Multi-specific monoclonal antibody MsMab-2 recognizes IDH1-R132L and IDH2-R172M mutations

Satoshi Ogasawara, Mika Kato Kaneko, Yuta Tsujimoto, Xing Liu, Yukinari Kato

Research output: Contribution to journalArticlepeer-review

15 Citations (Scopus)

Abstract

Mutations of isocitrate dehydrogenase 1/2 (IDH1/2) produce oncometabolite R(-)-2-hydroxyglutarate in several tumors. Arginine 132 (R132) of IDH1 and arginine 172 (R172) of IDH2 are functionally important residues. Although MsMab-1 monoclonal antibody (MAb), which is multi-specific for mutated IDH1/2, has been established, MsMab-1 does not react with all IDH1/2 mutations. Herein, we immunized rats with IDH1-R132L peptide, and screened IDH1-R132L-reactive/ IDH1-wild-type non-reactive MAbs in enzyme-linked immunosorbent assay. Unexpectedly, the newly established MsMab-2 MAb recognized not only IDH1-R132L but also IDH2-R172M in Western blot analyses, neither of which was detected by MsMab-1. Taken together, the combination of MsMab-1 and MsMab-2 could be useful in diagnosis of mutated IDH1/2-bearing tumors.

Original languageEnglish
Pages (from-to)377-381
Number of pages5
JournalMonoclonal antibodies in immunodiagnosis and immunotherapy
Volume32
Issue number6
DOIs
Publication statusPublished - 2013 Dec 1

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

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