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Related Experiment Video

Updated: May 6, 2026

A Protocol for Functional Assessment of Whole-Protein Saturation Mutagenesis Libraries Utilizing High-Throughput Sequencing
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SepM mutation in Streptococcus mutans clinical isolates and related function analysis.

Shanshan Liu1,2, Yidan Shao2, Zhenzhen Zhang3

  • 1Department of Stomatology, The First Affiliated Hospital of Bengbu Medical College, 287 Chuang Huai Road, Bengbu, 233004, China.

BMC Oral Health
|June 25, 2024
PubMed
Summary

Mutations in the Streptococcus mutans sepM gene enhance its ability to inhibit Streptococcus gordonii growth. These sepM mutations increase the cleavage of CSP-21, leading to a stronger inhibitory effect.

Keywords:
CariesExpressionGene polymorphismSepM

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Area of Science:

  • Microbiology
  • Bacterial Pathogenesis
  • Molecular Biology

Background:

  • Streptococcus mutans (S. mutans) causes dental caries.
  • Streptococcus gordonii (S. gordonii) inhibits S. mutans growth.
  • The SepM protein in S. mutans promotes inhibition of S. gordonii by cleaving CSP-21 and activating the ComDE system.

Purpose of the Study:

  • Investigate sepM mutations in S. mutans clinical isolates.
  • Determine the role of sepM mutations in regulating S. mutans interactions with S. gordonii.

Main Methods:

  • Categorized 286 S. mutans strains into inhibitory (n=114) and non-inhibitory (n=172) groups.
  • Performed Sanger sequencing of the sepM gene.
  • Analyzed gene/protein expression, purified mutated proteins, and assessed SepM-CSP-21 binding affinity.

Main Results:

  • C482T, G533A, and G661A mutations were more frequent in the inhibitory group.
  • Mutant SepM (G533A, G661A) showed increased binding affinity to CSP-21 in a pH-dependent manner.
  • Expression of SepM, phosphorylated ComD, and ComE was higher in isolates with G533A mutation.

Conclusions:

  • Mutant sepM enhances S. mutans inhibition of S. gordonii.
  • Increased CSP-21 cleavage by mutant SepM contributes to the inhibitory effect.