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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 
 Thrombosis Research, Vol.118(3) : 353-360, 2006 
Journal Title
 Thrombosis Research 
Issue Date
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.
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1. Journal Papers (연구논문) > 1. College of Medicine (의과대학) > Dept. of Internal Medicine (내과학교실)
1. Journal Papers (연구논문) > 1. College of Medicine (의과대학) > Dept. of Laboratory Medicine (진단검사의학교실)
Yonsei Authors
송경순(Song, Kyung Soon)
장양수(Jang, Yang Soo) ORCID logo https://orcid.org/0000-0002-2169-3112
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