The N-terminal fragment of GRP94 is sufficient for peptide presentation via professional antigen-presenting cells.

@article{Biswas2006TheNF,
  title={The N-terminal fragment of GRP94 is sufficient for peptide presentation via professional antigen-presenting cells.},
  author={Chhanda Biswas and Uma Sriram and Bogoljub Ciric and Olga Ostrovsky and Stefania Gallucci and Yair Argon},
  journal={International immunology},
  year={2006},
  volume={18 7},
  pages={1147-57}
}
The chaperone glucose-regulated protein 94 (GRP94) has long been used to augment peptide presentation to T cells. This chaperone binds antigenic peptides, binds to receptors on professional antigen-presenting cells (APCs), activates these cells and after internalization, transfers the peptides to MHC class I for activation of T cells. Here we show that all these activities reside within amino acids 1-355 of GRP94. This small fragment is sufficient to bind peptides, to bind and be taken up by… CONTINUE READING