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10.18632/oncotarget.12167 http://scihub22266oqcxt.onion/10.18632/oncotarget.12167 C5342741!5342741 !27659529     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27659529 &cmd=llinks): Failed to open stream: HTTP request failed! 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Induction of anti-EGFR immune response with mimotopes identified from a phage display peptide library by panitumumab |pdf=|usr=}}{{27659529 }} gab.com Text Induction of anti-EGFR immune response with mimotopes identified from a phage display peptide library by panitumumab JO: Oncotarget http://www.kidney.de/pget.php?&tw=1&pmid=27659529 #FOAvip The epidermal growth factor receptor (EGFR) is overexpressed in several epithelial tumors. Anti-EGFR humanized monoclonal antibodies, cetuximab and panitumumab, in combination with chemotherapy have improved the prognosis for patients with wild-type RAS tumors. To identify mimotopes of EGFR and develop mimotope-based EGFR vaccines, we screened a phage display peptide library with panitumumab. Two EGFR mimotopes P19 and P26, which could be recognized by panitumumab specifically, were isolated. To enhance the immune responses, we generated recombinant proteins of P19 or P26 fused to a heat-shock cognate protein 70 (Hsc70), and evaluated the efficacy of Hsc70-P19 and Hsc70-P26 as vaccines in vivo. Immunization with Hsc70-P19 or Hsc70-P26 fusion protein stimulated the immune system to produce specific antibodies against peptides as well as EGFR. Moreover, antibodies elicited against mimotopes could induce antibody-dependent cellular cytotoxicity (ADCC), complement-dependent cytotoxicity (CDC), and inhibit the proliferation of EGFR-overexpressing A431 cells. Treatment with Hsc70-P19 and Hsc70-P26 significantly reduced tumor growth in BALB/c transplantable lung cancer models. Although there was no sequence homology between the phage-derived peptides and EGFR by alignments, both peptides mimic the conformational structure of EGFR binding to panitumumab. In conclusion, the mimotopes we identified from phage display peptide library could be promising candidate vaccines for active anti-EGFR immunotherapy against cancers. Twit Text FOAVip Induction of anti-EGFR immune response with mimotopes identified from a phage display peptide library by panitumumab ????Oncotarget http://www.kidney.de/pget.php?&tw=1&pmid=27659529 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27659529 #FOAvip English Wikipedia <ref>{{Cite pmid|27659529 }}</ref> Induction of anti-EGFR immune response with mimotopes identified from a phage display peptide library by panitumumab #MMPMID27659529 Wang A ; Cui M ; Qu H ; Di J ; Wang Z ; Xing J ; Wu F ; Wu W ; Wang X ; Shen L ; Jiang B ; Su X Oncotarget 2016[Nov]; 7 (46 ): 75293-75306 PMID27659529 show ga The epidermal growth factor receptor (EGFR) is overexpressed in several epithelial tumors. Anti-EGFR humanized monoclonal antibodies, cetuximab and panitumumab, in combination with chemotherapy have improved the prognosis for patients with wild-type RAS tumors. To identify mimotopes of EGFR and develop mimotope-based EGFR vaccines, we screened a phage display peptide library with panitumumab. Two EGFR mimotopes P19 and P26, which could be recognized by panitumumab specifically, were isolated. To enhance the immune responses, we generated recombinant proteins of P19 or P26 fused to a heat-shock cognate protein 70 (Hsc70), and evaluated the efficacy of Hsc70-P19 and Hsc70-P26 as vaccines in vivo. Immunization with Hsc70-P19 or Hsc70-P26 fusion protein stimulated the immune system to produce specific antibodies against peptides as well as EGFR. Moreover, antibodies elicited against mimotopes could induce antibody-dependent cellular cytotoxicity (ADCC), complement-dependent cytotoxicity (CDC), and inhibit the proliferation of EGFR-overexpressing A431 cells. Treatment with Hsc70-P19 and Hsc70-P26 significantly reduced tumor growth in BALB/c transplantable lung cancer models. Although there was no sequence homology between the phage-derived peptides and EGFR by alignments, both peptides mimic the conformational structure of EGFR binding to panitumumab. In conclusion, the mimotopes we identified from phage display peptide library could be promising candidate vaccines for active anti-EGFR immunotherapy against cancers. |*Cell Surface Display Techniques [MESH] |*Epitope Mapping/methods [MESH] |*Peptide Library [MESH] |Animals [MESH] |Antibodies, Monoclonal/*immunology/metabolism/pharmacology [MESH] |Antibody-Dependent Cell Cytotoxicity/immunology [MESH] |Cell Line, Tumor [MESH] |Cell Proliferation/drug effects [MESH] |Epitopes/chemistry/*immunology/metabolism [MESH] |ErbB Receptors/chemistry/*immunology/metabolism [MESH] |Humans [MESH] |Immunity, Cellular [MESH] |Mice [MESH] |Models, Molecular [MESH] |Panitumumab [MESH] |Peptides/chemistry/immunology/metabolism [MESH] |Protein Binding [MESH] |Protein Conformation [MESH] |Recombinant Fusion Proteins [MESH] |Signal Transduction/drug effects [MESH]Induction of anti-EGFR immune response with mimotopes identified from (epmc).pdf DeepDyve Pubget Overpricing