Evaluation of a novel Escherichia coli fusion system for the production of recombinant immunogenic proteins

Abstract

Recombinant protein production has been widely applied for therapeutic and diagnostic applications, namely for polyclonal antibody production. Antibodies are usually raised against a specific protein by immunisation of animals with the purified protein. The Escherichia coli host cell is widely used for the bioproduction of proteins with biomedical interest but some of them are still difficult to express properly in this host system, resulting in insoluble protein aggregates. Gene fusion technology has been employed to optimise recombinant protein production in E. coli. Fusion partners have also been used to increase protein immunogenicity. In this work, the immunopotentiating properties of a novel fusion partner (H partner) were studied. The H partner was fused to three target proteins with diagnostic interest: CP12, a 12 kDa surface protein from Cryptosporidium parvum oocysts; CWP, a cyst wall protein from Giardia lamblia; and ENT, a surface protein from Entamoeba histolytica trophozoites. The results obtained here show the H partner as a promising tool for immunodiagnostic and immunoprophylactic purposes.