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

被引：25

作者：

Mertens, Johann ^{[1
,2
]}

Casado, Santiago ^{[1
]}

Mata, Carlos P. ^{[3
]}

Hernando-Perez, Mercedes ^{[4
]}

de Pablo, Pedro J. ^{[4
]}

Carrascosa, Jose L. ^{[2
,3
]}

Caston, Jose R. ^{[2
,3
]}

机构：

[1] Inst Madrileno Estudios Avanzados Nanociencia IMD, Madrid 28049, Spain

[2] Unidad Asociada Nanobiotecnol CNB CSIC IMDEA, E-28049 Madrid, Spain

[3] CSIC, Ctr Nacl Biotecnol, Dept Struct Macromol, E-28049 Madrid, Spain

[4] Univ Autonoma Madrid, Dept Fis Mat Condensada Co3, E-28049 Madrid, Spain

来源：

SCIENTIFIC REPORTS | 2015年 / 5卷

关键词：

BURSAL DISEASE VIRUS; STRUCTURAL POLYMORPHISM; CRYSTAL-STRUCTURE; CATALYTIC DYAD; RNA-POLYMERASE; VP3; IDENTIFICATION; DOMAIN; INTERPLAY; DYNAMICS;

D O I：

10.1038/srep13486

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页数：11

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