Ogier J A, Schöller M, Lepoivre Y, Gangloff S, M'Zoughi R, Klein J P
Institut National de la Santé et de la Recherche Médicale Unité 157, Faculté de Chirurgie Dentaire, Strasbourg, France.
Infect Immun. 1991 May;59(5):1620-6. doi: 10.1128/iai.59.5.1620-1626.1991.
Streptococcus mutans surface proteins may be important in immunization against dental caries. We report the existence of an open reading frame of 1,005 bp that lies 1,162 bases upstream of the S. mutans OMZ175 sr gene and that encodes a cell wall-associated protein. This open reading frame codes for 335 amino acid residues. The first 18-amino acid region is predominantly hydrophobic and resembles a signal peptide, and the hydrophobic C-terminal region may function as an anchor to the bacterial cell wall. On the basis of the predicted antigenic determinants of the deduced amino acid sequence, a 16-residue synthetic peptide corresponding to the middle hydrophilic coiled region was synthesized. Antibodies raised against this synthetic peptide reacted with a protein with an apparent Mr of 40,000 that was identified by Western immunoblotting in a cell wall extract from S. mutans OMZ175. The high reactivity in an enzyme-linked immunosorbent assay of the antibodies with whole S. mutans OMZ175 cells showed that this protein was located on the bacterial cell surface. Furthermore, the antipeptide immunoglobulin G recognized an identical determinant on the cell surface of other members of the S. mutans group. However, the function of this protein is not yet known.
变形链球菌表面蛋白在龋齿免疫中可能具有重要作用。我们报告了一个1005 bp的开放阅读框的存在，它位于变形链球菌OMZ175 sr基因上游1162个碱基处，编码一种细胞壁相关蛋白。这个开放阅读框编码335个氨基酸残基。前18个氨基酸区域主要是疏水性的，类似于信号肽，而疏水性的C末端区域可能作为细菌细胞壁的锚定物。根据推导氨基酸序列预测的抗原决定簇，合成了一个与中间亲水性卷曲区域相对应的16个残基的合成肽。针对该合成肽产生的抗体与一种表观分子量为40000的蛋白质发生反应，该蛋白质通过Western免疫印迹法在变形链球菌OMZ175的细胞壁提取物中得到鉴定。抗体在酶联免疫吸附试验中与完整的变形链球菌OMZ175细胞具有高反应性，表明该蛋白质位于细菌细胞表面。此外，抗肽免疫球蛋白G在变形链球菌组其他成员的细胞表面识别相同的决定簇。然而，该蛋白质的功能尚不清楚。
