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Journal of Virology, December 2006, p. 12260-12270, Vol. 80, No. 24
0022-538X/06/$08.00+0     doi:10.1128/JVI.01323-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

The African Swine Fever Virus Nonstructural Protein pB602L Is Required for Formation of the Icosahedral Capsid of the Virus Particle{triangledown}

Carolina Epifano,1 Jacomine Krijnse-Locker,2 María L. Salas,1 Javier M. Rodríguez,1* and José Salas2

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 23 June 2006/ Accepted 3 October 2006

African swine fever virus (ASFV) protein pB602L has been described as a molecular chaperone for the correct folding of the major capsid protein p72. We have studied the function of protein pB602L during the viral assembly process by using a recombinant ASFV, vB602Li, which inducibly expresses the gene coding for this protein. We show that protein pB602L is a late nonstructural protein, which, in contrast with protein p72, is excluded from the viral factory. Repression of protein pB602L synthesis inhibits the proteolytic processing of the two viral polyproteins pp220 and pp62 and leads to a decrease in the levels of protein p72 and a delocalization of the capsid protein pE120R. As shown by electron microscopy analysis of cells infected with the recombinant virus vB602Li, the viral assembly process is severely altered in the absence of protein pB602L, with the generation of aberrant "zipper-like" structures instead of icosahedral virus particles. These "zipper-like" structures are similar to those found in cells infected under restrictive conditions with the recombinant virus vA72 inducibly expressing protein p72. Immunoelectron microscopy studies show that the abnormal forms generated in the absence of protein pB602L contain the inner envelope protein p17 and the two polyproteins but lack the capsid proteins p72 and pE120R. These findings indicate that protein pB602L is essential for the assembly of the icosahedral capsid 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 11 October 2006.

Journal of Virology, December 2006, p. 12260-12270, Vol. 80, No. 24
0022-538X/06/$08.00+0     doi:10.1128/JVI.01323-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.





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