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Dimerization of glycoprotein E(rns) of classical swine fever virus is not essential for viral replication and infection.
- Source :
-
Archives of virology [Arch Virol] 2005 Nov; Vol. 150 (11), pp. 2271-86. Date of Electronic Publication: 2005 Jun 28. - Publication Year :
- 2005
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Abstract
- 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 homo-dimerization. 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.
- Subjects :
- Animals
Cell Line
Classical Swine Fever Virus genetics
Classical Swine Fever Virus pathogenicity
DNA Primers
Dimerization
Kidney
Molecular Sequence Data
Swine
Viral Envelope Proteins genetics
Viral Proteins isolation & purification
Viral Proteins metabolism
Classical Swine Fever virology
Classical Swine Fever Virus physiology
Viral Envelope Proteins metabolism
Virus Replication physiology
Subjects
Details
- Language :
- English
- ISSN :
- 0304-8608
- Volume :
- 150
- Issue :
- 11
- Database :
- MEDLINE
- Journal :
- Archives of virology
- Publication Type :
- Academic Journal
- Accession number :
- 15986175
- Full Text :
- https://doi.org/10.1007/s00705-005-0569-y