Application of Mass Spectrometry-Based Multi-Omics in Biomedical Research

A special issue of Life (ISSN 2075-1729). This special issue belongs to the section "Medical Research".

Deadline for manuscript submissions: 26 June 2026 | Viewed by 539

Special Issue Editors


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Guest Editor
Mass Spectrometry Technology Access Center at McDonnell Genome Institute (MTAC@MGI), Washington University in Saint Louis School of Medicine, St. Louis, MO, USA
Interests: mass spectrometry-based multi-omics applications

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Co-Guest Editor
Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO, USA
Interests: mass spectrometry-based applications

Special Issue Information

Dear Colleagues,

Mass spectrometry (MS) has long been a cornerstone of molecular analysis, but its full potential is now being realized through integrated, multi-omics strategies that combine proteomics, metabolomics, lipidomics, and mass spectrometry imaging (MSI).

Proteomics provides insight into protein abundance and post-translational modifications, while metabolomics and lipidomics capture metabolic states that reflect cellular function and phenotype. MSI adds a powerful spatial dimension, localizing molecules directly within tissues and revealing heterogeneity that bulk analyses overlook. When integrated, these platforms enable researchers not only to identify molecular changes but also to place them in a functional and anatomical context, paving the way for breakthroughs in precision medicine, oncology, neurology, cardiovascular research, and drug development.

This Special Issue seeks research articles, reviews, and technical advances that leverage MS-based multi-omics in biomedical research. Submissions may include the following:

  • Integrated omics workflows combining two or more MS-based modalities;
  • Spatial multi-omics and MSI applications in disease biology or drug delivery;
  • Novel sample preparation, acquisition strategies, or data analysis pipelines;
  • Translational studies identifying biomarkers or therapeutic targets;
  • Computational and statistical methods for multi-omics data integration.

By bringing together leaders across analytical chemistry, bioinformatics, and translational science, this Special Issue aims to highlight innovations that expand the capabilities and impact of MS-based multi-omics in modern biomedical research.

Prof. Dr. Young Ah Goo
Guest Editor

Dr. Byoung-Kyu Cho
Co-Guest Editor

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Keywords

  • mass spectrometry
  • multi-omics
  • proteomics
  • metabolomics
  • lipidomics
  • mass spectrometry imaging (MSI)
  • biomarker discovery
  • translational research

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Published Papers (1 paper)

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Research

18 pages, 5736 KB  
Article
Macrophage Proteomic Profiling Reveals Divergent TLR4-Dependent and -Independent Responses to Kdo2-Lipid A and Lipid IVa
by Jiraphorn Issara-Amphorn, Jenna L. Schoonmaker, Clinton Bradfield, Sung Hwan Yoon, Iain D. C. Fraser and Aleksandra Nita-Lazar
Life 2026, 16(5), 753; https://doi.org/10.3390/life16050753 - 1 May 2026
Viewed by 257
Abstract
Macrophages harness pattern recognition receptors (PRRs) to detect conserved bacterial components and mount effective immune responses. Many Gram-negative bacteria modify their lipid A structures to limit recognition by Toll-like receptor 4 (TLR4) and cytosolic Caspase-11 lipopolysaccharide sensors. One common evasion strategy is to [...] Read more.
Macrophages harness pattern recognition receptors (PRRs) to detect conserved bacterial components and mount effective immune responses. Many Gram-negative bacteria modify their lipid A structures to limit recognition by Toll-like receptor 4 (TLR4) and cytosolic Caspase-11 lipopolysaccharide sensors. One common evasion strategy is to reduce the lipid A acylation state from hexa- to tetra-acylation. This alteration can limit binding to receptors and dampen subsequent immune signaling responses, yet the proteomic alterations associated with this altered immunogenicity remain incompletely understood. Here, we systematically profiled proteomic alterations induced by extracellular or transfected hexa-acylated Kdo2-lipid A (Kdo2) and tetra-acylated lipid-IVa (IVa) to assess TLR4-dependent, TLR4-independent, and non-canonical inflammasome activation pathways. Kdo2 elicited stronger inflammatory responses in immortalized bone-marrow-derived macrophages (iBMDMs), as evidenced by robust TNF production, Caspase-11 cleavage, and IL-1α/IL-1β release. In contrast, IVa elicited minimal TNF secretion and failed to effectively induce non-canonical inflammasome activation. Global label-free quantitative proteomic analysis of iBMDMs stimulated with a low dose of immunogenic LPS displayed route-specific immune signatures: enrichment of TNF signaling, interferon-associated pathways, and mitochondrial metabolic remodeling. Equimolar amounts of low-acylated LPS failed to effectively induce these immune signatures, supporting a threshold-dependent model in which the lipid A structure and route of exposure define inflammatory progression. Collectively, our findings provide mechanistic insight into how lipid A structural variation modulates macrophage immune programming and cytosolic inflammasome activation. Full article
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