The pestivirus glycoprotein E rns , a ribonuclease, is expressed on the surface of virions and in infected cells as a disulfide-linked homodimer. E rns is involved in the infection process and its RNase activity is probably involved in viral replication and pathogenesis. The most C-terminal cysteine residue forms an intermolecular disulfide bond with another E rns monomer, resulting in an E rns dimer. To study the function of dimerisation of E rns for viral replication, the cysteine residue at amino acid position 438 was mutated into a serine residue. The mutated C438S gene was cloned into a vector containing an infectious cDNA copy of the CSFV C-strain genome. Using reverse genetics, a mutant virus was generated that only expressed monomeric E rns , confirming that Cys 438 is essential for homodimerisation. Characterization of this mutant virus and of a baculovirus-expressed C438S mutant protein indicated that the loss of the dimeric state of E rns reduced the affinity of binding of virions and E rns to heparan sulphate (HS), the receptor for E rns on the cell surface of SK6 cells. This suggests that interaction of virus-bound E rns homodimers with membrane associated HS may be a joined action of the two HS-binding domains (one in each monomer) present in the homodimer.
Archives of Virology – Springer Journals
Published: Nov 1, 2005
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