Rubella virus (RV) virions contain, in addition to the RNA genome, a c
apsid protein (C) and two envelope glycoproteins (E1 and E2). The C pr
otein in isolated virions has been reported to be a disulfide-linked d
imer (C2). There are two cysteine residues (Cys-152 and Cys-196) withi
n the C protein. To define the role of disulfide-linked C2 dimer in vi
rion formation, site-directed mutagenesis was used to alter the Cys-15
2 residue to serine. The association of mutant C protein with envelope
glycoproteins was examined by transient expression of the cDNAs in CO
S cells. Mutation at the Cys-152 residue completely abolished the form
ation of C2 dimer. However, C2 dimerization does not appear to be impo
rtant for the assembly of RV structural proteins into virus-like parti
cles. (C) 1996 Academic Press, Inc.