Restoration of glycoprotein Erns dimerization via pseudoreversion partially restores virulence of classical swine fever virus

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The E2 glycoprotein of classical swine fever virus is a virulence determinant in swine.

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Identification of a novel virulence determinant within the E2 structural glycoprotein of classical swine fever virus.

Classical swine fever virus (CSFV) E2 glycoprotein contains a discrete epitope (TAVSPTTLR, residues 829-837 of CSFV polyprotein) recognized by monoclonal antibody (mAb) WH303, used to differentiate CSFV from related ruminant pestiviruses, Bovine Viral Diarrhea Virus (BVDV) and Border Disease Virus (BDV), that infect swine without causing disease. Progressive mutations were introduced into mAb W...

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Antibody responses of pigs to defined Erns fragments after infection with classical swine fever virus.

Antibody responses of pigs to defined Erns fragments, after classical swine fever virus (CSFV) infection, were studied by using an enzyme-linked immunosorbent assay (ELISA). Selection of various E(rns) fragments was based on an immunodominant Erns region encompassing three overlapping antigenic regions, amino acids 65 to 145 (Erns(aa)65-145) (AR1), 84 to 160 (Erns(aa)84-160) (AR2), and 109 to 2...

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N-linked glycosylation status of classical swine fever virus strain Brescia E2 glycoprotein influences virulence in swine.

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 ...

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Mutations in classical swine fever virus NS4B affect virulence in swine.

NS4B is one of the nonstructural proteins of classical swine fever virus (CSFV), the etiological agent of a severe, highly lethal disease of swine. Protein domain analysis of the predicted amino acid sequence of the NS4B protein of highly pathogenic CSFV strain Brescia (BICv) identified a putative Toll/interleukin-1 receptor (TIR)-like domain. This TIR-like motif harbors two conserved domains, ...

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ژورنال

عنوان ژورنال: Journal of General Virology

سال: 2018

ISSN: 0022-1317,1465-2099

DOI: 10.1099/jgv.0.000990