The E.coli derived recombinant protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-192. The FLSCN labeled protein is fused with b-galactosidase (114 kDa) at N-terminus.
Hepatitis C Virus (HCV) is a significant global health concern, affecting millions of individuals worldwide. The virus is known for its ability to cause chronic liver diseases, including cirrhosis and hepatocellular carcinoma. The HCV particle contains a single-stranded positive-sense RNA genome that encodes a single polyprotein, which is further processed to generate multiple polypeptides, including structural and nonstructural proteins .
The core protein of HCV is a structural protein that plays a crucial role in the formation of the viral nucleocapsid. It is involved in various stages of the viral life cycle, including viral assembly, replication, and interaction with host cell factors . The core protein is approximately 22 kDa in size and is highly conserved among different HCV genotypes, making it an important target for diagnostic and therapeutic applications.
Recombinant HCV core proteins are produced using various expression systems to study their structure, function, and immunogenicity. The FLSCN (Full-Length Synthetic Core Nucleocapsid) recombinant HCV core protein is one such example. This recombinant protein is designed to mimic the native core protein of HCV, allowing researchers to investigate its properties in a controlled laboratory setting.
The production of recombinant HCV core proteins typically involves the use of bacterial, yeast, or mammalian expression systems. The gene encoding the core protein is cloned into an expression vector, which is then introduced into the host cells. The recombinant protein is expressed, harvested, and purified using various chromatographic techniques to ensure high purity and yield .
Recombinant HCV core proteins have several applications in research and clinical settings: