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5GJ6

Functional and structural characterization of P[19] rotavirus VP8* interaction with histo-blood group antigens

5GJ6 の概要
エントリーDOI10.2210/pdb5gj6/pdb
分子名称Outer capsid protein VP4, SULFATE ION (3 entities in total)
機能のキーワードrotavirus, p[19] vp8*, viral protein
由来する生物種Human rotavirus A
細胞内の位置Host rough endoplasmic reticulum . Virion : Q9Q2P6
タンパク質・核酸の鎖数8
化学式量合計145361.17
構造登録者
Sun, X.,Duan, Z. (登録日: 2016-06-28, 公開日: 2016-09-07, 最終更新日: 2023-11-08)
主引用文献Sun, X.,Li, D.,Peng, R.,Guo, N.,Jin, M.,Zhou, Y.,Xie, G.,Pang, L.,Zhang, Q.,Qi, J.,Duan, Z.J.
Functional and Structural Characterization of P[19] Rotavirus VP8* Interaction with Histo-blood Group Antigens.
J. Virol., 90:9758-9765, 2016
Cited by
PubMed Abstract: Rotaviruses (RVs) of species A (RVA) are a major causative agent of acute gastroenteritis. Recently, histo-blood group antigens (HBGAs) have been reported to interact with human RVA VP8* proteins. Human P[19] is a rare P genotype of porcine origin that infects humans sporadically. The functional and structural characteristics of P[19] VP8* interaction with HBGAs are unknown. In this study, we expressed and purified the VP8* proteins of human and porcine P[19] RVs. In oligosaccharide and saliva binding assays, P[19] VP8* proteins showed obvious binding to A-, B-, and O-type saliva samples irrespective of the secretor status, implying broad binding patterns. However, they did not display specific binding to any of the oligosaccharides tested. In addition, we solved the structure of human P[19] VP8* at 2.4 Å, which revealed a typical galectin-like fold. The structural alignment demonstrated that P[19] VP8* was most similar to that of P[8], which was consistent with the phylogenetic analysis. Structure superimposition revealed the basis for the lack of binding to the oligosaccharides. Our study indicates that P[19] RVs may bind to other oligosaccharides or ligands and may have the potential to spread widely among humans. Thus, it is necessary to place the prevalence and evolution of P[19] RVs under surveillance.
PubMed: 27535055
DOI: 10.1128/JVI.01566-16
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.388 Å)
構造検証レポート
Validation report summary of 5gj6
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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