ABSTRACT
Currently, the genus Pestivirus comprises four approved species, namely bovine viral diarrhoea viruses 1 and 2 (BVDV-1, BVDV-2), classical swine fever virus and border disease virus (BDV). Recently, three major genotypes have been identified within the species BDV and termed as subgroups BDV-1, BDV-2 and BDV-3. Here, an isolate from animals in a herd showing BD-like syndromes, which occurred in central Italy was analysed. A reverse transcriptase polymerase chain reaction was performed using primers that specifically amplify a fragment of the 5'-non-coding region (5'-NCR) from BDV. Both the 5'-NCR fragment and the entire Npro gene were sequenced and used for genetic typing. The 5'-NCR sequence revealed that the newly isolated Pestivirus could be allocated to the BDV species. Interestingly, the Npro sequence of this virus isolate significantly differed from all the ovine pestiviruses previously described, providing evidence for the presence of an additional subgroup within the species BDV.
Subject(s)
Border Disease/epidemiology , Border Disease/virology , Border disease virus/genetics , DNA, Viral/analysis , Disease Outbreaks/veterinary , Animals , Border disease virus/classification , Border disease virus/isolation & purification , Goats , Italy/epidemiology , Phylogeny , Reverse Transcriptase Polymerase Chain Reaction/veterinary , SheepABSTRACT
Shc proteins are targets of activated tyrosine kinases and have been implicated in the transmission of activation signals to Ras. Upon phosphorylation, Shc proteins form stable complexes with cellular tyrosine-phosphorylated proteins and with the Grb2 adaptor protein. Two Shc isoforms of 52 and 46 kDa have been characterized. They share a C-terminal SH2 domain, a proline- and glycine-rich region (collagen homologous region 1; CH1) and a N-terminal phospho-tyrosine binding domain (PTB). We report her ethe initial characterization of two Shc related human cDNAs: ShcB and ShcC. The ShcB and ShcC cDNAs code for proteins that are highly similar and share the same modular organization as Shc. PTB and SH2 domains of ShcB and ShcC have similar binding specificities in vitro and bind to activated EGFR in a phosphotyrosine-dependent manner. Based on these findings we propose to rename Shc as ShcA. Anti-ShcB and anti-ShcC antibodies recognize specific polypeptides of 52, 47 kDa (ShcB) and 54 kDa (ShcC) in mammalian cells. Since these two genes are predominantly expressed in specific brain tissues, these Shc family members may be involved in cell type-specific signaling, in the nervous system.
