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
