Virus-like particles from Escherichia Coli-derived untagged papaya ringspot virus capsid protein purified by immobilized metal affinity chromatography enhance the antibody response against a soluble antigen.

摘要: There is a growing interest in using virus-like particles (VLPs) as scaffolds for the presentation of antigens choice to immune system. In this work, VLPs from papaya ringspot virus capsid protein expressed Escherichia coli were evaluated enhancers antibody response against soluble antigen. Interestingly, although lacks histidine tag, its purification by immobilized metal affinity chromatography was achieved. The formation demonstrated electron microscopy first time protein. enriched polyethylene glycol precipitation. Additionally, these chemically coupled green fluorescent order evaluate them antigen carriers; however, bioconjugate instability observed. Nonetheless, adjuvant effect on BALB/c mice evaluated, GFP antigen, resulting significant increase anti-GFP IgG response, particularly, IgG1 class, demonstrating that enhance chosen study.