3QQ3

Crystal structure of swine major histocompatibility complex class I SLA-1 0401 and identification of 2009 pandemic swine-origin influenza A H1N1 virus cytotoxic T lymphocyte epitope peptides

3QQ3 の概要

• エントリーDOI: 10.2210/pdb3qq3/pdb
• 関連するPDBエントリー: 1Q94 3QQ4
• 分子名称: MHC class I antigen, Beta-2-microglobulin, 9-mer peptide from Neuraminidase, ... (4 entities in total)
• 機能のキーワード: swine mhc class 1, sla-1*0401, epitope of influenza virus, immune system
• 由来する生物種: Sus scrofa (pigs); 詳細
• 細胞内の位置: Secreted (By similarity): Q07717
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 88882.52

構造登録者

Zhang, N.,Qi, J.,Gao, F.,Pan, X.,Chen, R.,Li, Q.,Chen, Z.,Li, X.,Xia, C.,Gao, G.F. (登録日: 2011-02-15, 公開日: 2011-12-28)

主引用文献

Zhang, N.,Qi, J.,Feng, S.,Gao, F.,Liu, J.,Pan, X.,Chen, R.,Li, Q.,Chen, Z.,Li, X.,Xia, C.,Gao, G.F.
Crystal structure of swine major histocompatibility complex class I SLA-1 0401 and identification of 2009 pandemic swine-origin influenza A H1N1 virus cytotoxic T lymphocyte epitope peptides.
J.Virol., 85:11709-11724, 2011

PubMed Abstract: The presentation of viral epitopes to cytotoxic T lymphocytes (CTLs) by swine leukocyte antigen class I (SLA I) is crucial for swine immunity. To illustrate the structural basis of swine CTL epitope presentation, the first SLA crystal structures, SLA-1 0401, complexed with peptides derived from either 2009 pandemic H1N1 (pH1N1) swine-origin influenza A virus (S-OIV(NW9); NSDTVGWSW) or Ebola virus (Ebola(AY9); ATAAATEAY) were determined in this study. The overall peptide-SLA-1 0401 structures resemble, as expected, the general conformations of other structure-solved peptide major histocompatibility complexes (pMHC). The major distinction of SLA-1 0401 is that Arg(156) has a "one-ballot veto" function in peptide binding, due to its flexible side chain. S-OIV(NW9) and Ebola(AY9) bind SLA-1 0401 with similar conformations but employ different water molecules to stabilize their binding. The side chain of P7 residues in both peptides is exposed, indicating that the epitopes are "featured" peptides presented by this SLA. Further analyses showed that SLA-1 0401 and human leukocyte antigen (HLA) class I HLA-A 0101 can present the same peptides, but in different conformations, demonstrating cross-species epitope presentation. CTL epitope peptides derived from 2009 pandemic S-OIV were screened and evaluated by the in vitro refolding method. Three peptides were identified as potential cross-species influenza virus (IV) CTL epitopes. The binding motif of SLA-1 0401 was proposed, and thermostabilities of key peptide-SLA-1 0401 complexes were analyzed by circular dichroism spectra. Our results not only provide the structural basis of peptide presentation by SLA I but also identify some IV CTL epitope peptides. These results will benefit both vaccine development and swine organ-based xenotransplantation.

PubMed: 21900158
DOI: 10.1128/JVI.05040-11

実験手法

X-RAY DIFFRACTION (2.59 Å)