Binding of mAb II-5c to Aα20–78 fragment of fibrinogen inhibits a neoantigenic determinant exposure within Bβ126–135 site of a molecule
DOI:
https://doi.org/10.15407/dopovidi2014.05.149Keywords:
Bβ126–135 site of a molecule, fibrinogen, mAb II-5c, neoantigenic determinantAbstract
The influence of mAb II-5c, epitope of which was localized within Aα20–78 fragment of the E-region of fibrinogen molecule, on the exposure of mAb I-3c neoantigenic determinant at the transformation of fibrinogen to fibrin has been investigated. Using ELISA, SPR, and electrophoretic analysis, we have found that mAb II-5c inhibited the binding of mAb I-3c to fibrin, thrombin to fibrin, and thrombin cleavage of fibrinopeptide A from fibrinogen in fibrinogen + thrombin and X-fragment fibrinogen + thrombin systems. These data support our hypothesis that the thrombin-fibrinogen substrate complex is a trigger of the restructuring of a fibrinogen molecule at the transformation in fibrin, which is accompanied by the formation of neoantigenic determinants of mAb I-3c within Bβ126–135 site of a molecule.
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