COMPARISON OF STREPTOCOCCUS-MUTANS AND STREPTOCOCCUS-SANGUIS RECEPTORS FOR HUMAN SALIVARY AGGLUTININ
COMPARISON OF STREPTOCOCCUS-MUTANS AND STREPTOCOCCUS-SANGUIS RECEPTORS FOR HUMAN SALIVARY AGGLUTININ
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DOI：
10.1016/0882-4010(90)90022-i
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发表时间：
1990-09-01
影响因子：
3.8
通讯作者：
MALAMUD, D
中科院分区：
文献类型：
--
作者：
DEMUTH, DR;LAMMEY, MS;MALAMUD, D
口腔链球菌对唾液凝集素介导的聚集的敏感性各不相同。为了了解这种特异性的分子基础，比较了变形链球菌KPSK 2（MSL-1）和血链球菌M5（SSP-5）凝集素受体的结构和功能。免疫学筛选一株S.对变形链球菌KPSK 2（MSL-1）和血链球菌M5（SSP-5）进行了比较。免疫学筛选一株S.变形链球菌KPSK 2基因组DNA文库产生了两个相同的克隆，其表达与来自该生物体的SDS提取物中的220 kDa肽共迁移的链球菌蛋白。该蛋白抑制凝集素介导的S.以剂量依赖性方式抑制变形杆菌KPSK 2。MSL-1基因与S.变异株SpaP和pac基因，尽管单个碱基取代改变了几个氨基酸。MSL-1与从S.血吸虫M5所有三种蛋白质MSL-1、P1和SSP-5共享至少一个表位，因为单克隆和多克隆抗SSP-5抗体与MSL-1和P1两者反应。然而，其他单克隆抗体对SSP-5具有特异性，并且似乎与与MSL-1或P1几乎没有同源性的肽结构域反应。糖抑制研究表明，凝集素介导的S。岩藻糖和乳糖对变形杆菌KPSK 2的抑制作用最强。唾液酸是S.血凝素与S.变异株KPSK 2.这些结果表明，虽然MSL-1和SSP-5蛋白在遗传和免疫学上相关，但它们对凝集素结合位点的特异性不同。
Oral streptococci vary in their susceptibility to salivary agglutinin-mediated aggregation. To understand the molecular basis of this specificity, the structure and function of receptors for agglutinin from Streptococcus mutans KPSK2 (MSL-1) and Streptococcus sanguis M5 (SSP-5) were compared. Immunological screening of an S. mutans KPSK2 (MSL-1) and Streptococcus sanguis M5 (SSP-5) were compared. Immunological screening of an S. mutans KPSK2 genomic DNA library yielded two identical clones expressing a streptococcal protein that co-migrated with a 220 kDa peptide in SDS extracts from this organism. This protein inhibited agglutinin-mediated aggregation of S. mutans KPSK2 in a dose-dependent manner. The MSL-1 gene is homologous to the S. mutans SpaP and pac genes although single base substitutions alter several amino acids. MSL-1 is also similar to the agglutinin receptor (SSP-5) cloned from S. sanguis M5. All three proteins, MSL-1, P1, and SSP-5 share at least one epitope since monoclonal and polyclonal anti-SSP-5 antibodies react with both MSL-1 and P1. However, other monoclonal antibodies are specific for SSP-5 and appear to react with a peptide domain exhibiting little homology to MSL-1 or P1. Sugar inhibition studies showed that agglutinin-mediated aggregation of S. mutans KPSK2 was most potently inhibited by fucose and lactose. Sialic acid, a potent inhibitor of S. sanguis aggregation, had no effect on the interaction of agglutinin with S. mutans KPSK2. These results suggest that while the MSL-1 and SSP-5 proteins are genetically and immunologically related, their specificity for binding sites on agglutinin differs.