4POS

Structure of Human Polyomavirus 9 VP1 pentamer in complex with 3'-sialyllactosamine

4POS の概要

• エントリーDOI: 10.2210/pdb4pos/pdb
• 関連するPDBエントリー: 4FMI 4MBZ 4POQ 4POR 4POT
• 関連するBIRD辞書のPRD_ID: PRD_900067
• 分子名称: VP1, N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (6 entities in total)
• 機能のキーワード: jelly roll fold, capsid formation, receptor interaction, carbohydrate, sialyloligosaccharide, viral coat protein, viral protein
• 由来する生物種: Human polyomavirus 9
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 310514.98

構造登録者

Khan, Z.M.,Stehle, T. (登録日: 2014-02-26, 公開日: 2014-04-09, 最終更新日: 2024-11-20)

主引用文献

Khan, Z.M.,Liu, Y.,Neu, U.,Gilbert, M.,Ehlers, B.,Feizi, T.,Stehle, T.
Crystallographic and glycan microarray analysis of human polyomavirus 9 VP1 identifies N-glycolyl neuraminic acid as a receptor candidate.
J.Virol., 88:6100-6111, 2014

PubMed Abstract: Human polyomavirus 9 (HPyV9) is a closely related homologue of simian B-lymphotropic polyomavirus (LPyV). In order to define the architecture and receptor binding properties of HPyV9, we solved high-resolution crystal structures of its major capsid protein, VP1, in complex with three putative oligosaccharide receptors identified by glycan microarray screening. Comparison of the properties of HPyV9 VP1 with the known structure and glycan-binding properties of LPyV VP1 revealed that both viruses engage short sialylated oligosaccharides, but small yet important differences in specificity were detected. Surprisingly, HPyV9 VP1 preferentially binds sialyllactosamine compounds terminating in 5-N-glycolyl neuraminic acid (Neu5Gc) over those terminating in 5-N-acetyl neuraminic acid (Neu5Ac), whereas LPyV does not exhibit such a preference. The structural analysis demonstrated that HPyV9 makes specific contacts, via hydrogen bonds, with the extra hydroxyl group present in Neu5Gc. An equivalent hydrogen bond cannot be formed by LPyV VP1.

PubMed: 24648448
DOI: 10.1128/JVI.03455-13

実験手法

X-RAY DIFFRACTION (2 Å)