Structural Determination of the Australian Bat Lyssavirus Nucleoprotein and Phosphoprotein Complex

被引：1
作者：
Donnelly, Camilla M. [1 ,2 ,3 ]
Stewart, Murray [4 ]
Roby, Justin A. [1 ,2 ]
Sundaramoorthy, Vinod [3 ,5 ]
Forwood, Jade K. [1 ,2 ]
机构：
[1] Charles Sturt Univ, Sch Dent & Med Sci, Wagga Wagga, NSW 2678, Australia
[2] Charles Sturt Univ, Gulbali Inst, Wagga Wagga, NSW 2678, Australia
[3] CSIRO, Australian Ctr Dis Preparedness, Diagnost Surveillance & Response, Geelong, Vic 3219, Australia
[4] Cambridge Biomed Campus, MRC Lab Mol Biol, Francis Crick Ave, Cambridge CB2 0QH, England
[5] Deakin Univ, Sch Med, Geelong, Vic 3216, Australia
来源：
VIRUSES-BASEL | 2024年 / 16卷 / 01期
关键词：
rhabdovirus; Australian bat lyssavirus; rabies virus; phosphoprotein; nucleoprotein; nucleocapsid; X-ray crystallography; small-angle X-ray scattering; RABIES VIRUS NUCLEOPROTEIN; P PROTEIN; INTERFERON ANTAGONIST; ENSEMBLE STRUCTURE; CRYSTAL-STRUCTURE; RNA; IDENTIFICATION; TRANSCRIPTION; PHOSPHORYLATION; REPLICATION;
D O I：
10.3390/v16010033
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
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 (N0P) 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 N0P demonstrated a highly conserved interface in this complex. Because the N0P interface is conserved in the lyssaviruses of phylogroup I, it is an attractive therapeutic target for multiple rabies-causing viral species.
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页数：13
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