Proline-rich protein from S. mutans can perform a competitive mineralization function to enhance bacterial adhesion to teeth

A proline-rich region was found in Streptococcus mutans (S. mutans) surface antigen I/II (Ag I/II). The functions of this region were explored to determine its role in the cariogenic abilities of S. mutans; specifically, the proline-rich region was compared with human amelogenin. The full-length amelogenin genes were cloned from human (AmH) and surface antigen I/II genes from S. mutans. Then, the genes expressed and purified. We analyzed the structure and self-assembly ability of AmH and Ag I/II, compared their capacities to induce mineralization, and assessed the adhesion ability of S. mutans to AmH- and Ag I/II-coated tooth slices. AmH formed ordered chains and net frames in the early stage of protein self-assembly, while Ag I/II formed irregular and overlapping structures. AmH induced mineralization possessed a parallel rosary structure, while Ag I/II-induced mineralization is rougher and more irregular. The S. mutans adhesion assay indicated that the adhesion ability S. mutans on the Ag I/II-induced crystal layer was significantly higher than that on the AmH-induced crystal layer. S. mutans' Ag I/II may have evolved to resemble human amelogenin and form a rougher crystal layer on teeth, which play a competitive mineralization role and promotes better bacterial adhesion and colonization. Thus, the cariogenic ability of S. mutans Ag I/II is increased.

Automated summary

A proline-rich region was found in the surface antigen I/II of Streptococcus mutans. This region was compared with human amelogenin to explore its role in the cariogenic abilities of S. mutans. The study revealed differences between Ag I/II and amelogenin in terms of protein self-assembly, mineralization induction, and bacterial adhesion ability.