Nonstructural proteins NS2-3 and NS4A of classical swine fever virus: essential features for infectious particle formation

Moulin, Hervé R; Seuberlich, Torsten; Bauhofer, Oliver; Bennett, Lea C; Tratschin, Jon-Duri; Hofmann, Martin A; Ruggli, Nicolas (2007). Nonstructural proteins NS2-3 and NS4A of classical swine fever virus: essential features for infectious particle formation. Virology, 365(2), pp. 376-89. New York, N.Y.: Academic Press 10.1016/j.virol.2007.03.056

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The nonstructural protein NS2-3 of pestiviruses undergoes tightly regulated processing. For bovine viral diarrhea virus it was shown that uncleaved NS2-3 is required for infectious particle formation while cleaved NS3 is essential for genome replication. To further investigate the functions of NS2-3 and NS4A in the pestivirus life cycle, we established T7 RNA polymerase-dependent trans-complementation for p7-NS2-3-4A of classical swine fever virus (CSFV). Expression of NS2-3 and NS4A in trans restored the production of infectious particles from genomes lacking NS2-3 expression. Co-expression of cleaved NS4A was essential. None of the enzymatic activities harbored by NS2-3 were required for infectious particle formation. Importantly, expression of uncleavable NS2-3 together with NS4A rescued infectious particles from a genome lacking NS2, demonstrating that cleaved NS2 per se has no additional essential function. These data indicate that NS2-3 and NS3, each in association with NS4A, have independent functions in the CSFV life cycle.

Item Type:

Journal Article (Original Article)

Division/Institute:

05 Veterinary Medicine > Department of Clinical Research and Veterinary Public Health (DCR-VPH) > Experimental Clinical Research

UniBE Contributor:

Seuberlich, Torsten

ISSN:

0042-6822

Publisher:

Academic Press

Language:

English

Submitter:

Factscience Import

Date Deposited:

04 Oct 2013 14:52

Last Modified:

21 Jan 2014 15:05

Publisher DOI:

10.1016/j.virol.2007.03.056

PubMed ID:

17482232

Web of Science ID:

000248985200014

URI:

https://boris.unibe.ch/id/eprint/22268 (FactScience: 33745)

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