Streptococcus mutans cell division protein FtsZ has higher GTPase and polymerization activities in acidic environment. (13th March 2022)

• Record Type: Journal Article
• Authors: Chen, Yuxing; Li, Yongliang; Yuan, Chongyang; Liu, Shujun; Xin, Fengjiao; Deng, Xuliang; Wang, Xiaoyan
• Is Part Of: Molecular oral microbiology. Volume 37:Number 3(2022)
• Page Start: 97
• Page End: 108
• Publication Date: 2022-03-13
• Subjects: FtsZ -- GTPase -- polymerization -- Streptococcus mutans; Mouth -- Microbiology -- Periodicals; Respiratory infections -- Microbiology -- Periodicals; Mouth -- Diseases -- Immunological aspects -- Periodicals; 617.522
• DOI: 10.1111/omi.12364
• Languages: English
• ISSNs: 2041-1006

Abstract

Abstract: The acid tolerance of Streptococcus mutans plays an important role in its cariogenic process. Streptococcus mutans initiates a powerful transcriptional and physiological adaptation mechanism, eventually shielding the cellular machinery from acid damage and contributing to bacterial survival under acidic stress conditions. Although S. mutans contains complex regulatory systems, existing studies have shown that S. mutans, unlike Escherichia coli, cannot maintain a neutral intracellular environment. As the pH of the extracellular environment decreases, the intracellular pH decreases in parallel. There is insufficient knowledge regarding the acid resistance of the intracellular proteins of S. mutans, particularly when it comes to the key cytoskeletal division protein FtsZ. In this study, the data showed that S. mutans had similar cell division progress in acidic and neutral environments. The splitting position was in the middle of cells, and the cytoplasm was divided evenly in the acidic environment. Additionally, the tread milling velocity of S. mutans FtsZ in the middle of cells was not affected by the acidic environment. Streptococcus mutans FtsZ had higher GTPase activity in pH 6.0 buffer than in the neutral environment. Furthermore, the polymerization of S. mutans FtsZ in the acidic environment was more robust than that in the neutral environment. After two particular amino acids of S. mutans, FtsZ amino acids were mutated (E88K, L269K), the polymerization of S. mutans FtsZ in the acidic environment was significantly reduced. Overall, S. mutans FtsZ exhibited higher functional activity in pH 6.0 buffer in vitro. The acid resistance of S. mutans FtsZ is affected by its particular amino acids.