Journal of Microbiology

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Mannose phosphotransferase system subunit IID of Streptococcus mutans elicits maturation and activation of dendritic cells: Sungho Jeong, Chaeyeon Park, Dongwook Lee, Hyun Jung Ji, Ho Seong Seo, Cheol-Heui Yun, Jintaek Im, Seung Hyun Han; J. Microbiol. 2025;63(10):e2505014. Published online October 31, 2025; DOI: https://doi.org/10.71150/jm.2505014

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Abstract PDF: Streptococcus mutans is a Gram-positive pathogen that causes dental caries and subsequent pulpal infection leading to pulpitis. Although dendritic cells (DCs) are known to be involved in disease progression and immune responses during S. mutans infection, little is known about which component of S. mutans is responsible for the DC responses. Although the mannose phosphotransferase system (Man-PTS) is the primary sugar transporter of S. mutans, it is also a potential virulence factor. Since Man-PTS subunit IID (ManIID) embedded on the bacterial membrane is indispensable for Man-PTS function, we investigated its role in the maturation and activation of DCs stimulated with a ManIID-deficient strain (Δpts) of S. mutans and recombinant ManIID (rManIID) protein. When mouse bone marrow-derived DCs were treated with heat-killed S. mutans wild-type (WT) or Δpts, bacterial adherence and internalization of Δpts were lower than those of WT. Moreover, the heat-killed S. mutans Δpts strain was inferior to the wild-type in inducing expression of phenotypic maturation markers, such as CD80, CD86, MHC-I, and MHC-II, and proinflammatory cytokine, IL-6. In line with the trends in marker expression, the endocytic capacity of DCs treated with the Δpts strain was comparable to that of untreated DCs whereas DCs treated with the WT strain dose-dependently lost their endocytic capacity. Furthermore, rManIID dose-dependently promoted both phenotypic maturation marker expression and IL-6 production by DCs. Collectively, these results demonstrate that ManIID plays a crucial role in the adhesion and internalization of S. mutans into DCs and is one of the major immune-stimulating agents responsible for maturation and activation of DCs during S. mutans infection.

Journal Article

Short-chain fatty acids inhibit the biofilm formation of Streptococcus gordonii through negative regulation of competence-stimulating peptide signaling pathway: Taehwan Park , Jintaek Im , A Reum Kim , Dongwook Lee , Sungho Jeong , Cheol-Heui Yun , Seung Hyun Han; J. Microbiol. 2021;59(12):1142-1149. Published online December 4, 2021; DOI: https://doi.org/10.1007/s12275-021-1576-8

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Streptococcus gordonii, a Gram-positive commensal bacterium, is an opportunistic pathogen closely related to initiation and progression of various oral diseases, such as periodontitis and dental caries. Its biofilm formation is linked with the development of such diseases by enhanced resistance against antimicrobial treatment or host immunity. In the present study, we investigated the effect of short-chain fatty acids (SCFAs) on the biofilm formation of S. gordonii. SCFAs, including sodium acetate (NaA), sodium propionate (NaP), and sodium butyrate (NaB), showed an effective inhibitory activity on the biofilm formation of S. gordonii without reduction in bacterial growth. SCFAs suppressed S. gordonii biofilm formation at early time points whereas SCFAs did not affect its preformed biofilm. A quorum-sensing system mediated by competence-stimulating peptide (CSP) is known to regulate biofilm formation of streptococci. Interestingly, SCFAs substantially decreased mRNA expression of comD and comE, which are CSP-sensor and its response regulator responsible for CSP pathway, respectively. Although S. gordonii biofilm formation was enhanced by exogenous synthetic CSP treatment, such effect was not observed in the presence of SCFAs. Collectively, these results suggest that SCFAs have an anti-biofilm activity on S. gordonii through inhibiting comD and comE expression which results in negative regulation of CSP quorum-sensing system. SCFAs could be an effective anti-biofilm agent against S. gordonii for the prevention of oral diseases.

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