Interaction between two putative glycosyltransferases is required for glycosylation of a serine-rich streptococcal adhesin.

@article{Bu2008InteractionBT,
  title={Interaction between two putative glycosyltransferases is required for glycosylation of a serine-rich streptococcal adhesin.},
  author={Su Hong Bu and Yirong Li and Meixian Zhou and Parastoo Azadin and Meiqin Zeng and PAULA M. FIVES-TAYLOR and Hui Wu},
  journal={Journal of bacteriology},
  year={2008},
  volume={190 4},
  pages={1256-66}
}
Fap1, a serine-rich glycoprotein, is essential for fimbrial biogenesis and biofilm formation of Streptococcus parasanguinis (formerly S. parasanguis). Fap1-like proteins are conserved in many streptococci and staphylococci and have been implicated in bacterial virulence. Fap1 contains two serine-rich repeat regions that are modified by O-linked glycosylation. A seven-gene cluster has been identified, and this cluster is implicated in Fap1 biogenesis. In this study, we investigated the initial… CONTINUE READING