8FWL

Crystal structure of Australian bat lyssavirus nucleoprotein in complex with phosphoprotein chaperone

8FWL の概要

• エントリーDOI: 10.2210/pdb8fwl/pdb
• 分子名称: Phosphoprotein,Nucleoprotein, DI(HYDROXYETHYL)ETHER (3 entities in total)
• 機能のキーワード: chaperone, lyssavirus, nucleoprotein, phosphoprotein, rabies, viral protein
• 由来する生物種: Lyssavirus australis; 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 63901.60

構造登録者

Donnelly, C.M.,Stewart, M.,Forwood, J.K. (登録日: 2023-01-23, 公開日: 2023-03-08, 最終更新日: 2024-03-20)

主引用文献

Donnelly, C.M.,Stewart, M.,Roby, J.A.,Sundaramoorthy, V.,Forwood, J.K.
Structural Determination of the Australian Bat Lyssavirus Nucleoprotein and Phosphoprotein Complex.
Viruses, 16:33-33, 2023

PubMed Abstract: Australian bat lyssavirus (ABLV) shows similar clinical symptoms as rabies, but there are currently no protein structures available for ABLV proteins. In lyssaviruses, the interaction between nucleoprotein (N) and phosphoprotein (N) in the absence of RNA generates a complex (NP) that is crucial for viral assembly, and understanding the interface between these two proteins has the potential to provide insight into a key feature: the viral lifecycle. In this study, we used recombinant chimeric protein expression and X-ray crystallography to determine the structure of ABLV nucleoprotein bound to residues 1-40 of its phosphoprotein chaperone. Comparison of our results with the recently generated structure of RABV CVS-11 NP demonstrated a highly conserved interface in this complex. Because the NP interface is conserved in the lyssaviruses of phylogroup I, it is an attractive therapeutic target for multiple rabies-causing viral species.

PubMed: 38229694
DOI: 10.3390/v16010033

実験手法

X-RAY DIFFRACTION (2.19 Å)