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Comprehensive Mass Spectrometric Survey of Streptococcus pyogenes Subcellular Proteomes
Laura Wilk1, Lotta Happonen1, Johan Malmström1
1Division of Infection Medicine, Department of Clinical Sciences, Lund University , Lund, Sweden.
Abstract:
Streptococcus pyogenes is a major global health burden causing a wide variety of diseases. Because a vaccine against this bacterium is still lacking, vaccine candidates or antimicrobial therapies are urgently needed. Here we use an invasive and clinically relevant streptococcal M1 serotype to characterize the bacterial proteome in-depth. An elaborate fractionation technique is employed to separate the different cell fractions, followed by shotgun mass-spectrometry analysis, allowing us to confirm the expression of nearly two-thirds (1022) of the 1690 open reading frames predicted for the streptococcal M1 reference proteome. In contrast with other studies, we present the entire isolated membrane proteome, which opens up a whole new source for drug targets. We show both the unique and most prevalent proteins for each cellular fraction and analyze the presence of predicted cell-wall-anchored proteins and lipoproteins. With our approach, we also identify a variety of novel proteins whose presence has not been reported in previous proteome studies. Proteins of interest, potential virulence factors, and drug or vaccine targets are discussed for each cellular fraction. Overall, the results of this work represent the so-far widest proteomic approach to characterize the protein composition and localization in S. pyogenes.
Insights
This study deeply characterizes the Streptococcus pyogenes proteome, identifying novel drug and vaccine targets. The research provides a comprehensive map of bacterial proteins, crucial for developing new antimicrobial therapies against this global health threat.
Area of Science:
- Microbiology
- Proteomics
- Bacteriology
Background:
- Streptococcus pyogenes is a significant global health concern causing diverse diseases.
- There is a critical need for vaccines and antimicrobial therapies due to the lack of a current vaccine.
- An invasive and clinically relevant M1 serotype was chosen for in-depth proteomic characterization.
Purpose of the Study:
- To comprehensively characterize the proteome of Streptococcus pyogenes M1 serotype.
- To identify novel proteins and potential drug or vaccine targets.
- To present the complete isolated membrane proteome as a source for new therapeutic strategies.
Main Methods:
- Utilized an elaborate cell fractionation technique to isolate different bacterial cell components.
- Performed shotgun mass-spectrometry analysis for in-depth proteome characterization.
- Analyzed the presence and localization of cell-wall-anchored proteins and lipoproteins.
Main Results:
- Confirmed expression of nearly two-thirds (1022/1690) of predicted open reading frames.
- Presented the entire isolated membrane proteome, a novel resource for drug discovery.
- Identified numerous novel proteins not previously reported in S. pyogenes proteome studies.
- Characterized unique and prevalent proteins within each cellular fraction.
Conclusions:
- This study represents the most extensive proteomic analysis of S. pyogenes to date.
- The findings offer valuable insights into bacterial protein composition and localization.
- Identified potential virulence factors and novel targets for vaccine and drug development against S. pyogenes infections.
