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Journal of Virology, December 2006, p. 11456-11466, Vol. 80, No. 23
0022-538X/06/$08.00+0     doi:10.1128/JVI.01468-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Generation of Filamentous Instead of Icosahedral Particles by Repression of African Swine Fever Virus Structural Protein pB438L{triangledown}

Carolina Epifano,1 Jacomine Krijnse-Locker,2 María L. Salas,1 José Salas,1 and Javier M. Rodríguez1*

Centro de Biología Molecular Severo Ochoa (Consejo Superior de Investigaciones Científicas-Universidad Autónoma de Madrid), Universidad Autónoma de Madrid, Cantoblanco, 28049 Madrid, Spain,1 European Molecular Biology Laboratory, Cell Biology and Biophysics Program, Heidelberg, Germany2

Received 11 July 2006/ Accepted 14 September 2006

The mechanisms involved in the construction of the icosahedral capsid of the African swine fever virus (ASFV) particle are not well understood at present. Capsid formation requires protein p72, the major capsid component, but other viral proteins are likely to play also a role in this process. We have examined the function of the ASFV structural protein pB438L, encoded by gene B438L, in virus morphogenesis. We show that protein pB438L associates with membranes during the infection, behaving as an integral membrane protein. Using a recombinant ASFV that inducibly expresses protein pB438L, we have determined that this structural protein is essential for the formation of infectious virus particles. In the absence of the protein, the virus assembly sites contain, instead of icosahedral particles, large aberrant tubular structures of viral origin as well as bilobulate forms that present morphological similarities with the tubules. The filamentous particles, which possess an aberrant core shell domain and an inner envelope, are covered by a capsid-like layer that, although containing the major capsid protein p72, does not acquire icosahedral morphology. This capsid, however, is to some extent functional, as the filamentous particles can move from the virus assembly sites to the plasma membrane and exit the cell by budding. The finding that, in the absence of protein pB438L, the viral particles formed have a tubular structure in which the icosahedral symmetry is lost supports a role for this protein in the construction or stabilization of the icosahedral vertices of the virus particle.

* Corresponding author. Mailing address: Centro de Biología Molecular Severo Ochoa (CSIC-UAM), Facultad de Ciencias, Universidad Autónoma de Madrid, Cantoblanco, 28049 Madrid, Spain. Phone: 34 91 497 84 38. Fax: 34 91 497 47 99. E-mail: jrodriguez{at}cbm.uam.es.

{triangledown} Published ahead of print on 27 September 2006.

Journal of Virology, December 2006, p. 11456-11466, Vol. 80, No. 23
0022-538X/06/$08.00+0     doi:10.1128/JVI.01468-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Rodriguez, I., Nogal, M. L., Redrejo-Rodriguez, M., Bustos, M. J., Salas, M. L. (2009). The African Swine Fever Virus Virion Membrane Protein pE248R Is Required for Virus Infectivity and an Early Postentry Event. J. Virol. 83: 12290-12300 [Abstract] [Full Text]  


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