| Title | Phosphosite-dependent presentation of dual phosphorylated peptides MHC class I molecules |
| Authors | Zhao, Yingze Sun, Mingwei Zhang, Nan Liu, Xueyuan Yue, Can Feng, Lei Ji, Shushen Liu, Xiao Qi, Jianxun Wong, Catherine C. L. Gao, George F. Liu, William J. |
| Affiliation | Chinese Ctr Dis Control & Prevent China CDC, Natl Inst Viral Dis Control & Prevent, NHC Key Lab Biosafety, Beijing 100052, Peoples R China Chinese Acad Med Sci, Res Unit Adapt Evolut & Control Emerging Viruses, Beijing 102206, Peoples R China Chinese Acad Sci, Inst Microbiol, CAS Key Lab Pathogen Microbiol & Immunol, Beijing 100101, Peoples R China Peking Univ, Peking Univ Hlth Sci Ctr, Ctr Preds Med Multiom Res, Beijing 100191, Peoples R China Shandong Univ, Cheeloo Coll Med, Sch Publ Hlth, Jinan 250012, Peoples R China Univ Chinese Acad Sci, Savaid Med Sch, Beijing 100049, Peoples R China |
| Keywords | PROTEIN RECOGNITION SEQUENCE SUITE |
| Issue Date | 15-Apr-2022 |
| Publisher | ISCIENCE |
| Abstract | Phosphopeptides presented by major histocompatibility complex (MHC) class I have been regarded as a pivotal type of cancer neoantigens that are recognized by T cells. The structural basis of single-phosphorylated peptide presentation has been well studied. Diphosphorylation with one interval between two sites is one of the prevalent forms of multisite-phosphorylated peptides. Herein, we determined the molecular basis of presentation of two P4/P6 double pS-containing peptides by HLA-B27 and compared them with unmodified and single-phosphorylated peptide complexes. These data clarified not only the HLA allele-specific presentation of phosphopeptides by MHC class I molecules but also the cooperativity of peptide conformation within P4 and P6 phosphorylation sites. The phosphorylation of P6 site can influence the binding mode of P4 phosphorylated site to HLA-B27. And we found the diphospho-dependent attenuated effect of peptide binding affinity. This study provides insights into the MHC presentation features of diphosphopeptides, which is different from monophosphopeptides. |
| URI | http://hdl.handle.net/20.500.11897/642865 |
| DOI | 10.1016/j.isci.2022.104013 |
| Indexed | SCI(E) |
| Appears in Collections: | 医学部待认领 |
