Novel monoclonal antibody that recognizes new neoantigenic determinant of D-dimer

Hyun Ju Doh, Kyung Soon Song, Myung Seo Kang, Doo Sik Kim, Kyung Ah Kim, Jemo Kang, Yangsoo Jang, Kwang Hoe Chung

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)


Our novel monoclonal antibody (mAb) B4 reacted with only D-dimer but not intact fibrinogen, or fibrinogen degradation products (FgDP) such as D-monomer, E fragment on ELISA. B4 didn't react with denatured D-dimer, while it reacted well with denatured D-monomer rather than the native form, indicating that B4 recognizes some neoconformational epitope in D-dimer. In our epitope study, B4 recognized the N-terminal (Bβ134-142) of D-dimer, which corresponds to the most flexible segment of coiled coil backbone. It was confirmed by inhibition assay of B4 binding to D-dimer using the synthesized peptides with this sequence. As the other evidence, B4 didn't bind to some D-dimer species produced from a particular fibrinogen variant. This fibrinogen variant is mutated BβLys133 residue to Gln133 thus it doesn't produce the particular N-terminal epitope of D134∼ by plasmin. Finally, our mAb was useful for clinical application. ELISA using our mAbs was well correlated with other commercial D-dimer ELISAs and in some clinical samples it was preferable to them. These results suggest that the epitope for B4 is another neoantigenic determinant in native D-dimer as distinct from native D-monomer.

Original languageEnglish
Pages (from-to)353-360
Number of pages8
JournalThrombosis Research
Issue number3
Publication statusPublished - 2006

All Science Journal Classification (ASJC) codes

  • Hematology


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