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Journal of Virology, November 2001, p. 10815-10828, Vol. 75, No. 22
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.22.10815-10828.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

C Terminus of Infectious Bursal Disease Virus Major Capsid Protein VP2 Is Involved in Definition of the T Number for Capsid Assembly

José R. Castón,1 Jorge L. Martínez-Torrecuadrada,2 Antonio Maraver,3 Eleuterio Lombardo,3 José F. Rodríguez,3 J. Ignacio Casal,2 and José L. Carrascosa1,*

Departments of Structure of Macromolecules1 and Molecular and Cellular Biology,3 Centro Nacional de Biotecnología, CSIC, Campus Universidad Autónoma de Madrid, 28049 Madrid, and Ingenasa, 28037 Madrid,2 Spain

Received 25 April 2001/Accepted 31 July 2001

Infectious bursal disease virus (IBDV), a member of the Birnaviridae family, is a double-stranded RNA virus. The IBDV capsid is formed by two major structural proteins, VP2 and VP3, which assemble to form a T=13 markedly nonspherical capsid. During viral infection, VP2 is initially synthesized as a precursor, called VPX, whose C end is proteolytically processed to the mature form during capsid assembly. We have computed three-dimensional maps of IBDV capsid and virus-like particles built up by VP2 alone by using electron cryomicroscopy and image-processing techniques. The IBDV single-shelled capsid is characterized by the presence of 260 protruding trimers on the outer surface. Five classes of trimers can be distinguished according to their different local environments. When VP2 is expressed alone in insect cells, dodecahedral particles form spontaneously; these may be assembled into larger, fragile icosahedral capsids built up by 12 dodecahedral capsids. Each dodecahedral capsid is an empty T=1 shell composed of 20 trimeric clusters of VP2. Structural comparison between IBDV capsids and capsids consisting of VP2 alone allowed the determination of the major capsid protein locations and the interactions between them. Whereas VP2 forms the outer protruding trimers, VP3 is found as trimers on the inner surface and may be responsible for stabilizing functions. Since elimination of the C-terminal region of VPX is correlated with the assembly of T=1 capsids, this domain might be involved (either alone or in cooperation with VP3) in the induction of different conformations of VP2 during capsid morphogenesis.

* Corresponding author. Mailing address: Departamento de Estructura de Macromoléculas, Centro Nacional de Biotecnología, CSIC, Campus UAM, Cantoblanco, 28049 Madrid, Spain. Phone: 34-91-585- 4509. Fax: 34-91-585-4506. E-mail: jlcarrascosa{at}cnb.uam.es.

Journal of Virology, November 2001, p. 10815-10828, Vol. 75, No. 22
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.22.10815-10828.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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