Structural determination of the Australian bat lyssavirus nucleoprotein and phosphoprotein complex

Camilla M. Donnelly; Murray Stewart; Justin A. Roby; Vinod Sundaramoorthy; Jade K. Forwood

doi:10.3390/v16010033

Structural determination of the Australian bat lyssavirus nucleoprotein and phosphoprotein complex

Camilla M. Donnelly, Murray Stewart, Justin A. Roby, Vinod Sundaramoorthy, Jade K. Forwood

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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 (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.

Original language	English
Article number	33
Pages (from-to)	1-13
Number of pages	13
Journal	Viruses
Volume	16
Issue number	1
Early online date	Dec 2023
DOIs	https://doi.org/10.3390/v16010033
Publication status	Published - Jan 2024

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439419295 Published articleFinal published version, 3.18 MBLicence: CC BY

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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 (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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AU - Donnelly, Camilla M.

AU - Stewart, Murray

AU - Roby, Justin A.

AU - Sundaramoorthy, Vinod

AU - Forwood, Jade K.

PY - 2024/1

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AB - 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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KW - X-ray crystallography

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Structural determination of the Australian bat lyssavirus nucleoprotein and phosphoprotein complex

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