ArticleIranian journal of biotechnology2015
Expression and Purification of HCV Core and Core-E1E2 Proteins in Different Bacterial Strains.
Article in Iranian journal of biotechnology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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4 authors at 3 institutions in 1 country.
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Abstract
backgroundHepatitis C virus (HCV) is a main public health problem causing chronic liver infection and subsequently liver cirrhosis and lethal hepatocellular carcinoma (HCC). Vaccination based on HCV capsid proteins has attracted a special interest for prevention of viral infections. The core protein is a basic and evolutionary most conserved protein, which regulates the cellular processes related to viral replication and pathogenesis. The envelope E1 and E2 proteins involve in generation of the infectious particles, viral entry by binding to a host cell receptor, and modulation of the immune responses.
objectivesIn current study, the efficient generation of recombinant core and core- MATERIALS AND
methodsThe expression of HCV core and core-E1E2 proteins was performed using prokaryotic pET-28a and pQE-30 expression systems in BL21/ Rosetta, and M15 strains, respectively. The recombinant proteins were purified using affinity chromatography under native conditions and also reverse staining method. Finally, the levels of recombinant proteins were assessed by BCA kit and spectrophotometer.
resultsThe data showed a clear band of ~573 bp for HCV core and ~2238 bp for core-
conclusionsThis study is the first report for purification of HCV core and core-
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