Search of cellular protein(s) binding to the similar structure of HBV epsilon and HCV3'X
| Project/Area Number |
15590704
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (C)
|
| Allocation Type | Single-year Grants |
|---|
| Section | 一般 |
|---|
| Research Field |
Gastroenterology
|
|---|
| Research Institution | Japanese Foundation for Cancer Research |
|---|
Principal Investigator |
KAJINO Kazunori Japanese Foundation for Cancer Research, The JFCR Cancer Institute, Dept of Experimental Pathology, Associate, 癌研究所・実験病理部, 研究員 (80260066)
|
|---|
| Project Period (FY) |
2003 – 2004
|
| Project Status |
Completed (Fiscal Year 2004)
|
| Budget Amount *help |
¥3,500,000 (Direct Cost: ¥3,500,000)
Fiscal Year 2004: ¥1,300,000 (Direct Cost: ¥1,300,000)
Fiscal Year 2003: ¥2,200,000 (Direct Cost: ¥2,200,000)
|
|---|
| Keywords | hepatitis B virus / hepatitis C virus / RNA binding protein(s) / RNA結合蛋白 / HBV / HCV |
|---|
| Research Abstract |
The genomic structures and replication mechanisms of hepatitis B virus (HBV) and hepatitis C virus (HCV) are different, but these two viruses share the biological characteristics; Both 1) take the form of RNA as the replicative intermediates, 2) are hepatotropic. 3) are not directly cytopathic but cause the persistent inflammation of the liver, predisposing occurrence of hepatocellular carcinoma (HCC). Epsilon structure of HBV RNA and 3'X structure of HCV RNA are indispensable for the replication or packaging of these viruses. We reported the similar secondary structures containing the identical 7 bases in both structures, and hypothesized that the biological similarity attributes to this structural similarity. As one of the steps to verify the hypothesis, we searched the cellular protein(s) recognizing this common structure. By SDS-southwestern method, 110 kDa, 35 kDa, and 15 kDa proteins were bound by the RNA or DNA oligomeres taking the form of this common structure. Of these 3 proteins, that of 35 kDa showed the strongest binding signal. To identify these protein(s), we examined the binding activity of 600 thousand clones of lambda gt11 expression libraries constructed from HepG2 cDNA by southwestern method. We isolated 4 independent clones. One of them was ribosomal binding protein L5 which was 34 kDa and compatible to the expected size. We are also analyzing other 3 clones. Our future task is to study the effect of these proteins on the replication of HBV or HCV.
|
Report
(3 results)
Research Products
(5 results)
