Rubella virus capsid protein (RUBV C)

The Rubella virus capsid protein is an essential structural component of the Rubella virus (RUBV), the sole member of the Rubivirus genus. Its primary role is to package the single-stranded, positive-sense RNA genome into a compact icosahedral nucleocapsid, which then associates with the viral envelope glycoproteins E1 and E2 for budding [1, 13]. The protein consists of a disordered N-terminal region responsible for RNA binding and a more structured C-terminal domain that facilitates dimerization and assembly [3, 5]. This structural domain exhibits a unique polypeptide fold not observed in related alphaviruses, highlighting its potential as a specific target for drug design [5, 6]. Beyond its structural function, the capsid protein acts as a multifunctional regulatory factor, modulating viral RNA replication through interactions with the viral replicase p150 and inhibiting host cell translation by binding to poly(A)-binding protein (PABP) [8, 12]. It also influences host cell survival and metabolism by interacting with proteins such as Bax to regulate apoptosis and p32 to reorganize mitochondria into perinuclear clusters [10, 17]. Rubella infection is primarily known for causing German measles and severe birth defects, termed congenital rubella syndrome (CRS), when contracted during pregnancy [5, 18]. While prevention is currently managed through the MMR vaccine, the capsid protein is an active target for the development of novel antiviral therapies, including small molecules like Rhizophorin, designed to disrupt its assembly and host-interaction domains [7, 11].

Other names

Coat proteinC proteinNucleocapsid proteinRubella virus C proteinCapsid protein

Inhibition of viral nucleocapsid assembly, disruption of viral RNA binding, and interference with host protein interactions such as p32 or poly(A)-binding protein (PABP) binding.