1994 Fiscal Year Final Research Report Summary
Epitope domain and plasminogen activating site (s) in streptokinase molecule
Project/Area Number |
05670268
|
Research Category |
Grant-in-Aid for General Scientific Research (C)
|
Allocation Type | Single-year Grants |
Research Field |
Bacteriology (including Mycology)
|
Research Institution | Nippon Medical School |
Principal Investigator |
OHKUNI Hisashi Nippon Medical School Institute of Gerontology Professor, 老人病研究所, 教授 (60060365)
|
Co-Investigator(Kenkyū-buntansha) |
TODOME Yuko Nippon Medical School Institute of Gerontology Assistant Professor, 老人病研究所, 講師 (20089626)
|
Project Period (FY) |
1993 – 1994
|
Keywords | straptokinase / epitope / acute glomerulonephritis / plasminogen |
Research Abstract |
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).
|