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Updated: Jan 21, 2026

Purification of a High Molecular Mass Protein in Streptococcus mutans
Published on: September 14, 2019
Sortase A-mediated modification of the Streptococcus mutans transcriptome and virulence traits
Xuan Chen1, Chengcheng Liu1,2, Xian Peng1
1State Key Laboratory of Oral Diseases, National Clinical Research Center for Oral Diseases, Sichuan University, Chengdu, China.
Sortase A (SrtA) deletion in Streptococcus mutans enhances acid tolerance and reduces exopolysaccharide (EPS) production, impacting virulence. These changes are linked to altered gene transcription.
Area of Science:
- Microbiology
- Molecular Biology
- Genomics
Background:
- Sortase A (SrtA) in Streptococcus mutans anchors surface proteins, contributing to adhesion and biofilm formation.
- Limited functional characterization exists for SrtA and its gene (srtA) beyond adhesion roles.
Purpose of the Study:
- To investigate the impact of srtA deletion on Streptococcus mutans virulence determinants beyond adhesion.
- To explore if observed effects are due to changes in genomic transcription.
Main Methods:
- Acid-killing assays, glycolytic rate assessments, and exopolysaccharide (EPS) formation tests were employed.
- RNA-sequencing was performed on both wild-type and srtA-deleted strains during exponential and stationary growth phases.
Main Results:
- SrtA deletion enhanced aciduricity under direct pH 2.8 exposure, but this was repressed with pre-induced acid tolerance.
- Reduced EPS formation was observed in mature biofilms of the srtA mutant strain.
- SrtA deletion caused significant, growth-phase-dependent transcriptional changes, affecting genes related to aciduricity, carbohydrate transport, and EPS formation.
Conclusions:
- Streptococcus mutans srtA plays a multifaceted role in virulence, influencing acid tolerance and glucan formation.
- Transcriptional alterations resulting from srtA loss partially explain the observed changes in virulence traits.
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