6ODF

EEEV glycoproteins bound with heparan sulfate

6ODF の概要

• エントリーDOI: 10.2210/pdb6odf/pdb
• EMDBエントリー: 20019
• 分子名称: E1, E2, 2-O-sulfo-beta-L-galactopyranuronic acid-(1-4)-[(2R,3R,4R,5R,6R)-2,4,5-trihydroxy-6-(sulfooxy)tetrahydro-2H-pyran-3-yl]sulfamic acid (3 entities in total)
• 機能のキーワード: eeev, virus
• 由来する生物種: Eastern equine encephalitis virus (EEEV); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 383429.13

構造登録者

Rossmann, M.G.,Chen, C.L. (登録日: 2019-03-26, 公開日: 2020-04-01, 最終更新日: 2024-11-20)

主引用文献

Chen, C.L.,Hasan, S.S.,Klose, T.,Sun, Y.,Buda, G.,Sun, C.,Klimstra, W.B.,Rossmann, M.G.
Cryo-EM structure of eastern equine encephalitis virus in complex with heparan sulfate analogues.
Proc.Natl.Acad.Sci.USA, 117:8890-8899, 2020

PubMed Abstract: Eastern equine encephalitis virus (EEEV), a mosquito-borne icosahedral alphavirus found mainly in North America, causes human and equine neurotropic infections. EEEV neurovirulence is influenced by the interaction of the viral envelope protein E2 with heparan sulfate (HS) proteoglycans from the host's plasma membrane during virus entry. Here, we present a 5.8-Å cryoelectron microscopy (cryo-EM) structure of EEEV complexed with the HS analog heparin. "Peripheral" HS binding sites were found to be associated with the base of each of the E2 glycoproteins that form the 60 quasi-threefold spikes (q3) and the 20 sites associated with the icosahedral threefold axes (i3). In addition, there is one HS site at the vertex of each q3 and i3 spike (the "axial" sites). Both the axial and peripheral sites are surrounded by basic residues, suggesting an electrostatic mechanism for HS binding. These residues are highly conserved among EEEV strains, and therefore a change in these residues might be linked to EEEV neurovirulence.

PubMed: 32245806
DOI: 10.1073/pnas.1910670117

実験手法

ELECTRON MICROSCOPY (5.8 Å)