IngentaConnect Asparaginase Display of Human Cholesteryl Ester Transfer Protein ...

Authors: Gaofu, Qi¹; Rongyue, Cao¹; Dan, Mao¹; Xiuyun, Zhao¹; Xuejun, Wang¹; Jie, Wu¹; Jingjing, Liu¹

Source: Protein and Peptide Letters, Volume 13, Number 2, February 2006 , pp. 149-154(6)

Publisher: Bentham Science Publishers

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.

Keywords: Asparaginase; CETP B cell epitope; tetanus toxin helper T cell epitope; atherosclerosis; vaccine

Document Type: Research article

DOI: 10.2174/092986606775101689

Affiliations: 1: Biopharmaceutical College, China Pharmaceutical University, Tongjiaxiang 24, Nanjing 210009, Jiangsu, P.R. China.

The full text electronic article is available for purchase. You will be able to download the full text electronic article after payment.

$55.10 plus tax Refund Policy

Asparaginase Display of Human Cholesteryl Ester Transfer Protein (CETP) B Cell Epitopes for Inducing High Titers of Anti-CETP Antibodies In Vivo