6KX9

Crystal structure of 8-mer peptide from avian influenza H5N1 virus in complex with BF2*1501

6KX9 の概要

• エントリーDOI: 10.2210/pdb6kx9/pdb
• 分子名称: MHC class I, Beta-2-microglobulin, 8-pepide (ARG-ARG-ALA-LEU-ARG-GLU-GLY-TYR), ... (4 entities in total)
• 機能のキーワード: mhc class i, chicken, avian influenza virus, h5n1, epitope, 8-mer, immune system
• 由来する生物種: Gallus gallus (Chicken); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 43295.81

構造登録者

Xiao, L.,Zhang, L. (登録日: 2019-09-10, 公開日: 2020-04-01, 最終更新日: 2023-11-22)

主引用文献

Li, X.,Zhang, L.,Liu, Y.,Ma, L.,Zhang, N.,Xia, C.
Structures of the MHC-I molecule BF2*1501 disclose the preferred presentation of an H5N1 virus-derived epitope.
J.Biol.Chem., 295:5292-5306, 2020

PubMed Abstract: Lethal infections by strains of the highly-pathogenic avian influenza virus (HPAIV) H5N1 pose serious threats to both the poultry industry and public health worldwide. A lack of confirmed HPAIV epitopes recognized by cytotoxic T lymphocytes (CTLs) has hindered the utilization of CD8 T-cell-mediated immunity and has precluded the development of effectively diversified epitope-based vaccination approaches. In particular, an HPAIV H5N1 CTL-recognized epitope based on the peptide MHC-I-β2m (pMHC-I) complex has not yet been designed. Here, screening a collection of selected peptides of several HPAIV strains against a specific pathogen-free pMHC-I (pBF2*1501), we identified a highly-conserved HPAIV H5N1 CTL epitope, named HPAIV-PA We determined the structure of the BF2*1501-PA complex at 2.1 Å resolution to elucidate the molecular mechanisms of a preferential presentation of the highly-conserved PA epitope in the chicken B15 lineage. Conformational characteristics of the PA epitope with a protruding Tyr-7 residue indicated that this epitope has great potential to be recognized by specific TCRs. Moreover, significantly increased numbers of CD8 T cells specific for the HPAIV-PA epitope in peptide-immunized chickens indicated that a repertoire of CD8 T cells can specifically respond to this epitope. We anticipate that the identification and structural characterization of the PA epitope reported here could enable further studies of CTL immunity against HPAIV H5N1. Such studies may aid in the development of vaccine development strategies using well-conserved internal viral antigens in chickens.

PubMed: 32152225
DOI: 10.1074/jbc.RA120.012713

実験手法

X-RAY DIFFRACTION (2.902 Å)