The epidermal growth factor receptor (EGFR) is over-expressed in various human epithelial tumors usually due to the gene amplification. EGFR gene amplification in tumors frequently contain its rearrangements and among them, the most common extracellular domain mutation is receptor variant III, EGFRvIII (also known as de2-7EGFR or DEGFR). The molecular mass of EGFRvIII is approximately 145 kDa and this genetic change of tumor-specific mutation results from a deletion of 267 amino acids spanning exons 2-7 of the EGFR gene. These consequences make the variant EGFRvIII incapable of binding known ligand. It is expressed in a majority of patients with glioblastoma multiforme. And the evidence shows aberrant EGFRvIII signaling is important for driving tumor progression. FcαRI (Fc fragment of IgA receptor), also referred to FcalphaRI or CD89, is the most prominent and only human immunoglobulin A (IgA) Fc receptor that binds the heavy-chain constant region of IgA via two extracellular binding sites. This receptor is a transmembrane glycoprotein mapping at the chromosome 19q13.42 and belongs to the immunoglobulin (Ig) gene superfamily. FcαRI is expressed on the surface of blood myeloid cells, such as monocyte/macrophages, neutrophils, eosinophils, dendritic cells, and Kupffer cells, in which it mediates immunologic responses to pathogens. IgA plays an important role in immune protection. It interacts with IgA-opsonized targets and initiates a number of immunologic defense processes, for instance, phagocytosis, stimulation of the release of inflammatory mediators, and antibody-dependent cell-mediated cytotoxicity.