Structural basis for simultaneous recognition of an O-glycan and its attached peptide of mucin family by immune receptor PILRα

Kimiko Kuroki, Jing Wang, Toyoyuki Ose, Munechika Yamaguchi, Shigekazu Tabata, Nobuo Maita, Seiko Nakamura, Mizuho Kajikawa, Amane Kogure, Takeshi Satoh, Hisashi Arase, Katsumi Maenaka

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22 Citations (Scopus)

Abstract

Paired Ig-like type 2 receptor α (PILRα) recognizes a wide range of O-glycosylated mucin and related proteins to regulate broad immune responses. However, the molecular characteristics of these recognitions are largely unknown. Here we show that sialylated O-linked sugar T antigen (sTn) and its attached peptide region are both required for ligand recognition by PILRα. Furthermore, we determined the crystal structures of PILRα and its complex with an sTn and its attached peptide region. The structures show that PILRα exhibits large conformational change to recognize simultaneously both the sTn O-glycan and the compact peptide structure constrained by proline residues. Binding and functional assays support this binding mode. These findings provide significant insight into the binding motif and molecular mechanism (which is distinct from sugar-recognition receptors) by which O-glycosylated mucin proteins with sTn modifications are recognized in the immune system as well as during viral entry.

Original languageEnglish
Pages (from-to)8877-8882
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume111
Issue number24
DOIs
Publication statusPublished - 2014

All Science Journal Classification (ASJC) codes

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    Kuroki, K., Wang, J., Ose, T., Yamaguchi, M., Tabata, S., Maita, N., Nakamura, S., Kajikawa, M., Kogure, A., Satoh, T., Arase, H., & Maenaka, K. (2014). Structural basis for simultaneous recognition of an O-glycan and its attached peptide of mucin family by immune receptor PILRα. Proceedings of the National Academy of Sciences of the United States of America, 111(24), 8877-8882. https://doi.org/10.1073/pnas.1324105111