Key result
An RNA gel mobility shift assay demonstrated a specific interaction between the 5' noncoding region of the hepatitis C virus genome and the recombinant core protein.
Demonstrates a specific in vitro interaction between the HCV 5'NCR RNA and core protein, suggesting a mechanism for viral genome encapsidation.
Does not alter clinical practice; leaves open whether core-5'NCR interaction drives HCV encapsidation in vivo.
Little is known about the molecular interactions required for hepatitis C virion assembly. The 5' noncoding region (5'NCR) of the RNA genome is highly conserved and has extensive secondary structure. The highly basic core protein is rich in arginine and lysine residues. We postulate that a specific interaction between these structures may be important for virion assembly. Using an RNA gel mobility shift assay, a specific interaction has been demonstrated between the RNA of the 5'NCR and recombinant core protein. Proteins from other regions of the virus do not interact with the viral RNA. The interaction is inhibited competitively by unlabelled sense polarity RNA, but antisense 5'NCR RNA and nonspecific RNAs compete only at much higher concentrations. These data suggest that there is a specific interaction between the 5'NCR of the hepatitis C virus (HCV) genome and HCV core protein. This interaction may be important for the specific encapsidation of the viral genome during HCV replication.
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Fan et al. (1999) studied Hepatitis C virus. Recombinant core protein and 5'NCR RNA vs. Proteins from other regions of the virus / antisense 5'NCR RNA / nonspecific RNAs was evaluated on Specific interaction between the RNA of the 5'NCR and recombinant core protein. An RNA gel mobility shift assay demonstrated a specific interaction between the 5' noncoding region of the hepatitis C virus genome and the recombinant core protein.
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