MALDI TIMS IMS Reveals Ganglioside Molecular Diversity within Murine S. aureus Soft Tissue Abscesses.

21 November 2023, Version 1
This content is a preprint and has not undergone peer review at the time of posting.


Gangliosides play important roles in innate and adaptive immunity. The high degree of structural heterogeneity results in significant variability in ganglioside expression patterns and greatly complicates linking structure and function. Structural characterization at the site of infection is essential in elucidating host ganglioside function in response to invading pathogens, such as Staphylococcus aureus (S. aureus). Matrix-assisted laser desorption/ionization imaging mass spectrometry (MALDI IMS) enables high-specificity spatial investigation of in-tact gangliosides. Here, ganglioside structural and spatial heterogeneity within an S. aureus-infected mouse kidney abscess was characterized. Differences in spatial distributions were observed for gangliosides of different classes and those that differ in ceramide chain composition and oligosaccharide-bound sialic acid. Furthermore, integrating trapped ion mobility spectrometry (TIMS) allowed for the gas-phase separation and visualization of monosialylated ganglioside isomers that differ in sialic acid type and position. The isomers differ in spatial distributions within the host-pathogen interface, where molecular patterns revealed new molecular zones in the abscess previously unidentified by traditional histology.


Staphylococcus aureus
Imaging mass spectrometry
Matrix-assisted laser desorption/ionization
Trapped ion mobility spectrometry
Ion mobility mass spectrometry

Supplementary materials

Supplemental Materials
Ganglioside synthesis pathway; average mass spectrum of control and infected mouse kidney section; tables listing gangliosides identified in a 10 DPI mouse kidney section, including GM3, GM2, GM1, GalNAc- and extended series GM1b, and GD1; on-tissue fragmentation of GalNAc-GM1b; tables list-ing ganglioside isomers identified in 10 DPI mouse kidney, including GM1a and GM1b, and NeuAc-tCer and NeuGc-dCer; on-tissue fragmentation of a- and o-series ganglioside isomers (m/z 1626.95); molecular structures of GM1 isomers detected at m/z 1532.83; detailed on-tissue fragmentation of m/z 1532.83.


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