Construction and characterization of a camelized, human, VH-based peptide vaccine against CD20 antigen. (February 2013)

• Record Type: Journal Article
• Authors: Liu, Jianbin; Tan, Yanguo; Zhang, Ranxing
• Is Part Of: Immunotherapy. Volume 5:Number 2(2013:Feb.)
• Page Start: 135
• Page End: 141
• Publication Date: 2013-02
• Subjects: camelized human VH -- CD20 -- peptide vaccine -- single-domain antibody; Immunotherapy -- Periodicals; 615.37
• DOI: 10.2217/imt.12.152
• Languages: English
• ISSNs: 1750-743X

Abstract

Aim: The purpose of this study was to construct and characterize a camelized, human, heavy-chain variable (VH) fragment-based peptide vaccine against CD20 antigen.Materials & methods: Camelized, human VH with improved solubility and stability was used as a vaccine scaffold. A CD20 B-cell epitope was introduced into the complementarity determining region 3 of the engineered VH and a measles virus-derived T-helper epitope was grafted into the complementarity determining region 3. The chimeric VH fragment was synthesized in bacteria and purified for immunization of mice. The titers and antigen-binding specificity of the antibody elicited by the chimeric peptide vaccine were assessed in vitro .Results: Notably, the CD20 epitope within the chimeric VH peptide elicited high-titered anti-CD20 antibody. Besides binding to GST–CD20 fusion protein, the antibody was cross-reactive with the native CD20 antigen on Raji cells.Conclusion: In conclusion, the chimeric VH peptide vaccine consisting of the CD20 epitope can induce the production of the CD20-specific antibody, likely having potential implications in preventing CD20 overexpression cancers.