Purification of the glycoprotein G from viral haemorrhagic septicaemia virus, a fish rhabdovirus, by lectin affinity chromatography.
A new method for the isolation of glycoprotein G from viral haemorrhagic septicaemia virus (VHSV), a fish rhabdovirus, was developed by using affinity chromatography with immobilized Concanavalin A (ConA). The glycoprotein G was isolated from detergent solubilized concentrated virions and from large-volume virion-free supernatants from VHSV infected cells (soluble form). The purity achieved was higher than 85%. The estimated recovery of the initial glycoprotein G present in the virions was between 20 and 50%. These glycoprotein G preparations showed the presence of about 30% of trimers by ultracentrifugation, reacted with antibodies to the phosphatidylserine binding domain (p2) in a pH-dependent manner by ELISA and bound phosphatidylserine in a pH-dependent manner by solid-phase binding assays. These data suggest that ConA purified glycoprotein G conserved most of its native properties and conformation.[1]References
- Purification of the glycoprotein G from viral haemorrhagic septicaemia virus, a fish rhabdovirus, by lectin affinity chromatography. Perez, L., Estepa, A., Coll, J.M. J. Virol. Methods (1998) [Pubmed]
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