Structural insights into the multifunctional protein VP3 of birnaviruses

Structure
Arnau CasañasNúria Verdaguer

Abstract

Infectious bursal disease virus (IBDV), a member of the Birnaviridae family, is the causative agent of one of the most harmful poultry diseases. The IBDV genome encodes five mature proteins; of these, the multifunctional protein VP3 plays an essential role in virus morphogenesis. This protein, which interacts with the structural protein VP2, with the double-stranded RNA genome, and with the virus-encoded, RNA-dependent RNA polymerase, VP1, is involved not only in the formation of the viral capsid, but also in the recruitment of VP1 into the capsid and in the encapsidation of the viral genome. Here, we report the X-ray structure of the central region of VP3, residues 92-220, consisting of two alpha-helical domains connected by a long and flexible hinge that are organized as a dimer. Unexpectedly, the overall fold of the second VP3 domain shows significant structural similarities with different transcription regulation factors.

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Citations

Jan 24, 2009·Proceedings of the National Academy of Sciences of the United States of America·Daniel LuqueJosé R Castón
May 24, 2012·The Journal of Biological Chemistry·Nerea IrigoyenJosé F Rodríguez
Dec 10, 2008·Journal of Molecular Biology·Daniel LuqueJosé R Castón
Mar 16, 2018·Journal of Virology·María Cecilia GimenezLaura Ruth Delgui
Jul 20, 2018·Journal of Virology·Carlos P MataJosé R Castón
Dec 28, 2012·Journal of Virology·Olivier EscaffreNicolas Eterradossi
Jan 4, 2013·Journal of Virology·Mohammad W BaharJonathan M Grimes
Aug 28, 2015·Journal of Virology·Diego FerreroNúria Verdaguer
Nov 27, 2020·Journal of Virology·Diego S FerreroNuria Verdaguer

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