A replicon trans-packaging system reveals the requirement of nonstructural proteins for the assembly of bovine viral diarrhea virus (BVDV) virion

Delin Liang, Limei Chen, Israrul H. Ansari, Laura H.V.G. Gil, Christina L. Topliff, Clayton L. Kelling, Ruben O. Donis

Research output: Contribution to journalArticle

5 Scopus citations

Abstract

A selective trans-packaging system was developed to produce and isolate bovine viral diarrhea virus (BVDV) pseudo-particles with complementing reporter replicons and their packaging proteins expressed in trans with recombinant vaccinia virus. The encapsidation of replicon rNS3-5B was dependent not only on the in trans expression of structural proteins C, Erns, E1 and E2, but also the nonstructural proteins, p7 and contiguous precursor NS2-3-4A. Nonstructural p7, NS4B, NS5A or NS5B could be expressed in cis and in trans with precursor NS2-3-4A without significantly affecting virion assembly efficiency. NS2-3-4A was identified as an in trans functional precursor in virion assembly. BVDV genomes with mutant NS5B, which did not undergo active replication, were packaged 5-fold less efficiently than the intact genomes demonstrating the importance of replication in virion packaging. These results suggest that genome replication and assembly are closely associated, consistent with a model in which these two steps are coupled for maximum efficiency.

Original languageEnglish (US)
Pages (from-to)331-340
Number of pages10
JournalVirology
Volume387
Issue number2
DOIs
StatePublished - May 10 2009

Keywords

  • BVDV
  • Complementation
  • NS2-3-4A precursor
  • Pseudo-particles
  • Replication
  • Trans-packaging
  • Virion assembly

ASJC Scopus subject areas

  • Virology

Fingerprint Dive into the research topics of 'A replicon trans-packaging system reveals the requirement of nonstructural proteins for the assembly of bovine viral diarrhea virus (BVDV) virion'. Together they form a unique fingerprint.

  • Cite this