The sortase of Streptococcus mutans mediates cell wall anchoring of a surface protein antigen.

Sortase has been shown to be a protease that catalyzes the cell wall anchoring of surface proteins containing an LPXTG motif in gram-positive bacteria. In this study, we determined the complete nucleotide sequence of the sortase gene (srtA) of Streptococcus mutans and found a surface protein that was linked to the cell wall by the sortase. The results show that srtA gene of S. mutans consisted of 741 bp and encoded for a sortase protein of 246 amino acids with a molecular weight of 27 489. The deduced amino acid sequence of the S. mutans sortase was highly homologous (65-58%) to those of other Streptococcal species. In a S. mutans mutant lacking sortase, two surface proteins of 200 and 75 kDa were released to the culture supernatant. Western blot analysis with specific antiserum showed that the 200 kDa protein was a surface protein antigen designated PAc. These results suggest that the sortase catalyzes anchoring of the antigen PAc to the cell wall.