摘要
表面蛋白抗原Ⅰ/Ⅱ(AgⅠ/Ⅱ、P1、PAc、SpaP、SspA、SspB等)广泛存在于口腔链球菌细胞壁表面,介导变异链球菌、表兄链球菌、格登链球菌等口腔链球菌与牙表面的黏附,影响牙菌斑的形成,是影响龋病形成和发展的主要毒力因子之一。自有研究报道了变异链球菌表面蛋白抗原Ⅰ/Ⅱ的V区(SpaP-V)晶体结构之后,陆续有其AgⅠ/Ⅱ的三维结构、格登链球菌V区(SspB-V)的三维结构和C末端(SspB-C)的三维结构见诸报道,逐步揭示了口腔链球菌表面蛋白抗原Ⅰ/Ⅱ的三维立体结构,进一步解释了其功能机制。本文就口腔链球菌表面蛋白抗原的三维结构和相关功能表位的研究情况作一综述。
Surface proteins, such as Ag I / II, P1, PAc, SpaP, SspA, and SspB, are widely observed in oral Streptococcus. These proteins mediate the attachment of Streptococcus mutans, Streptococcus sobrinus, Streptococcus gordonii, and so on to tooth surfaces, influence the formation of dental plaque, and are the main virulent factors for the development of caries diseases. The crystal structure of region V ofAg I / II （SpaP-V） was first studied, after which research on the 3D structures of the full-length Ag I / II as well as regions V and C of SspB was performed. The 3D structures of Ag I / II were also gradually elucidated to better explain the mechanism of function of the proteins. Research advances on the 3D structure of Ag I /II and the related functional epitopes are finally reviewed.
出处
《国际口腔医学杂志》
CAS
2013年第5期670-673,共4页
International Journal of Stomatology
关键词
变异链球菌
表面蛋白抗原
三维结构
功能表位
Streptococcus mutans
surface protein antigen
three dimensional structure
functional epitope
