Iwaki M, Okahashi N, Takahashi I, Kanamoto T, Sugita-Konishi Y, Aibara K, Koga T
Department of Biomedical Research on Foods, National Institute of Health, Tokyo, Japan.
Infect Immun. 1990 Sep;58(9):2929-34. doi: 10.1128/iai.58.9.2929-2934.1990.
A recombinant Streptococcus lactis strain which carries the structural gene for a surface protein antigen (PAc) of 190,000 daltons from Streptococcus mutans serotype c was constructed for development of an oral vaccine against dental caries. The gene from S. mutans MT8148 joined to shuttle vector pSA3 was successfully transformed into S. lactis IL1403. A small amount of PAc was detected in the cell homogenate and cytoplasmic fraction of the recombinant S. lactis, but not in the culture supernatant of the recombinant, by Western immunoblotting and dot immunoblotting. The level of PAc-specific mRNA in the recombinant strain was lower than that in S. mutans MT8148. However, significant salivary immunoglobulin A and serum immunoglobulin G responses to PAc were induced in mice immunized orally with the recombinant S. lactis.
构建了一种重组乳酸链球菌菌株，其携带来自变形链球菌血清型c的190,000道尔顿表面蛋白抗原（PAc）的结构基因，用于开发抗龋齿口服疫苗。来自变形链球菌MT8148的基因与穿梭载体pSA3连接后成功转化到乳酸链球菌IL1403中。通过蛋白质免疫印迹和斑点免疫印迹在重组乳酸链球菌的细胞匀浆和细胞质部分中检测到少量PAc，但在重组菌的培养上清液中未检测到。重组菌株中PAc特异性mRNA的水平低于变形链球菌MT8148中的水平。然而，用重组乳酸链球菌口服免疫的小鼠对PAc产生了显著的唾液免疫球蛋白A和血清免疫球蛋白G反应。
