Characterization of the African swine fever virion protein j18L

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Abstract
The African swine fever virus (ASFV) open reading frame (ORF) that is named j18L in the Malawi (LIL20/1) isolate and E199L in the Ba71V isolate encodes a cysteine rich protein of 195 amino acids with a predicted molecular mass of 21·7 kDa and a hydrophobic domain near the C terminus. There are several possible motifs for glycosylation, phosphorylation and myristoylation. Rabbit antisera and monoclonal antibodies raised against a recombinant ASFV j18L protein expressed as a fusion protein with glutathione S-transferase (GST) identified proteins of 19·0–20 kDa in cells infected with different ASFV strains and with a recombinant vaccinia virus expressing j18L. The monoclonal antibodies detected a protein of 20·0 kDa whereas rabbit antisera detected two proteins with relative molecular masses of 15·0 and 20·0 kDa in purified extracellular ASF virions. In ASFV-infected cells, the j18L protein was expressed late post-infection and was localized mainly in the viral factories.

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