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. 1990 Aug;64(8):3563–3569. doi: 10.1128/jvi.64.8.3563-3569.1990

Pestivirus glycoprotein which induces neutralizing antibodies forms part of a disulfide-linked heterodimer.

E Weiland 1, R Stark 1, B Haas 1, T Rümenapf 1, G Meyers 1, H J Thiel 1
PMCID: PMC249648  PMID: 2370675

Abstract

Neutralizing monoclonal antibodies directed against hog cholera virus (HCV) precipitated two HCV-encoded glycoproteins, HCV gp55 and HCV gp33. Immunoassay with bacterial fusion proteins and Western immunoblotting with extracts from infected cells revealed that the antibodies recognized only HCV gp55. Coprecipitation of HCV gp33 was shown to be due to intermolecular disulfide bridges. One of the antibodies also reacted with the major glycoprotein of another pestivirus, bovine viral diarrhea virus (BVDV). The analogous BVDV glycoproteins exhibited a distribution of cysteine residues which was almost identical to that of HCV gp55 and gp33. The two BVDV glycoproteins were also linked by disulfide bridges.

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