Genomic organization of the structural proteins of borna disease virus revealed by a cDNA clone encoding the 38-kDa protein

Abstract

Borna disease is a rare neurological disease of sheep and horses. The etiological agent, borna disease virus (BDV), has been shown to be an RNA virus but has not been characterized sufficiently to assign it to a virus family. Previous studies have shown that three BDV-specific proteins of 14, 24 and 38 to 39 kDa are found in infected animals and cell culture (Ludwig et al., 1988, Prog. Med. Virol. 35, 107-151). cDNA clones have been isolated that encode the 14- and 24-kDa proteins; using the nucleotide sequences from these clones additional cDNAs were isolated that contained a large open reading frame (ORF) corresponding to the 38-kDa protein. Monoclonal antibodies against the BDV 38- to 39-kDa protein recognized the protein product of the large ORF. The relative gene order of the three BDV proteins (5' 38, 14, and 24 kDa 3') can be deduced from cDNAs which include portions of both the 24- and 38-kDa ORFs. The abundance of these proteins in BDV-infected animals and cultured cells suggests that these proteins are structural components of the virus. Previously all BDV-specific mRNAs (10.5, 3.6, 2.1, and 0.85 kb) were thought to be organized as overlapping 3' coterminal RNAs. Oligonucleotide probes made to the nucleotide sequence of the cDNA that encodes the 38-kDa protein identified an additional BDV-specific mRNA of 1.4 kb. This 1.4-kb mRNA species partially overlaps with the 2.1-kb RNA but is not 3' coterminal.