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TitleInfectious bursal disease virus capsid assembly and maturation by structural rearrangements of a transient molecular switch.
Journal, issue, pagesJ Virol, Vol. 81, Issue 13, Page 6869-6878, Year 2007
Publish dateApr 18, 2007
AuthorsDaniel Luque / Irene Saugar / José F Rodríguez / Nuria Verdaguer / Damiá Garriga / Carmen San Martín / Javier A Velázquez-Muriel / Benes L Trus / José L Carrascosa / José R Castón /
PubMed AbstractInfectious 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- ...Infectious 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 alpha-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 alpha-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 alpha-helix in the precursor capsid, as a five-alpha-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.
External linksJ Virol / PubMed:17442720 / PubMed Central
MethodsEM (single particle)
Resolution7.2 - 14.0 Å
Structure data

EMDB-1237:
Infectious bursal disease virus capsid assembly and maturation by structural rearrangements of a transient molecular switch.
Method: EM (single particle) / Resolution: 7.2 Å

EMDB-1238:
Infectious bursal disease virus capsid assembly and maturation by structural rearrangements of a transient molecular switch.
Method: EM (single particle) / Resolution: 10.4 Å

EMDB-1239:
Infectious bursal disease virus capsid assembly and maturation by structural rearrangements of a transient molecular switch.
Method: EM (single particle) / Resolution: 14.0 Å

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