Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 26 nm in diameter, and consisting of 89 capsid proteins dimers (178 capsid proteins). Involved in viral genome encapsidation through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome. The capsid contains also 1 copy of the A2 maturation protein. Acts as a translational repressor of viral replicase synthesis late in infection. This latter function is the result of capsid protein interaction with an RNA hairpin which contains the replicase ribosome-binding site. Homodimer. The capsid proteins form dimers that assemble by group of 5. Twelve such pentamers are linked together with free dimers. The homodimers binds to the viral RNA via an operator hairpin, but also to many other RNA sequences in the viral genome; this interaction probably shifts the virus from the replicative to the assembly phase and ensures specific encapsidation of the viral genome. The shell is composed of 178 copies of the capsid protein and 1 copy of the maturation protein. Belongs to the Levivirus capsid protein family. Icosahedral capsid structure Icosahedral capsid structure