%0 Journal Article %T Generation of fusion protein EGFRvIII-HBcAg and its anti-tumor effect in vivo %A Xiao-yi Duan %A Dong-gang Han %A Ming-xin Zhang %A Jian-sheng Wang %J Journal of Experimental & Clinical Cancer Research %D 2009 %I BioMed Central %R 10.1186/1756-9966-28-133 %X Epidermal growth factor receptor (EGFR) plays an important role in tumor cell proliferation, differentiation and survival. Increasing evidences suggest that alterations within the EGFR gene may be as important as EGFR-overexpression to induce oncogenic effects [1-3]. The most common variation is an in-frame deletion of exons 2-7 in the mRNA, resulting in a truncated mutant (epidermal growth factor receptor variant III, EGFRvIII). Even though EGFRvIII is lack of a portion of extracellular ligand-binding domain and can not bind to its ligand, the tyrosine kinase in the intracellular portion can be constitutively activated, thereby leading to receptor dimerization, autophosphorylation and stimulation of signal transduction cascades[4]. Because EGFRvIII is present with a high frequency in several different types of tumor and has not been detected in normal tissues, it is an ideal target for tumor specific therapy[5,6]. Among approaches directed to EGFRvIII, vaccine is a promising strategy.Recombinant protein has been intensively studied as a vaccine on the basis of genetic engineering technology. Compared with peptide vaccine, recombinant protein has many advantages such as easy manipulation, mass production and low cost. The carrier of foreign epitope is important for construction of recombinant protein. Hepatitis B core protein (HBcAg) is one of the most promising delivery vehicles for its high-density, immunogenic presentation of foreign epitope and its production in various expression systems[7]. The e1 loop in the main determinant of the core antigen is considered as the most promising insertion site[8].Pep-3, a 13-amino-acid peptide corresponding to the amino acid sequence of the EGFRvIII fusion junction (LEEKKGNYVVTDH), is an immunogenic peptide that was firstly reported by Moscatello[9]. In this study, foreign epitope, encoding Pep-3, was inserted into the immunodominant e1 loop of the HBcAg to prepare the recombinant fusion protein. Next, the antigenicity and i %U http://www.jeccr.com/content/28/1/133