Structural and thermodynamic analyses reveal critical features of glycopeptide recognition by the human PILRα immune cell receptor.

@article{Furukawa2017StructuralAT,
  title={Structural and thermodynamic analyses reveal critical features of glycopeptide recognition by the human PILRα immune cell receptor.},
  author={Atsushi Furukawa and Kosuke Kakita and Tomoki Yamada and Mikihiro Ishizuka and Jiro Sakamoto and Nanao Hatori and Naoyoshi Maeda and Fumina Ohsaka and Takashi Saitoh and Takao Nomura and Kimiko Kuroki and Hisanori Nambu and Hisashi Arase and Shigeki Matsunaga and Masahiro Anada and Toyoyuki Ose and Shunichi Hashimoto and Katsumi Maenaka},
  journal={The Journal of biological chemistry},
  year={2017},
  volume={292 51},
  pages={21128-21136}
}
Before entering host cells, herpes simplex virus-1 uses its envelope glycoprotein B to bind paired immunoglobulin-like type 2 receptor α (PILRα) on immune cells. PILRα belongs to the Siglec (sialic acid (SA)-binding immunoglobulin-like lectin)-like family, members of which bind SA. PILRα is the only Siglec member to recognize not only the sialylated O… CONTINUE READING