A protein with simultaneous capsid scaffolding and dsRNA-binding activities enhances the birnavirus capsid mechanical stability
Entity
UAM. Departamento de Física de la Materia CondensadaPublisher
Nature Publishing GroupDate
2015-09-04Citation
10.1038/srep13486
Scientific Reports 5 (2015): 13486
ISSN
2045-2322DOI
10.1038/srep13486Funded by
This work was supported by grants from the Spanish Ministry of Economy and Competitivity (FIS2011-29493 to PJP, BFU2011-29038 to JLC and BFU2014-55475R to JRC) and Comunidad Autónoma de Madrid (S2013/MIT-2850 to JLC and S2013/MIT-2807 to JRC)Project
Gobierno de España. FIS2011-29493; Gobierno de España. BFU2011-29038; Gobierno de España. BFU2014-55475R; Comunidad de Madrid. S2013/MIT-2850/NANOFRONTMAG-CM; Comunidad de Madrid. S2013/MIT-2807/NANOBIOSOMAEditor's Version
http://dx.doi.org/10.1038/srep13486Subjects
Viral capsids; Multifunctional proteins; Ribonucleoproteins (RNP); Capsid structural; FísicaAbstract
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 capsidstabilizing and genetic information platforms
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Google Scholar:Mertens, Johann
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Casado, Santiago
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Mata, Carlos P.
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Hernando Pérez, Mercedes
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Pablo Gómez, Pedro José de
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Carrascosa, José L.
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Castón, José R.
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