Elucidation of the critical epitope of an anti-EGFR monoclonal antibody EMab-134

Mika K. Kaneko, Shinji Yamada, Shunsuke Itai, Yao Wen Chang, Takuro Nakamura, Miyuki Yanaka, Yukinari Kato

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

The epidermal growth factor receptor (EGFR) is a type-1 transmembrane receptor tyrosine kinase, which activates the downstream signaling cascades in many tumors, such as oral and lung cancers. We previously developed EMab-134, a novel anti-EGFR monoclonal antibody (mAb), which reacts with endogenous EGFR-expressing cancer cell lines and normal cells independent of glycosylation in Western blotting, flow cytometry, and immunohistochemical analysis. EMab-134 showed very high sensitivity (94.7%) to oral squamous cell carcinomas in immunohistochemical analysis. In this study, we performed enzyme-linked immunosorbent assay (ELISA), flow cytometry, and immunohistochemical analysis to determine the epitope of EMab-134. A blocking peptide (375–394 amino acids of EGFR) neutralized the EMab-134 reaction against oral cancer cells in flow cytometry and immunohistochemistry. The minimum epitope of EMab-134 was found to be the 377-RGDSFTHTPP−386 sequence. Our findings can be applied for the production of more functional anti-EGFR mAbs that in turn can be used for antitumor treatments.

Original languageEnglish
Pages (from-to)54-57
Number of pages4
JournalBiochemistry and Biophysics Reports
Volume14
DOIs
Publication statusPublished - 2018 Jul

Keywords

  • EGFR
  • Epitope mapping
  • Monoclonal antibody
  • Oral cancer

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry

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