4MBZ

Structure of B-Lymphotropic Polyomavirus VP1 in complex with 3'-sialyllactosamine

4MBZ の概要

• エントリーDOI: 10.2210/pdb4mbz/pdb
• 関連するPDBエントリー: 4MBX 4MBY
• 関連するBIRD辞書のPRD_ID: PRD_900067
• 分子名称: Major Capsid Protein VP1, N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose, N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
• 機能のキーワード: jelly roll, polyomavirus, viral capsid (structural) protein, dna encapsidation, receptor binding, sialylated oligosaccharides, viral protein
• 由来する生物種: B-lymphotropic polyomavirus
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 307537.48

構造登録者

Khan, Z.M.,Neu, U.,Stehle, T. (登録日: 2013-08-21, 公開日: 2013-12-04, 最終更新日: 2024-04-03)

主引用文献

Neu, U.,Khan, Z.M.,Schuch, B.,Palma, A.S.,Liu, Y.,Pawlita, M.,Feizi, T.,Stehle, T.
Structures of B-Lymphotropic Polyomavirus VP1 in Complex with Oligosaccharide Ligands.
Plos Pathog., 9:e1003714-e1003714, 2013

PubMed Abstract: B-Lymphotropic Polyomavirus (LPyV) serves as a paradigm of virus receptor binding and tropism, and is the closest relative of the recently discovered Human Polyomavirus 9 (HPyV9). LPyV infection depends on sialic acid on host cells, but the molecular interactions underlying LPyV-receptor binding were unknown. We find by glycan array screening that LPyV specifically recognizes a linear carbohydrate motif that contains α2,3-linked sialic acid. High-resolution crystal structures of the LPyV capsid protein VP1 alone and in complex with the trisaccharide ligands 3'-sialyllactose and 3'-sialyl-N-acetyl-lactosamine (3SL and 3SLN, respectively) show essentially identical interactions. Most contacts are contributed by the sialic acid moiety, which is almost entirely buried in a narrow, preformed cleft at the outer surface of the capsid. The recessed nature of the binding site on VP1 and the nature of the observed glycan interactions differ from those of related polyomaviruses and most other sialic acid-binding viruses, which bind sialic acid in shallow, more exposed grooves. Despite their different modes for recognition, the sialic acid binding sites of LPyV and SV40 are half-conserved, hinting at an evolutionary strategy for diversification of binding sites. Our analysis provides a structural basis for the observed specificity of LPyV for linear glycan motifs terminating in α2,3-linked sialic acid, and links the different tropisms of known LPyV strains to the receptor binding site. It also serves as a useful template for understanding the ligand-binding properties and serological crossreactivity of HPyV9.

PubMed: 24204265
DOI: 10.1371/journal.ppat.1003714

実験手法

X-RAY DIFFRACTION (1.75 Å)