A simple method to purify recombinant HCV core protein expressed in Pichia pastoris for obtaining virus-like particles and producing monoclonal antibodies.

This study focuses on a simple method to purify recombinant hcv core protein expressed in pichia pastoris for obtaining virus-like particles and producing monoclonal antibodies.. The research employs high-performance liquid chromatography (HPLC) techniques to address analytical challenges in the biopharmaceutical field. In this study, we describe an optimized method of obtaining virus-like particles (VLPs) of the recombinant hepatitis C virus (HCV) core protein (HCcAg) expressed in yeast cells (Pichia pastoris), which can be used for the construction of diagnostic test systems and vaccine engineering. The described simplified procedure was developed to... Research Background and Significance Hepatitis C virus (HCV) remains a significant global health concern, with chronic infections leading to severe liver diseases, including cirrhosis and hepatocellular carcinoma. Recombinant expression of viral proteins, such as the HCV core antigen (HCcAg), is pivotal for developing diagnostic assays, virus-like particles (VLPs), and vaccine candidates. Pichia pastoris, a methylotrophic yeast, serves as an effective eukaryotic expression system due to its capacity for post-translational modifications and high-level protein production. However, purification of recombinant HCcAg from Pichia pastoris presents analytical challenges, including protein heterogeneity and contaminants derived from the host system. The study by Pechelyulko et al. (2021) addresses these challenges by developing a simplified and robust purification method using high-performance liquid chromatography (HPLC). This approach is critical for producing high-purity protein suitable for downstream applications, such as monoclonal antibody production and VLP assembly, which are essential for both diagnostic and vaccine