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Journal of Virology, December 2009, p. 12290-12300, Vol. 83, No. 23
0022-538X/09/$08.00+0     doi:10.1128/JVI.01333-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

The African Swine Fever Virus Virion Membrane Protein pE248R Is Required for Virus Infectivity and an Early Postentry Event {triangledown}

Irene Rodríguez, María L. Nogal, Modesto Redrejo-Rodríguez, María J. Bustos, and María L. Salas*

Centro de Biología Molecular Severo Ochoa (Consejo Superior de Investigaciones Científicas-Universidad Autónoma de Madrid), Universidad Autónoma de Madrid, Cantoblanco, 28049 Madrid, Spain

Received 29 June 2009/ Accepted 17 September 2009

The African swine fever virus (ASFV) protein pE248R, encoded by the gene E248R, is a late structural component of the virus particle. The protein contains intramolecular disulfide bonds and has been previously identified as a substrate of the ASFV-encoded redox system. Its amino acid sequence contains a putative myristoylation site and a hydrophobic transmembrane region near its carboxy terminus. We show here that the protein pE248R is myristoylated during infection and associates with the membrane fraction in infected cells, behaving as an integral membrane protein. Furthermore, the protein localizes at the inner envelope of the virus particles in the cytoplasmic factories. The function of the protein pE248R in ASFV replication was investigated by using a recombinant virus that inducibly expresses the gene E248R. Under repressive conditions, the ASFV polyproteins pp220 and pp62 are normally processed and virus particles with morphology indistinguishable from that of those produced in a wild-type infection or under permissive conditions are generated. Moreover, the mutant virus particles can exit the cell as does the parental virus. However, the infectivity of the pE248R-deficient virions was reduced at least 100-fold. An investigation of the defect of the mutant virus indicated that neither virus binding nor internalization was affected by the absence of the protein pE248R, but a cytopathic effect was not induced and early and late gene expression was impaired, indicating that the protein is required for some early postentry event.

* Corresponding author. Mailing address: Centro de Biología Molecular Severo Ochoa (CSIC-UAM), C/Nicolás Cabrera, 1, Universidad Autónoma de Madrid, 28049 Madrid, Spain. Phone: 34 91 196 44 67. Fax: 34 91 196 44 20. E-mail: mlsalas{at}cbm.uam.es

{triangledown} Published ahead of print on 30 September 2009.

Journal of Virology, December 2009, p. 12290-12300, Vol. 83, No. 23
0022-538X/09/$08.00+0     doi:10.1128/JVI.01333-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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