Backbone trace of partitivirus capsid protein from electron cryomicroscopy and homology modeling.

Biophysical Journal
Jinghua TangTimothy S Baker

Abstract

Most dsRNA viruses have a genome-enclosing capsid that comprises 120 copies of a single coat protein (CP). These 120 CP subunits are arranged as asymmetrical dimers that surround the icosahedral fivefold axes, forming pentamers of dimers that are thought to be assembly intermediates. This scheme is violated, however, in recent structures of two dsRNA viruses, a fungal virus from family Partitiviridae and a rabbit virus from family Picobirnaviridae, both of which have 120 CP subunits organized as dimers of quasisymmetrical dimers. In this study, we report the CP backbone trace of a second fungal partitivirus, determined in this case by electron cryomicroscopy and homology modeling. This virus also exhibits quasisymmetrical CP dimers that are connected by prominent surface arches and stabilized by domain swapping between the two CP subunits. The CP fold is dominated by alpha-helices, although beta-strands mediate several important contacts. A dimer-of-dimers assembly intermediate is again implicated. The disordered N-terminal tail of each CP subunit protrudes into the particle interior and likely interacts with the genome during packaging and/or transcription. These results broaden our understanding of conserved and variable aspe...Continue Reading

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Citations

Oct 12, 2010·Nucleic Acids Research·Catherine L LawsonWah Chiu
May 20, 2011·Journal of Virology·Xiaodong YanTimothy S Baker
Nov 7, 2012·Current Opinion in Virology·Max L Nibert, Yuko Takagi
Oct 18, 2011·Journal of Molecular Biology·Jinghua TangTimothy S Baker
Mar 17, 2015·Virology·Said A GhabrialNobuhiro Suzuki
Apr 15, 2016·PLoS Pathogens·Aaron M CollierYizhi J Tao
Jun 24, 2019·Virus Genes·Karel Petrzik
May 13, 2011·The Journal of General Virology·Jennifer L MillerTrevor Sewell
May 27, 2017·Archives of Virology·Hongliu AnFan Li
Sep 13, 2018·Viruses·Daniel LuqueJosé R Castón

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