The NS5A protein of bovine viral diarrhoea virus interacts with the alpha subunit of translation elongation factor-1

A cellular protein that interacts with the NS5A polypeptide of bovine viral diarrhoea virus (BVDV) was identified in a yeast two-hybrid screen. The NS 5A interactor was identified as the oc subunit of bovine translation elonga tion factor 1A (eEF1A). Cell-free binding studies were performed with chime ric NS5A fused to glutathione S-transferase (GST-NS5A) expressed in bacteri a. GST-NS5A bound specifically to both in vitro-translated and mammalian ce ll-expressed eEF1A. Moreover, purified eEF1A bound specifically to GST-NS5A attached to a solid phase. Conservation of this interaction was then analy sed using a set of NS5A proteins derived from divergent BVDV strains encomp assing known biotypes and genotypes. NS5A from all BVDV strains tested so f ar interacted with eEF1A. The conserved association of eEF1A with virus mol ecules involved in genome replication and the postulated role of pestivirus and hepacivirus NS5A in replication indicate that this interaction may pla y a role in the replication of BVDV.