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Infectious bursal disease virus capsid assembly and maturation by structural rearrangements of a transient molecular switch

AutorLuque, Daniel; Saugar, Irene ; Rodríguez, José Francisco; Verdaguer, Núria ; Garriga, Damià; San Martín, Carmen; Velázquez-Muriel, Javier; Trus, Benes L.; Carrascosa, José L.; Castón, José R.
Fecha de publicaciónjul-2007
EditorAmerican Society for Microbiology
CitaciónJournal of Virology 81(13): 6869-6878 (2007)
ResumenInfectious bursal disease virus (IBDV), a double-stranded RNA (dsRNA) virus belonging to the Birnaviridae family, is an economically important avian pathogen. The IBDV capsid is based on a single-shelled T=13 lattice, and the only structural subunits are VP2 trimers. During capsid assembly, VP2 is synthesized as a protein precursor, called pVP2, whose 71-residue C-terminal end is proteolytically processed. The conformational flexibility of pVP2 is due to an amphipathic α-helix located at its C-terminal end. VP3, the other IBDV major structural protein that accomplishes numerous roles during the viral cycle, acts as a scaffolding protein required for assembly control. Here we address the molecular mechanism that defines the multimeric state of the capsid protein as hexamers or pentamers. We used a combination of three-dimensional cryo-electron microscopy maps at or close to subnanometer resolution with atomic models. Our studies suggest that the key polypeptide element, the C-terminal amphipathic α-helix, which acts as a transient conformational switch, is bound to the flexible VP2 C-terminal end. In addition, capsid protein oligomerization is also controlled by the progressive trimming of its C-terminal domain. The coordination of these molecular events correlates viral capsid assembly with different conformations of the amphipathic α-helix in the precursor capsid, as a five-α-helix bundle at the pentamers or an open star-like conformation at the hexamers. These results, reminiscent of the assembly pathway of positive single-stranded RNA viruses, such as nodavirus and tetravirus, add new insights into the evolutionary relationships of dsRNA viruses. Copyright © 2007, American Society for Microbiology. All Rights Reserved.
Versión del editorhttp://dx.doi.org/10.1128/JVI.00077-07
Identificadoresdoi: 10.1128/JVI.00077-07
issn: 0022-538X
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