Proteomic Studies of Staphylococcus aureus Pathogenicity

Staphylococcus aureus remains a leading cause of hospital- and community-acquired infections worldwide, ranging from superficial skin lesions to life-threatening pneumonia and sepsis. Proteomic approaches have become central to unravel the complexity of its pathogenic arsenal by mapping the entire complement of proteins expressed under diverse conditions. High-resolution mass spectrometry, quantitative labelling strategies and data-independent acquisition workflows have enabled comprehensive profiling of cytosolic, secreted and surface-associated proteins. These efforts have illuminated dynamic changes in metabolic enzymes, stress-response regulators and virulence factors during host colonisation, intracellular survival and biofilm formation. By comparing global proteomes from clinical isolates, mutant strains and in vivo models, researchers have identified novel antigens, adaptive signatures and potential therapeutic targets. This expanding proteomic knowledge is crucial for the development of rapid diagnostics, effective vaccines and next-generation antimicrobials against this versatile pathogen.

Research from Nature Portfolio

Recent studies have established a global ion library for data-independent acquisition mass spectrometry, achieving high-accuracy quantification of S. aureus proteins in both cell culture and animal models. Time-resolved analyses in human bronchial epithelial cells revealed temporal regulation of the SigB-dependent stress response alongside shifts in translation, fermentation and amino acid biosynthesis. In a murine pneumonia model, in vivo adaptation was characterised by increased abundance of oxidative stress response and fermentation proteins, coupled with downregulation of ribosomal subunits. This work provides an unprecedented view of proteome adaptation during infection. In a complementary investigation, seroproteomic profiling of ten non-covalently cell wall-bound proteins demonstrated elevated immunoglobulin G responses in patients with chronic wounds compared to healthy carriers. The study pinpointed highly immunogenic surface antigens that may serve as vaccine candidates or biomarkers of in vivo expression.

Proteomic Studies of Staphylococcus aureus Pathogenicity publication trend

The graph below shows the total number of articles in proteomic studies of staphylococcus aureus pathogenicity across all publications each year (not limited to Nature Index journals).

Technical terms

Proteome: The complete set of proteins expressed by an organism under a given condition.

Proteomics: Large-scale study of proteomes, typically involving identification and quantification of proteins by mass spectrometry.

Mass spectrometry: An analytical technique that measures the mass-to-charge ratio of ionised particles, essential for protein identification and quantification.

Secretome: The subset of proteins actively secreted or released by a cell or organism into the extracellular environment.

Surfaceome: The collection of proteins located on or associated with the cell surface, often involved in host-pathogen interactions.

Data-independent acquisition (DIA): A mass spectrometry method that systematically fragments all ions in a predefined mass range, allowing comprehensive and reproducible protein quantification.

References

1. A global Staphylococcus aureus proteome resource applied to the in vivo characterization of host-pathogen interactions. Scientific Reports (2017).
2. Human antibody responses against non-covalently cell wall-bound Staphylococcus aureus proteins. Scientific Reports (2018).
3. Surface-Shaving of Staphylococcus aureus Strains and Quantitative Proteomic Analysis Reveal Differences in Protein Abundance of the Surfaceome. Microorganisms (2024).
4. Comparative Secretome Analyses of Human and Zoonotic Staphylococcus aureus Isolates CC8, CC22, and CC398*. Molecular & Cellular Proteomics (2018).