Rubella Capsid-C
Description
Core Domains
The Capsid-C dimer forms a left-handed β-barrel, with hydrophobic interactions stabilizing the dimer interface . Structural flexibility in the BH loop enables adaptive interactions during assembly .
Virus Assembly
-
Dimerization: Capsid-C forms disulfide-linked dimers critical for nucleocapsid assembly. Mutations disrupting Cys-153 or Cys-197 impair virion production .
-
Membrane Interaction: Binds detergent molecules at hydrophobic pockets, suggesting interaction with the E2 glycoprotein’s cytoplasmic domain during budding .
RNA Binding and Replication
-
Replicon Rescue: Enhances replication of wild-type and mutant rubella replicons, including those with deletions in the 5′ UTR or 3′ cis-acting elements .
-
RNA Silencing Suppression: Acts as a viral suppressor of RNA interference (VSR) by binding double-stranded RNA and inhibiting Dicer-mediated siRNA generation .
Host Interactions
-
Anti-Apoptotic Activity: Binds mitochondrial Bax protein, preventing cytochrome c release and caspase activation .
-
p32 Interaction: Associates with host protein p32 at mitochondria, potentially modulating apoptosis and nucleocapsid assembly .
Functional Domains
Significance in Antiviral Development
The Capsid-C’s unique structure and multifunctionality make it a promising therapeutic target:
-
Assembly Inhibitors: Targeting the BH loop or dimer interface could disrupt virion formation .
-
Anti-Apoptotic Blockers: Small molecules interfering with Capsid-C–Bax interactions may reduce viral persistence .
-
VSR Activity: Disrupting RNA silencing suppression could enhance host antiviral responses .
Product Specs
Product Science Overview
Rubella virus (RUBV) is a member of the genus Rubivirus within the family Matonaviridae . It is an enveloped, single-stranded RNA virus with a positive-sense genome. The virus is known for causing rubella, also known as German measles, which is generally a mild disease in children and adults but can lead to severe congenital defects if a pregnant woman is infected .
The recombinant rubella virus capsid protein (C protein) is a laboratory-produced version of the natural capsid protein. It is often expressed in systems such as Saccharomyces cerevisiae (yeast) to ensure high purity and yield . This recombinant protein is used in various research applications, including studies on the virus’s structure, function, and immune response .
The capsid protein is essential for the assembly and stability of the viral particle. It interacts with the viral RNA to form the nucleocapsid, which is then enveloped by the host cell membrane containing the E1 and E2 glycoproteins . The recombinant capsid protein retains these properties, making it a valuable tool for studying the virus’s biology.
The capsid protein is a significant antigen that elicits an immune response in infected individuals. Antibodies against the capsid protein are often used as markers of rubella infection and immunity . The recombinant capsid protein is used in diagnostic assays to detect rubella-specific antibodies .
