国际口腔医学杂志Issue(5):578-582,5.DOI:10.7518/gjkq.2015.05.023
齿垢密螺旋体主要外鞘蛋白的结构和作用机制
Structure and action mechanism of major outer sheath protein of Treponema denticola
摘要
Abstract
The major outer sheath protein(Mosp), which consists of glucose, galactose, glutamine, galactosamine, and fucose, is the most abundant outer membrane protein on the cell surface of Treponema denticola(T.denticola) at low molecular polymer form. The central domain of Mosp plays a significant role in the adhesion of bacteria and the host proteins. Mosp also acts as an adhesion to some extent, thereby competitively inhibiting the combination of T.denticola, Porphyromonas gingivalis, and Fusobacterium nucleatum. Cytotoxicity is another contributing factor that allows the bacteria to obtain nutrients, transport bacterial products to the infected host cells, and mediate cytotoxic activity. Furthermore, the Mosp can destroy the migration of fibroblasts and neutrophils. However, the migration of fibroblasts is closely related to reconstruction and healing in periodontal connective tissues, whereas neutrophils play key roles in the periodontal innate immune system, thereby enabling neutrophils to limit the spread of pathogens. Understanding the mechanism underlying Mosp activity may provide new insights intothe reduction of T.denticola pathogenicity and may lay a solid theoretical foundation fordelaying the progression of periodontitis.关键词
齿垢密螺旋体/主要外鞘蛋白/牙周炎Key words
Treponema denticola/major outer sheath protein/periodontitis分类
生物科学引用本文复制引用
王骏,吴冷,赵蕾,吴亚菲..齿垢密螺旋体主要外鞘蛋白的结构和作用机制[J].国际口腔医学杂志,2015,(5):578-582,5.基金项目
国家自然科学基金(81371150);教育部留学回国人员科研启动基金(2013-693-11-11);卫生部牙周病科国家临床重点专科基金 ()