6P7S

Crystal Structure of the Cedar henipavirus Attachment G Glycoprotein globular domain in complex with the receptor ephrin-B1

6P7S の概要

• エントリーDOI: 10.2210/pdb6p7s/pdb
• 分子名称: Attachment glycoprotein, Ephrin-B1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: cedar virus, attachment, glycoprotein, g protein, viral protein, receptor, ephrin-b1, henipavirus
• 由来する生物種: Cedar virus; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 133778.77

構造登録者

Xu, K.,Nikolov, D.B.,Xu, Y. (登録日: 2019-06-06, 公開日: 2019-09-25, 最終更新日: 2024-10-23)

主引用文献

Laing, E.D.,Navaratnarajah, C.K.,Cheliout Da Silva, S.,Petzing, S.R.,Xu, Y.,Sterling, S.L.,Marsh, G.A.,Wang, L.F.,Amaya, M.,Nikolov, D.B.,Cattaneo, R.,Broder, C.C.,Xu, K.
Structural and functional analyses reveal promiscuous and species specific use of ephrin receptors by Cedar virus.
Proc.Natl.Acad.Sci.USA, 116:20707-20715, 2019

PubMed Abstract: Cedar virus (CedV) is a bat-borne henipavirus related to Nipah virus (NiV) and Hendra virus (HeV), zoonotic agents of fatal human disease. CedV receptor-binding protein (G) shares only ∼30% sequence identity with those of NiV and HeV, although they can all use ephrin-B2 as an entry receptor. We demonstrate that CedV also enters cells through additional B- and A-class ephrins (ephrin-B1, ephrin-A2, and ephrin-A5) and report the crystal structure of the CedV G ectodomain alone and in complex with ephrin-B1 or ephrin-B2. The CedV G receptor-binding site is structurally distinct from other henipaviruses, underlying its capability to accommodate additional ephrin receptors. We also show that CedV can enter cells through mouse ephrin-A1 but not human ephrin-A1, which differ by 1 residue in the key contact region. This is evidence of species specific ephrin receptor usage by a henipavirus, and implicates additional ephrin receptors in potential zoonotic transmission.

PubMed: 31548390
DOI: 10.1073/pnas.1911773116

実験手法

X-RAY DIFFRACTION (3.49 Å)