Novel monoclonal antibody that recognizes new neoantigenic determinant of D-dimer.
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 (Bbeta134-142) 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 BbetaLys133 residue to Gln133 thus it doesn't produce the particular N-terminal epitope of D134 approximately 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.
Doh
Hyun-Ju
HJ
BioBud Co. Ltd, 3F, Kyoungwon Bld., 132-42 Yonhui-dong, Seodaemun-ku, Seoul 120-110, Republic of Korea.
Song
Kyung-Soon
KS
Kang
Myung-Seo
MS
Kim
Doo-Sik
DS
Kim
Kyung-Ah
KA
Kang
Jemo
J
Jang
Yangsoo
Y
Chung
Kwang-Hoe
KH
D000911:Antibodies, Monoclonal / Q000737:chemistry* / Q000276:immunology*; D001665:Binding Sites; D018604:Epitope Mapping; D000939:Epitopes / Q000276:immunology*; D005338:Fibrin Fibrinogen Degradation Products / Q000737:chemistry* / Q000276:immunology*; D006801:Humans; D011485:Protein Binding
D000911:Antibodies, Monoclonal; D000939:Epitopes; D005338:Fibrin Fibrinogen Degradation Products; C036309:fibrin fragment D