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1 BBSRC Institute for Animal Health, Pirbright Laboratory, Ash Road, Pirbright, Woking GU24 0NF
and2 Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK
The African swine fever virus (ASFV) j13L gene encodes a 177 amino acid protein (19.0 kDa) with a putative transmembrane domain between residues 32 and 52. There is a potential signal peptide cleavage site at residue 54 and several possible motifs for phosphorylation and myristylation. Rabbit antisera raised against a synthetic peptide from the C terminus of the j13L ORF identified proteins of 25–27 kDa in cells infected with a recombinant vaccinia virus expressing the j13L ORF, in ASFV-infected cells and in purified extracellular ASF virions. In ASFV-infected cells the j13L protein was expressed late during infection and exhibited size variation (25–27 kDa) between the different ASFV strains. Nucleotide sequence analysis of the gene in these strains showed that these size differences were due to variation in the number and sequence of tandemly repeated amino acid repeats. Although ASFV-infected animals made antibodies to the j13L protein, no protection was observed when pigs were vaccinated with a recombinant vaccinia virus expressing the j13L ORF.
* Author for correspondence. Fax +44 1483 232448. e-mail linda.dixon@BBSRC.ac.uk
Received 4 October 1994;
accepted 22 December 1994.
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