The hinge region fragment of immunoglobulin G improves immunogenicity of recombinant gonadotrophin-releasing hormone conjugated to the T-helper epitope in designing peptide vaccines

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Blackwell Science Inc

RESUMO

In our previous study, the hinge fragment (225–232/225′–232′) of human immunoglobulin G1 (IgG1) was used as a space peptide linker for synthesizing the GnRH3–hinge–MVP chimeric peptide, whereby three repeated gonadotrophin-releasing hormone (GnRH) units and a T-cell epitope from measles virus fusion protein (MVP) were amide-bond-linked at the N and C terminus, respectively, to the hinge peptide for producing anti-GnRH antibody responses. To investigate whether or not the hinge region fragment can improve the immunogenicity of GnRH, we further synthesized and purified GnRH3–hinge–MVP, GnRH3–hinge and GnRH3–MVP using recombinant DNA technology. Under high pH conditions, GnRH3–hinge–MVP was capable of forming double-chain structures. Immunization of male mice with the immunogens of GnRH3–hinge–MVP resulted in the generation of high-titre antibodies specific for GnRH. The synthetic GnRH3–hinge and GnRH3–MVP induced a lower titre of anti-GnRH antibody than GnRH3–hinge–MVP. This was followed by a decrease in serum testosterone levels, which resulted in a low level of expression of the relaxin-like factor gene in the testis. Our data suggest that peptide and T-cell epitopes oriented at the N-terminus or C-terminus of hinge peptides simplify the antigenic peptide conjugates and may be considered as potential synthetic immunogens.

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