NDLI: SepM mutation in Streptococcus mutans clinical isolates and related function analysis

Content Provider	Springer Nature : BioMed Central
Author	Liu, Shanshan Shao, Yidan Zhang, Zhenzhen Xu, Wen Liu, Yudong Zhang, Kai Xu, Li Zheng, Qingwei Sun, Yu
Abstract	Background Streptococcus mutans (S. mutans) is an important pathogenic bacterium that causes dental caries, while Streptococcus gordonii (S. gordonii) is a non-cariogenic bacterium that inhibits the growth of S. mutans. The SepM protein can promote the inhibitory ability of S. mutans against S. gordonii by cleaving CSP-21 and activating the ComDE two-component system. This study was designed to explore sepM mutation in S. mutans clinical isolates and related function in the regulation of interactions with S. gordonii. Methods The S. mutans clinical strains that can inhibit the growth of S. gordonii constitute the inhibitory group. 286 C-serotype S. mutans strains were categorized into S. gordonii inhibitory (n = 114) and non-inhibitory bacteria (n = 172). We detected sanger sequencing of sepM gene, the expression levels of related genes and proteins in clinical isolates, obtained prokaryotic expression and purification of mutated proteins, and analyzed the effect of the target mutations on the binding between SepM and CSP-21. Results We found that C482T, G533A, and G661A missense mutations were presented at significantly higher frequency in the inhibitory group relative to the non-inhibitory group. There was no significant difference in the expression of the sepM gene between selected clinical isolates harboring the G533A mutation and the control group. The expression levels of SepM, phosphorylated ComD, and ComE in the mutation group were significantly higher than those in the control group. SepM_control and SepM_D221N (G661A at the gene level) were found to contain two residues close to the active center while SepM_G178D (G533A at the gene level) contained three residues close to the active center. At 25 °C and a pH of 5.5, SepM_D221N (G661A) exhibited higher affinity for CSP-21 (KD = 8.25 µM) than did the SepM control (KD = 33.1 µM), and at 25 °C and a pH of 7.5, SepM_G178D (G533A) exhibited higher affinity (KD = 3.02 µM) than the SepM control (KD = 15.9 µM). It means that it is pH dependent. Conclusions Our data suggest that increased cleavage of CSP-21 by the the mutant SepM may be a reason for the higher inhibitory effect of S. mutans on S. gordonii .
Related Links	https://bmcoralhealth.biomedcentral.com/counter/pdf/10.1186/s12903-024-04436-x.pdf
Ending Page	11
Page Count	11
Starting Page	1
File Format	HTM / HTML
ISSN	14726831
DOI	10.1186/s12903-024-04436-x
Journal	BMC Oral Health
Issue Number	1
Volume Number	24
Language	English
Publisher	BioMed Central
Publisher Date	2024-06-25
Access Restriction	Open
Subject Keyword	Dentistry Oral and Maxillofacial Surgery Gene polymorphism Expression SepM Caries
Content Type	Text
Resource Type	Article
Subject	Dentistry
Journal Impact Factor	2.6/2023
5-Year Journal Impact Factor	3.2/2023

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