title: Recombinant pestivirus E2 glycoproteins prevent viral attachment to permissive and non permissive cells with different efficiency.
abstract: Bovine viral diarrhoea virus (BVDV) is an economically important animal pathogen, which like other pestiviruses has similar molecular biological features to hepaciviruses, including human Hepatitis C virus. The pestivirus E2 glycoproteins are the major target for virus-neutralising antibodies, as well as playing a role in receptor binding and host range restriction. In this study, recombinant E2 glycoproteins (rE2) derived from three different pestivirus species were examined for their inhibitory effects on pestivirus infectivity in cell culture. Histidine-tagged rE2 glycoproteins of BVDV type 2 strain 178003, BVDV type 1 strain Oregon C24V and CSFV strain Alfort 187 were produced in Spodoptera frugiperda insect cells and purified under native conditions. The ability of rE2 glycoprotein to inhibit the infection of permissive cells by both homologous and heterologous virus was compared, revealing that the inhibitory effects of rE2 glycoproteins correlated with the predicted similarity of the E2 structures in the recombinant protein and the test virus. This result suggests that the sequence and structure of E2 are likely to be involved in the host specificity of pestiviruses at their point of uptake into cells.
authors.affiliation: Virology Department, Animal Health and Veterinary Laboratories Agency (Weybridge), Addlestone, Surrey, KT15 3NB, UK; The Pirbright Institute, Ash Road, Pirbright, Woking GU24 0NF, Surrey, UK. Electronic address: amin.asfor@pirbright.ac.uk.
authors.forename: A S
authors.initials: AS
authors.lastname: Asfor
authors.affiliation: Virology Department, Animal Health and Veterinary Laboratories Agency (Weybridge), Addlestone, Surrey, KT15 3NB, UK.
authors.forename: P R
authors.initials: PR
authors.lastname: Wakeley
authors.affiliation: Virology Department, Animal Health and Veterinary Laboratories Agency (Weybridge), Addlestone, Surrey, KT15 3NB, UK.
authors.forename: T W
authors.initials: TW
authors.lastname: Drew
authors.affiliation: The Pirbright Institute, Ash Road, Pirbright, Woking GU24 0NF, Surrey, UK.
authors.forename: D J
authors.initials: DJ
authors.lastname: Paton
mesh_terms: D000818:Animals; D006023:Glycoproteins / Q000235:genetics / Q000378:metabolism*; D010576:Pestivirus / Q000187:drug effects* / Q000502:physiology*; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism*; D061987:Sf9 Cells; D018411:Spodoptera; D014759:Viral Envelope Proteins / Q000235:genetics / Q000378:metabolism*; D053585:Virus Attachment / Q000187:drug effects*
chemical_list: D006023:Glycoproteins; D011994:Recombinant Proteins; D014759:Viral Envelope Proteins
keywords: Dimer; E2 glycoprotein; Glycosylation; Pestivirus; Viral inhibition