The class
Displaying CETP B cell epitopes on asparaginase induces high-titer anti-CETP antibodies lasting over eighteen weeks in mice (Protein Pept Lett 2006)
Original title: Asparaginase display of human cholesteryl ester transfer protein (CETP) B cell epitopes for inducing high titers of anti-CETP antibodies in vivo
Researchers built a recombinant chimeric enzyme, AnsB-TTP-CETPC, fusing asparaginase, a tetanus toxin helper T cell epitope, and a human CETP B cell epitope, expressed as a soluble protein in Escherichia coli with about 83% of native asparaginase's activity. Three immunization doses induced high-titer anti-CETP antibodies in mice, detectable by ELISA at a 1:12,800 dilution and confirmed specific by Western blot, that persisted for more than eighteen weeks. Displaying the CETP epitope on the asparaginase scaffold overcame its otherwise weak antigenicity and evoked a strong CETP-specific immune response, without causing pathological changes in mouse kidney tissue, positioning the construct as a candidate atherosclerosis vaccine.
Original abstract
The recombinant chimeric enzyme, AnsB-TTP-CETPC, comprising asparaginase, tetanus toxin helper T cell epitope and human CETP B cell epitope was expressed as a soluble protein in Escherichia coli. The purified chimeric enzyme exhibited approximate 83% activity of the native asparaginase. After immunization with three doses of chimeric enzyme, high titers of anti-CETP antibodies were induced and lasted more than eighteen weeks in mice, and could even be detected at a dilution of 1:12800 by normal ELISA assay. The specificity of anti-CETP antibody was verified by Western blot assay. After displaying on the surface of asparaginase, the weak antigenicity of CETP epitope was effectively overcome, there after a strong CETP-specific immune response was evoked in mice immunized with the chimeric enzyme. Histochemical analysis of mice kidney tissue showed that immunization with the chimeric enzyme did not cause any pathological changes in mice. Collectively, the chimeric enzyme may be further developed as a vaccine against atherosclerosis in the future.
Summary written by cetpinhibition.org from the published abstract; figures as published. Page updated 19 August 2026. Methods.