2004 Fiscal Year Final Research Report Summary
Super catalytic antbodies against Infuenza virus
| Project/Area Number |
15560678
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (C)
|
| Allocation Type | Single-year Grants |
|---|
| Section | 一般 |
|---|
| Research Field |
Biofunction/Bioprocess
|
|---|
| Research Institution | Hiroshima Prefectural University |
|---|
Principal Investigator |
HIFUMI Emi Hiroshima Prefectural University, School of Bioresources, Assislant Professor, 生物資源学部, 助手 (90254606)
|
|---|
| Project Period (FY) |
2003 – 2004
|
| Keywords | Influenza / Antibody / Protease / Hemagglutinin(HA) |
|---|
| Research Abstract |
Super catalytic antibody possesses highly characteristic features so as to not only specially bind to the antigen but also enzymatically decompose the antigen. It has been desired to prepare the super catalytic antibody targeting the conservative region of crucial proteins of microorganism such as bacteria and viruses. In this study, a surface protein of influenza virus was targeted for this purpose. In the following, some interesting results obtained so far are briefly described.
1, In the surface protein, hemagglutinin, of influenza virus type HINT and H2N2 there two conserved regions (TGLRN and GITNKVNSVIEK). The two peptides were synthesized as a one linear or cyclic peptide as an immunogen. The peptides were conjugated with h-IgG for immunization. And two kinds of monoclonal antibodies were obtained by using cell fusion technique.
2, The mRNAs were extracted from the hybridomas secreting monoclonal antibodies for investigating the cDNA sequence of the monoclonal antibodies. The germline genes of the light chains of the two monoclonal antibodies belonged to 8-12 and the heavy chains to 3558.46.
3, By using the deduced amino acid sequence from the cDNA, the structural analysis of the monoclonal antibodies were conducted by a work station. I found the discrete amino acid sequence possessing the catalytic activity in the structures.
4, Based on the above results, the light and heavy chains were purified and isolated from the monoclonal antibodies. The peptidase activity tests of the light and heavy chains are being performed at the present time. The peptide substrate was cleaved by those antibody subunits.
|
