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.
journal_name
Sci Repjournal_title
Scientific reportsauthors
Mertens J,Casado S,Mata CP,Hernando-Pérez M,de Pablo PJ,Carrascosa JL,Castón JRdoi
10.1038/srep13486subject
Has Abstractpub_date
2015-09-04 00:00:00pages
13486issn
2045-2322pii
srep13486journal_volume
5pub_type
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