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


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2015-10

AUTHORS

Johann Mertens, Santiago Casado, Carlos P Mata, Mercedes Hernando-Pérez, Pedro J de Pablo, José L Carrascosa, José 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. More... »

PAGES

13486

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/srep13486

DOI

http://dx.doi.org/10.1038/srep13486

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1045542224

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/26336920


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