, which serves as a crude measure of the specificity of aminoacyl-phosphatidylglycerol synthase MprF. No aminoacyl-cardiolipin was found. More importantly, the second most abundant species in this category is D-alanyl-phosphatidylglycerol, suggesting a possible role in the D-alanylation pathway of wall- and lipo-teichoic acids.http://f1000research.com/articles/5-121/v1Antimicrobials & Drug ResistanceBacterial Infections
collection DOAJ
language English
format Article
sources DOAJ
author Metin Atila
Yu Luo
spellingShingle Metin Atila
Yu Luo
Profiling and tandem mass spectrometry analysis of aminoacylated phospholipids in Bacillus subtilis  [version 1; referees: 1 approved, 2 approved with reservations]
F1000Research
Antimicrobials & Drug Resistance
Bacterial Infections
author_facet Metin Atila
Yu Luo
author_sort Metin Atila
title Profiling and tandem mass spectrometry analysis of aminoacylated phospholipids in Bacillus subtilis  [version 1; referees: 1 approved, 2 approved with reservations]
title_short Profiling and tandem mass spectrometry analysis of aminoacylated phospholipids in Bacillus subtilis  [version 1; referees: 1 approved, 2 approved with reservations]
title_full Profiling and tandem mass spectrometry analysis of aminoacylated phospholipids in Bacillus subtilis  [version 1; referees: 1 approved, 2 approved with reservations]
title_fullStr Profiling and tandem mass spectrometry analysis of aminoacylated phospholipids in Bacillus subtilis  [version 1; referees: 1 approved, 2 approved with reservations]
title_full_unstemmed Profiling and tandem mass spectrometry analysis of aminoacylated phospholipids in Bacillus subtilis  [version 1; referees: 1 approved, 2 approved with reservations]
title_sort profiling and tandem mass spectrometry analysis of aminoacylated phospholipids in bacillus subtilis  [version 1; referees: 1 approved, 2 approved with reservations]
publisher F1000 Research Ltd
series F1000Research
issn 2046-1402
publishDate 2016-01-01
description Cationic modulation of the dominantly negative electrostatic structure of phospholipids plays an important role in bacterial response to changes in the environment. In addition to zwitterionic phosphatidylethanolamine, Gram-positive bacteria are also abundant in positively charged lysyl-phosphatidylglycerol. Increased amounts of both types of lipids render Gram-positive bacterial cells more resistant to cationic antibiotic peptides such as defensins.  Lysyl and alanyl-phosphatidylglycerol as well as alanyl-cardiolipin have also been studied by mass spectroscopy. Phospholipids modified by other amino acids have been discovered by chemical analysis of the lipid lysate but have yet to be studied by mass spectroscopy. We exploited the high sensitivity of modern mass spectroscopy in searching for substructures in complex mixtures to establish a sensitive and thorough screen for aminoacylated phospholipids. The search for deprotonated aminoacyl anions in lipid extracted from Bacillus subtilis strain 168 yielded strong evidence as well as relative abundance of aminoacyl-phosphatidylglycerols, which serves as a crude measure of the specificity of aminoacyl-phosphatidylglycerol synthase MprF. No aminoacyl-cardiolipin was found. More importantly, the second most abundant species in this category is D-alanyl-phosphatidylglycerol, suggesting a possible role in the D-alanylation pathway of wall- and lipo-teichoic acids.
topic Antimicrobials & Drug Resistance
Bacterial Infections
url http://f1000research.com/articles/5-121/v1
work_keys_str_mv AT metinatila profilingandtandemmassspectrometryanalysisofaminoacylatedphospholipidsinbacillussubtilisversion1referees1approved2approvedwithreservations
AT yuluo profilingandtandemmassspectrometryanalysisofaminoacylatedphospholipidsinbacillussubtilisversion1referees1approved2approvedwithreservations
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