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Journal of Virology, January 2007, p. 924-933, Vol. 81, No. 2
0022-538X/07/$08.00+0     doi:10.1128/JVI.01824-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

N-Linked Glycosylation Status of Classical Swine Fever Virus Strain Brescia E2 Glycoprotein Influences Virulence in Swine{triangledown}

G. R. Risatti,2 L. G. Holinka,1 I. Fernandez Sainz,1 C. Carrillo,1,{dagger} Z. Lu,3 and M. V. Borca1*

Plum Island Animal Disease Center, ARS, USDA, Greenport, New York 11944,1 Department of Pathobiology and Veterinary Science, University of Connecticut, Storrs, Connecticut 06269,2 Plum Island Animal Disease Center, DHS, Greenport, New York 119443

Received 21 August 2006/ Accepted 26 October 2006

E2 is one of the three envelope glycoproteins of classical swine fever virus (CSFV). Previous studies indicate that E2 is involved in several functions, including virus attachment and entry to target cells, production of antibodies, induction of protective immune response in swine, and virulence. Here, we have investigated the role of E2 glycosylation of the highly virulent CSFV strain Brescia in infection of the natural host. Seven putative glycosylation sites in E2 were modified by site-directed mutagenesis of a CSFV Brescia infectious clone (BICv). A panel of virus mutants was obtained and used to investigate whether the removal of putative glycosylation sites in the E2 glycoprotein would affect viral virulence/pathogenesis in swine. We observed that rescue of viable virus was completely impaired by removal of all putative glycosylation sites in E2 but restored when mutation N185A reverted to wild-type asparagine produced viable virus that was attenuated in swine. Single mutations of each of the E2 glycosylation sites showed that amino acid N116 (N1v virus) was responsible for BICv attenuation. N1v efficiently protected swine from challenge with virulent BICv at 3 and 28 days postinfection, suggesting that glycosylation of E2 could be modified for development of classical swine fever live attenuated vaccines.

* Corresponding author. Mailing address: Plum Island Animal Disease Center, ARS, NAA, USDA, P.O. Box 848, Greenport, NY 11944-0848. Phone: (631) 323-3019. Fax: (631) 323-3006. E-mail: manuel.borca{at}ars.usda.gov.

{triangledown} Published ahead of print on 15 November 2006.

{dagger} Present address: Plum Island Animal Disease Center, APHIS, USDA, Greenport, NY 11944.

Journal of Virology, January 2007, p. 924-933, Vol. 81, No. 2
0022-538X/07/$08.00+0     doi:10.1128/JVI.01824-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Gallei, A., Blome, S., Gilgenbach, S., Tautz, N., Moennig, V., Becher, P. (2008). Cytopathogenicity of Classical Swine Fever Virus Correlates with Attenuation in the Natural Host. J. Virol. 82: 9717-9729 [Abstract] [Full Text]  


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