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Title: N-linked Glycosylation of Classical Swine Fever Virus Strain Brescia Erns Glycoprotein Alters Virulence in Swine

Author
item FERNANDEZ-SAINZ, IGNACIO - ORISE, ARS, PIADC
item Holinka-Patterson, Lauren
item LU, ZHIQIANG - DHS, S&T, PIADC
item RISATTI, GUILLERMO - UNIV OF CONNECTICUT STORR
item Borca, Manuel

Submitted to: Positive Strand RNA Virus International Conference Proceedings
Publication Type: Abstract Only
Publication Acceptance Date: 5/24/2007
Publication Date: 5/26/2007
Citation: Fernandez-Sainz, I., Holinka, L.G., Lu, Z., Risatti, G.R., Borca, M.V. 2007. N-linked Glycosylation of Classical Swine Fever Virus Strain Brescia Erns Glycoprotein Alters Virulence in Swine. Eighth International Symposium on Positive Strand RNA Virus, P2-K26, P.116

Interpretive Summary:

Technical Abstract: Erns is one of the three envelope glycoproteins of Classical Swine Fever Virus (CSFV). We recently reported the influence of glycosylation of E2 in the virulence of CSFV strain Brescia. Here, we studied the effect of Erns N-linked glycosylation pattern on virulence of CSFV strain Brescia in swine. Seven putative Erns N-linked glycosylation sites (Asn-X-Ser/Thr) were modified by site directed mutagenesis (Asn to Gln) using an infectious clone of highly virulent CSFV strain Brescia (BICv). A panel of mutants was then used to investigate whether the removal of putative glycosylation sites in the Erns glycoprotein would affect viral virulence/pathogenesis in swine. Besides confirming the glycosylation status of putative sites in Erns, this mutational analysis showed that BICv virulence/pathogenesis in swine is affected significantly by the glycosylation pattern of Erns.