Epitope domain and plasminogen activating site (s) in streptokinase molecule

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We have previously reported that a monoclonal antibody (mAb), N-59, prepared against streptokinase (SKase) from a group A,M type 12 streptococcal isolate (strain A374) from a patient with poststreptococcal glomerulonephritis (PSGN) recognized an epitope also present in SKase from a group C Streptococcus (strain H46A) which is not a PSGN isolate.However, another mAb, RU-1, prepared against SKase (nephritis strain-assiciated SKase, NSA-SKase) from strain A374 reacted only with the homologous SKase and not with common-SKase (C-SKase) from strain H46A.In addition, the complete amino acid sequence of the NSA-SKase of strain A374 was determined, and the epitope domain specific for RU-1 mAb reacted only with the NSA-SKase was localized to residues 164-236.Both pin technology and ELISA test were used to the determination of epitope domain involved in the internal region of NSA-SKase molecule reacted with RU-1 mAb. As the results, RU-1 mAb reacted with residues 177-185 (PSLKERYHL), and the minimum epitope domain, which reacts with RU-1 mAb, was residues 177-180 (PSLK).The other side, N-59 mAb reacted with almost all of SKase (C-SKase). The epitope domain of C-SKase reacted with N-59 mAb was analyzed. As the results, N-59 mAb recognized residues 324-332 (RDLYDPRDK) in C-SKase molecule, and the minimum epitope domain was residues 324-331 (RDLYDPRD).