A protein with simultaneous capsid scaffolding and dsRNA-binding activities enhances the birnavirus capsid mechanical stability

Scientific Reports
Johann MertensJosé R Castón

Abstract

Viral capsids are metastable structures that perform many essential processes; they also act as robust cages during the extracellular phase. Viruses can use multifunctional proteins to optimize resources (e.g., VP3 in avian infectious bursal disease virus, IBDV). The IBDV genome is organized as ribonucleoproteins (RNP) of dsRNA with VP3, which also acts as a scaffold during capsid assembly. We characterized mechanical properties of IBDV populations with different RNP content (ranging from none to four RNP). The IBDV population with the greatest RNP number (and best fitness) showed greatest capsid rigidity. When bound to dsRNA, VP3 reinforces virus stiffness. These contacts involve interactions with capsid structural subunits that differ from the initial interactions during capsid assembly. Our results suggest that RNP dimers are the basic stabilization units of the virion, provide better understanding of multifunctional proteins, and highlight the duality of RNP as capsid-stabilizing and genetic information platforms.

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Citations

Jan 19, 2017·International Journal of Molecular Sciences·Yao Qin, Shijun J Zheng
Oct 31, 2017·Journal of Physics. Condensed Matter : an Institute of Physics Journal·Elena PascualJosé R Castón
Apr 15, 2018·Journal of Biological Physics·Pedro J de PabloJosé L Carrascosa
Dec 13, 2017·Journal of Physics. Condensed Matter : an Institute of Physics Journal·Olga KononovaValeri Barsegov
Mar 16, 2018·Journal of Virology·María Cecilia GimenezLaura Ruth Delgui
Jul 20, 2018·Journal of Virology·Carlos P MataJosé R Castón
Nov 2, 2018·Analytical Chemistry·Panagiotis KondylisStephen C Jacobson

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Methods Mentioned

BETA
X-ray
atomic force microscopy
AFM
electrophoresis

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