Structure analysis and site-directed mutagenesis of defined key residues and motives for pilus-related sortase C1 in group B Streptococcus.

@article{Cozzi2011StructureAA,
  title={Structure analysis and site-directed mutagenesis of defined key residues and motives for pilus-related sortase C1 in group B Streptococcus.},
  author={Roberta Cozzi and Enrico Malito and Annalisa Nuccitelli and Mariapina D'Onofrio and Manuele Martinelli and Ilaria Ferlenghi and Guido Grandi and John L. Telford and Domenico Maione and C. Daniela Rinaudo},
  journal={FASEB journal : official publication of the Federation of American Societies for Experimental Biology},
  year={2011},
  volume={25 6},
  pages={
          1874-86
        }
}
In group B Streptococcus (GBS), 3 structurally distinct types of pili have been discovered as potential virulence factors and vaccine candidates. The pilus-forming proteins are assembled into high-molecular-weight polymers via a transpeptidation mechanism mediated by specific class C sortases. Using a multidisciplinary approach including bioinformatics, structural and biochemical studies, and in vivo mutagenesis, we performed a broad characterization of GBS sortase C1 of pilus island 2a. The… CONTINUE READING

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