Binding of the Streptococcus gordonii surface glycoproteins GspB and Hsa to specific carbohydrate structures on platelet membrane glycoprotein Ibalpha.

@article{Takamatsu2005BindingOT,
  title={Binding of the Streptococcus gordonii surface glycoproteins GspB and Hsa to specific carbohydrate structures on platelet membrane glycoprotein Ibalpha.},
  author={Daisuke Takamatsu and Barbara A. Bensing and Hui Cheng and Gary A Jarvis and Ian R Siboo and Jose Alejandro Poveda Lopez and John Mcleod Griffiss and Paul M Sullam},
  journal={Molecular microbiology},
  year={2005},
  volume={58 2},
  pages={380-92}
}
GspB and Hsa are homologous serine-rich surface glycoproteins of Streptococcus gordonii strains M99 and Challis, respectively, that mediate the binding of these organisms to platelet membrane glycoprotein (GP) Ibalpha. Both GspB and Hsa consist of an N-terminal putative signal peptide, a short serine-rich region, a region (BR) that is rich in basic amino acids, a longer serine-rich region and a C-terminal cell wall anchoring domain. To further assess the mechanisms for GspB and Hsa binding, we… CONTINUE READING

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