Characterization of the collagen-binding S-layer protein CbsA of Lactobacillus crispatus.

@article{Sillanp2000CharacterizationOT,
  title={Characterization of the collagen-binding S-layer protein CbsA of Lactobacillus crispatus.},
  author={Jouko Sillanp{\"a}{\"a} and B Mart{\'i}nez and Jenni Antikainen and Takahiro Toba and Nisse Kalkkinen and S Tankka and Kari Lounatmaa and Juha Ker{\"a}nen and Magnus H{\"o}{\"o}k and Benita Westerlund-Wikstr{\"o}m and Peter H. Pouwels and Timo K. Korhonen},
  journal={Journal of bacteriology},
  year={2000},
  volume={182 22},
  pages={6440-50}
}
The cbsA gene of Lactobacillus crispatus strain JCM 5810, encoding a protein that mediates adhesiveness to collagens, was characterized and expressed in Escherichia coli. The cbsA open reading frame encoded a signal sequence of 30 amino acids and a mature polypeptide of 410 amino acids with typical features of a bacterial S-layer protein. The cbsA gene product was expressed as a His tag fusion protein, purified by affinity chromatography, and shown to bind solubilized as well as immobilized… CONTINUE READING