Dimerization of rubella virus capsid protein is not required for virus particle formation.
Rubella virus (RV) virions contain, in addition to the RNA genome, a capsid protein (C) and two envelope glycoproteins (E1 and E2). The C protein in isolated virions has been reported to be a disulfide-linked dimer (C2). There are two cysteine residues (Cys-152 and Cys-196) within the C protein. To define the role of disulfide-linked C2 dimer in virion formation, site-directed mutagenesis was used to alter the Cys-152 residue to serine. The association of mutant C protein with envelope glycoproteins was examined by transient expression of the cDNAs in COS cells. Mutation at the Cys-152 residue completely abolished the formation of C2 dimer. However, C2 dimerization does not appear to be important for the assembly of RV structural proteins into virus-like particles.
Lee
J Y
JY
Department of Pathology, University of British Columbia, Vancouver, Canada.
Hwang
D
D
Gillam
S
S
D000818:Animals; D001483:Base Sequence; D001704:Biopolymers; D002213:Capsid / Q000502:physiology*; D002460:Cell Line; D003545:Cysteine / Q000502:physiology; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009838:Oligodeoxyribonucleotides; D011994:Recombinant Proteins / Q000235:genetics; D012412:Rubella virus / Q000235:genetics / Q000502:physiology*; D014758:Viral Core Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D019065:Virus Assembly / Q000502:physiology*
D001704:Biopolymers; D009838:Oligodeoxyribonucleotides; D011994:Recombinant Proteins; D014758:Viral Core Proteins; C074573:nucleocapsid protein (C), rubella virus; D003545:Cysteine